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Mu-driven transposition of recombinant mini-Mu unit DNA

Mu-driven transposition of recombinant mini-Mu unit DNA within the Corynebacterium glutamicum chromosome.

A dual-component Mu-transposition system was modified for the mixing/amplification of genes in Corynebacterium. The system consists of two varieties of plasmids: (i) a non-replicative integrative plasmid that accommodates the transposing mini-Mu(LR) unit bracketed by the L/R Mu ends or the mini-Mu(LER) unit, which moreover accommodates the enhancer component, E, and (ii) an integration helper plasmid that expresses the transposition issue genes for MuA and MuB.
Environment friendly transposition within the C. glutamicum chromosome (≈ 2 × 10-Four per cell) occurred primarily by the replicative pathway by way of cointegrate formation adopted by doable decision. Optimizing the E location within the mini-Mu unit considerably elevated the effectivity of Mu-driven intramolecular transposition-amplification in C. glutamicum in addition to in gram-negative micro organism.
The brand new C. glutamicum genome modification technique that was developed permits the resultant unbiased integration/amplification/fixation of goal genes at excessive copy numbers. After integration/amplification of the primary mini-Mu(LER) unit within the C. glutamicum chromosome, the E-element, which is bracketed by lox-like websites, is excised by Cre-mediated vogue, thereby fixing the truncated mini-Mu(LR) unit in its place for the following integration/ amplification of recent mini-Mu(LER) models. This technique was demonstrated utilizing the genes for the citrine and inexperienced fluorescent proteins, yECitrine and yEGFP, respectively.
postgenomeconsortium
postgenomeconsortium

Mouse anti VEGFR-3/Flt-4 (#1) (human)

101-M36 100ug
EUR 297.6

Mouse anti VEGFR-1/Flt-1-Biotin (#EWF) (human)

101-MBi28 50ug
EUR 297.6

VEGFR-1 / FLT-1 Antibody

abx239393-100ug 100 ug
EUR 577.2

VEGFR-1/FLT-1 antibody

E39-09393 100ug/100ul
EUR 225
Description: Available in various conjugation types.

VEGFR-1/FLT-1 antibody

CAF50629-100ug 100ug
EUR 312

Anti-Mouse VEGFR-1/Flt-1 Antibody

103-M31 100 µg
EUR 399
Description: Vascular Endothelial Growth Factor (VEGF or VEGF-A) family members are major mediators of vasculogenesis and angiogenesis. Specifically, biological activities attributed to VEGFs include: mitogenic activity on endothelial cells, increased permeability of endothelial cells to proteins, stimulation of monocyte migration across endothelial cells and angiogenic activity. Three VEGF family receptors have been described: Flt-1 (fms-like tyrosine kinase) also known as VEGF R1, KDR (kinase-insert domain-containing receptor) also known as Flk-1 and VEGF R2, and Flt-4 also known as VEGF R3. The three receptors contain seven extracellular immunoglobulin-like domains and share substantial sequence homology. In addition, neuropilin-1, a neuronal receptor, also acts as a co-receptor for VEGF when expressed on vascular endothelial cells, endothelial cell progenitors and monocytes. VEGF R1 is expressed primarily on endothelial cells but is also found on human peripheral blood monocytes. Through its endothelial mitogenic and hyperpermeability activities, VEGF influences a variety of immune functions related to wound healing and blood protein traffic across endothelial barriers.

Mouse anti VEGFR-3/Flt-4-Biotin (#1) (human)

101-MBi36 50ug
EUR 297.6

Recombinant Human FLT-1/VEGFR-1 Protein

RP01137 50μg
EUR 308.75

Rabbit anti VEGFR-3/Flt-4 (human)

102-PA22AG 50ug
EUR 240

Rabbit anti VEGFR-3/Flt-4 (human)

102-PA22S 100ug
EUR 240

Anti-Human VEGFR-1/Flt-1 (Peptide), soluble Antibody

102-PA21S 100 µg
EUR 126
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Rabbit Anti-Human VEGFR-1 Flt-1 (Peptide), soluble

102-PA21 100ug
EUR 240

Active Recombinant Human FLT-1/VEGFR-1 Protein

RP01188 5 μg
EUR 32.5

Human FLT-1/VEGFR-1 Control/blocking peptide #1

FLT11-P 100 ug
EUR 196.8

Anti-Hu/Mo VEGFR-1/Flt-1, Antagonistic Antibody

mV1004.1m-h-m 100 µg
EUR 645.75
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The antibody will bind near the ligand binding site of the receptor and has antagonistic activity by blocking the binding of natural ligands.

Biotinylated Recombinant Human FLT-1/VEGFR-1 Protein

RP02100 500μg
EUR 2843.75

Rabbit Anti-human FLT-1/VEGFR-1 IgG #1, aff pure

FLT11-A 100 ul
EUR 578.4

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein

S01-011 5 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein

S01-012 20 µg
EUR 157.5
Description: Recombinat human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein containing amino acid residues. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein

S01-013 5 µg
EUR 103.95
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein

S01-014 20 µg
EUR 199.5
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein

S01-015 5 µg
EUR 103.95
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein

S01-016 20 µg
EUR 199.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein

S01-009 5 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor precursor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein

S01-010 20 µg
EUR 157.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis binding VEGF with the same affinity as the full-length receptor.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M37 100 µg
EUR 199.5
Description: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk 1) and VEGFR-3 (FLT-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domains and kinase insert domains in their intracellular regions. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. These receptors play essential roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 24 aa residue signal peptide. Mature VEGFR-3 is composed of a 751 aa residue extracellular domain, a 22 aa residue transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF-C and VEGF-D have been shown to bind and activate VEGF R3 (Flt-4). The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stage of development. It is important for lymphangiogenesis.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M38 100 µg
EUR 399
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M870 100 µg
EUR 399
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

102-PA22 200 µg
EUR 147
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

102-PABi22 50 µg
EUR 157.5
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Human VEGFR-1/Flt-1 (D3)-His, soluble Recombinant Protein

S01-080 50 µg
EUR 378
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure

FLT12-M 100 ug
EUR 578.4

Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure

FLT14-M 100 ug
EUR 578.4

VEGFR-3/Flt-4

JP27779 96
EUR 611

Anti-Mouse VEGFR-3/FLT-4 Antibody

103-M36 100 µg
EUR 246.75
Description: VEGFR-3, also known as FLT4, is a member of the Tyr protein kinase family. The extracellular portion of VEGFR-3 contains 7 immunoglobulin (Ig)-like domains and the cytoplasmic portion contains a protein kinase domain. FLT4 regulates angiogenesis and lymphangiogenesis, its ligands are VEGF-C and D and its binding is mediated by the 2nd and 3rd Ig-like domains of FLT4. During fetal development VEGFR-3 is expressed on endothelial cells, however, in the adult mice, the vascular endothelial cells lose VEGFR-3 expression, but the lymphatic endothelium expresses it constitutively. In addition, VEGFR-3 expression can be induced in tumors with active angiogenesis.

Anti-Mouse VEGFR-3/FLT-4 Antibody

103-M38 100 µg
EUR 399
Description: Receptor tyrosine kinase VEGFR-3, also known as Flt-4, together with VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remaining linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Human VEGFR-3 / Flt-4 GENLISA ELISA

KBH0215 1 x 96 wells
EUR 286

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-005 10 µg
EUR 57.75
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-006 50 µg
EUR 168
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Rabbit Anti-Mouse FLT-1/VEGFR-1 (279-299aa) IgG, aff pure

FLT15-A 100 ul
EUR 578.4

Human VEGFR-3/FLT-4/Fc Chimera, soluble

SFC-010 50ug
EUR 378

Rabbit Anti-Mouse FLT-4/VEGFR-3 IgG #1, aff pure

FLT41-A 100 ug
EUR 578.4

Active Recombinant Human VEGFR-3/FLT-4 Protein

RP00123 10 μg
EUR 175.5

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-017 10 µg
EUR 103.95
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-017S 5 µg
EUR 63
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-018 50 µg
EUR 210
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

FLT-1/VEGFR1 Human, Antibody

GWB-BE9645 0.1 mg Ask for price

Rat Monoclonal anti-Mouse VEGFR-3 (FLT-4) Antibody

xAP-0836 100ug
EUR 280

Mouse FLT-4/VEGFR-3 Control/blocking peptide #1

FLT41-P 100 ug
EUR 196.8

Human FLT-4/VEGFR-3 control/blocking peptide #2

FLT42-P 100 ug
EUR 196.8

Rabbit Anti-Human FLT-4/VEGFR-3 IgG #2, aff pure

FLT42-A 100 ug
EUR 578.4

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-M05 10 µg
EUR 57.75
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-M06 50 µg
EUR 168
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Human VEGFR1/Flt-1 ELISA KIT

E42EH-249 96T/48T Ask for price

Human VEGFR-1/Flt1 ELISA Kit

EHV0045 96Tests
EUR 625.2

Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein

SFC-009 10 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-3/Fc is a disulfide-linked homodimeric protein. The sVEGFR-3/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3/FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The FLT-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial at latter stages of development. It is important for lymphangiogenesis.

VEGFR-1/Flt1/ Rat VEGFR- 1/ Flt1 ELISA Kit

ELA-E0147r 96 Tests
EUR 1063.2

Anti-VEGFR-1/FLT-1 antibody

PAab09393 100 ug
EUR 426

FLT-1/ VEGFR1 AB1

GWB-91AE5A 0.5 ml Ask for price

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC040659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405S conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC040659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405S conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC810658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC810658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC810659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC810659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC940659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF594 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC940659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF594 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC880659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF488A conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC880659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF488A conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC800658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC800658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC800659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC800659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC430658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF543 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC430658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF543 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC430659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF543 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC430659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF543 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC400659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF640R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC400659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF640R conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC050658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF405M conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC050658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF405M conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC050659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405M conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC050659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405M conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC470659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF647 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC470659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF647 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC550658-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF555 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/658) Antibody

BNC550658-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF555 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC550659-100 100uL
EUR 238.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF555 conjugate, Concentration: 0.1mg/mL

VEGFR1 / Flt-1(FLT1/659) Antibody

BNC550659-500 500uL
EUR 652.8
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF555 conjugate, Concentration: 0.1mg/mL

Outcomes of cytomegalovirus DNA viral hundreds expressed in copies per millilitre and worldwide models per millilitre are equal.

Quantification of Cytomegalovirus (CMV) DNA is required for the initiation and monitoring of anti-viral remedy and the detection of viral resistance. Nonetheless, because of the lack of standardisation of CMV DNA nucleic acid checks, it’s troublesome to set common thresholds. In 2010, the 1st WHO Worldwide Normal for Human Cytomegalovirus for Nucleic Acid Amplification Strategies was launched. Since then CMV DNA viral load assays have been calibrated utilizing this normal.
Three exterior high quality evaluation (EQA) suppliers despatched the identical 5 samples to their contributors and analysed the outcomes to find out the equivalence of reporting CMV DNA leads to worldwide models per millilitre (IU/mL), and in contrast the distinction in outcomes reported in IU/mL with these reported in copies per millilitre (c/mL), and to find out the speed of adoption of IU/mL. About 78% of contributors proceed to report leads to c/mL although six of the 12 industrial assays are calibrated towards the usual.
The vary of the outcomes reported in IU/mL was lower than these reported in c/mL indicating that the adoption of the WHO normal efficiently improved the reporting of the CMV viral load.
The variation in particular person pattern outcomes reported by completely different assays, no matter whether or not in IU/mL or c/mL, continues to be nice and subsequently extra standardisation of the assays is required to permit the setting of remedy and monitoring thresholds. This research can act as a bench mark to find out price of future adoption if reporting CMV DNA viral load leads to IU/mL.

S1 satellite tv for pc DNA repetitive models show equivalent construction and total variability in all Anatolian brown frog taxa.

S1 satellite tv for pc DNA from Palearctic brown frogs has a species-specific construction in all European species. We characterised S1 satellite tv for pc DNA from the Anatolian brown frogs Rana macrocnemis, R. camerani, and R. holtzi as a way to outline their taxonomic rank and the construction of this satellite tv for pc on this frog lineage. Southern blots of genomic DNA digested with KpnI, EcoRV, NdeI, NheI, or StuI produced the identical sample of satellite tv for pc DNA bands. Furthermore, quantitative dot blots confirmed that this satellite tv for pc DNA accounts for 0.1 % of the genome in all taxa.
  • Evaluation of the general genomic variability of the S1a repeat sequence in specimens from numerous populations demonstrated that this repetitive unit additionally has the identical dimension (476 bp), the identical most typical sequence (MCS) and the identical total variability in all three taxa, and in addition in R. macrocnemis tavasensis.
  • The S1a repetitive unit presents three deletions of 9, eight and 1 bp in comparison with the 494-bp S1a repeat from European frogs. The S1a MCS has three variable positions (sequence WWTK in positions 183-186), because of the presence of two repeat subpopulations with motifs AATG and WWTT in all taxa. In contrast to beforehand analyzed mitochondrial and nuclear sequences that present appreciable variations amongst these taxa, no distinction could possibly be detected within the construction and variability of the S1 satellite tv for pc repetitive models.
  • This implies that these taxa ought to belong to a single species. Our outcomes point out that this satellite tv for pc DNA selection most likely shaped when the Anatolian lineage radiated from widespread ancestor about Four mya, and since then has maintained its construction in all 4 taxa examined.

Human CellExp? DKK-1, Human Recombinant

7132-10 each
EUR 333.6

Human CellExp? DKK-1, Human Recombinant

7132-50 each
EUR 1358.4

DKK-1 (HEK293-expressed), Human

HY-P7155A 50ug
EUR 1011.6

human Dkk-1 Recombinant Protein

100-407 10 µg
EUR 196.35
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.

human Dkk-1 Recombinant Protein

100-407S 2 µg
EUR 92.4
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.

Human Dkk-1 Recombinant Protein

200-013 20 µg
EUR 136.5
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.

Human Dkk-1 Recombinant Protein

200-013S 5 µg
EUR 92.4
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.

Recombinant Human DKK-1 Protein

PROTO94907-3 10ug
EUR 380.4
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.

Dkk-1

GT30000 50 ug
EUR 631.2

Human DKK Antibody

E63C02401 100ug/100ul
EUR 225
Description: Available in various conjugation types.

Human DKK-1 PicoKine ELISA Kit

EK0867 96 wells
EUR 510
Description: For quantitative detection of human DKK1 in cell culture supernates, cell lysates, serum and plasma (heparin, EDTA).

Active Recombinant Human Dkk-1 Protein

RP01343 100μg
EUR 162.5

Human DKK-1 Recombinant Protein Lyophilized

IHUDKK1RLY2UG each
EUR 341
Description: Human DKK-1 Recombinant Protein Lyophilized

Human DKK-1 ELISA kit (4×96T)

LF-EK50798 4×96T
EUR 2641.2

Nori® Human DKK-1 ELISA Kit

GR106268 96-well
EUR 461

DKK-1 Antibody

F51803-0.4ML 0.4 ml
EUR 322.15
Description: DKK-1 is a protein that is a member of the dickkopf family. It is a secreted protein with two cysteine rich regions and is involved in embryonic development through its inhibition of the WNT signaling pathway. Elevated levels of DKK-1 in bone marrow plasma and peripheral blood is associated with the presence of osteolytic bone lesions in patients with multiple myeloma.

OKRC00363-96W - Dkk-1 ELISA Kit (Human)

OKRC00363-96W 96Wells
EUR 525

OKAG00221-96W - Dkk-1 ELISA Kit (Human)

OKAG00221-96W 1plate:12x8-WellMicrostrips
EUR 475

Human DKK Antibody-HRP

E63C02402 100ug/100ul
EUR 275
Description: Available in various conjugation types.

DKK-3 ELISA KIT|Human

EF000091 96 Tests
EUR 826.8

Human DKK Antibody-BIOTIN

E63C02403 100ug/100ul
EUR 275
Description: Available in various conjugation types.

Recombinant Human DKK1/Dkk-1 Protein (His Tag)

PKSH033697-10ug 10ug
EUR 178
Description: Human

Recombinant Human DKK1/Dkk-1 Protein (His Tag)

PKSH033697-50ug 50ug
EUR 523
Description: Human

human Dkk-3 Recombinant Protein

100-408 10 µg
EUR 196.35
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-l1 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains.  Playing an important regulatory role in vertebrate development through localized inhibition of Wnt regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-3 has been shown to potentiate, rather than inhibit, Wnt signaling through interactions with the high-affinity, transmembrane coreceptors Kremen-1 (Krm1) and Kremen-2 (Krm2). Recombinant human DKK-3 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 36.3 kDa and contains 329 amino acid residues. Due to glycosylation, human DKK-3 migrates at an apparent molecular weight of approximately 39-49 kDa by SDS-PAGE analysis under non-reducing conditions.

human Dkk-3 Recombinant Protein

100-408S 2 µg
EUR 92.4
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-l1 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains.  Playing an important regulatory role in vertebrate development through localized inhibition of Wnt regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-3 has been shown to potentiate, rather than inhibit, Wnt signaling through interactions with the high-affinity, transmembrane coreceptors Kremen-1 (Krm1) and Kremen-2 (Krm2). Recombinant human DKK-3 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 36.3 kDa and contains 329 amino acid residues. Due to glycosylation, human DKK-3 migrates at an apparent molecular weight of approximately 39-49 kDa by SDS-PAGE analysis under non-reducing conditions.

human Dkk-2 Recombinant Protein

100-436 10 µg
EUR 196.35
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 25.8 kDa and contains 234 amino acid residues. Due to glycosylation, human DKK-2 migrates at an apparent molecular weight of approximately 31-36 kDa by SDS-PAGE analysis under non-reducing conditions.

human Dkk-2 Recombinant Protein

100-436S 2 µg
EUR 92.4
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 25.8 kDa and contains 234 amino acid residues. Due to glycosylation, human DKK-2 migrates at an apparent molecular weight of approximately 31-36 kDa by SDS-PAGE analysis under non-reducing conditions.

Human Dkk-2 Recombinant Protein

200-014 20 µg
EUR 136.5
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 fused to a C terminal His-tag derived from E. coli has a molecular weight of 26.0 kDa and contains 234 amino acid residues.

Human Dkk-2 Recombinant Protein

200-014S 5 µg
EUR 92.4
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 fused to a C terminal His-tag derived from E. coli has a molecular weight of 26.0 kDa and contains 234 amino acid residues.

Recombinant Human Dkk-3 Protein

RP00209 10 μg
EUR 97.5

Recombinant Human Dkk-3 Protein

RP00355 10 μg
EUR 196.8

Anti-Human Dkk-1 Antibody

102-PA33 200 µg
EUR 204.75
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.

Anti-Human Dkk-1 Antibody

102-PA33S 100 µg
EUR 126
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.

Anti-Human Dkk-1 Antibody

101-M380 100 µg
EUR 399
Description: Dkk1 is a Dickkopf-related protein that inhibits Wnt signaling by binding the Wnt coreceptor LRP5/6. It also binds Kremen1 and Kremen2. Dkk1 is important in embryonic development.

Anti-Human Dkk-1 Antibody

101-M426 100 µg
EUR 399
Description: Dkk1 is a Dickkopf-related protein that inhibits Wnt signaling by binding the Wnt coreceptor LRP5/6. It also binds Kremen1 and Kremen2. Dkk1 is important in embryonic development.

Human Dkk-1 Protein, Fc Tag (MALS verified)

DK1-H5258 1mg
EUR 310.3
Description: Human Dkk-1, Fc Tag (DK1-H5258) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # NP_036374.1).

Dkk-1 ELISA Kit (Human) : 96 Wells (OKAG00221)

OKAG00221 96 Wells
EUR 715.2
Description: Description of target: This gene encodes a protein that is a member of the dickkopf family. It is a secreted protein with two cysteine rich regions and is involved in embryonic development through its inhibition of the WNT signaling pathway. Elevated levels of DKK1 in bone marrow plasma and peripheral blood is associated with the presence of osteolytic bone lesions in patients with multiple myeloma.;Species reactivity: Human;Application: ELISA;Assay info: Quantitative Colorimentric Sandwich ELISA;Sensitivity: 63 pg/mL

Human Dkk-1 Protein, His Tag, premium grade

DK1-H5221 1mg
EUR 139.1
Description: Human Dkk-1 Protein, His Tag, premium grade (DK1-H5221) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # NP_036374.1).

Biotinylated Human Dkk-1 Protein, Fc,Avitag™

DK1-H82F5 25ug
EUR 1487.3
Description: Biotinylated Human Dkk-1, Fc,Avitag (DK1-H82F5) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # O94907-1).

Human DKK-1(Dickkopf-related protein 1) ELISA Kit

EH0113 96T
EUR 628.92
Description: Method of detection: Double Antibody, Sandwich ELISA;Reacts with: Homo sapiens;Sensitivity: 18.75pg/ml

Human DKK-1(Dickkopf-related protein 1) ELISA Kit

EKF57029-48T 48T
EUR 396.9

Human DKK-1(Dickkopf-related protein 1) ELISA Kit

EKF57029-5x96T 5x96T
EUR 2693.25

Human DKK-1(Dickkopf-related protein 1) ELISA Kit

EKF57029-96T 96T
EUR 567

Rabbit Anti Human DKK PcAb

E61C02403 100ug
EUR 225
Description: Available in various conjugation types.

Rabbit Anti Human DKK PcAb

E61C02403a 1mg
EUR 1125
Description: Available in various conjugation types.

Dkk-1 Rabbit pAb

E2251891 100ul
EUR 225
Description: Available in various conjugation types.

Recombinant Human DKK-1/DKK1 Protein, 8* His Tag

E40KMH986 20ug
EUR 495

Human DKK-2 Protein, His Tag

DK2-H5323 1mg
EUR 224.7
Description: Human DKK-2 Protein, His Tag (DK2-H5323) is expressed from CHO cells. It contains AA Lys 34 - Ile 259 (Accession # Q9UBU2).

Recombinant Human DKK1/Dkk-1 Protein (His Tag)(Active)

PKSH031807-100ug 100ug
EUR 636
Description: Human

Recombinant Human DKK1/Dkk-1 Protein (His Tag)(Active)

PKSH031807-20ug 20ug
EUR 303
Description: Human

Human DKK-4 PicoKine ELISA Kit

EK0868 96 wells
EUR 546
Description: For Quantitative Detection of human DKK-4 in cell culture supernates, serum and plasma(heparin, EDTA).

Human DKK-3 PicoKine ELISA Kit

EK1323 96 wells
EUR 510
Description: For quantitative detection of human DKK-3 in cell culture supernates, cell lysates, serum and plasma (heparin, EDTA).

Dkk-1 Polyclonal Antibody

41928-100ul 100ul
EUR 302.4

Dkk-1 Polyclonal Antibody

41928-50ul 50ul
EUR 224.4

DKK-1 Recombinant Protein

40-225-0002mg 0.002 mg
EUR 311.1
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.

DKK-1 Recombinant Protein

40-225-001mg 0.01 mg
EUR 437.1
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.

Dkk-1 Polyclonal Antibody

E041928 100μg/100μl
EUR 255
Description: Available in various conjugation types.

Dkk-1 Polyclonal Antibody

E20-75562 100ug
EUR 225
Description: Available in various conjugation types.

Dkk-1 Polyclonal Antibody

ABP53293-003ml 0.03ml
EUR 189.6
Description: A polyclonal antibody for detection of Dkk-1 from Human, Mouse, Rat. This Dkk-1 antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human Dkk-1

Dkk-1 Polyclonal Antibody

ABP53293-01ml 0.1ml
EUR 346.8
Description: A polyclonal antibody for detection of Dkk-1 from Human, Mouse, Rat. This Dkk-1 antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human Dkk-1

Dkk-1 Polyclonal Antibody

ABP53293-02ml 0.2ml
EUR 496.8
Description: A polyclonal antibody for detection of Dkk-1 from Human, Mouse, Rat. This Dkk-1 antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human Dkk-1

Dkk-1 Recombinant Protein

96-861 0.1 mg
EUR 651.3
Description: Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via beta-catenin mediated Pdgfralpha and E-cadherin expression.

Dkk-1 Recombinant Protein

96-990 0.05 mg
EUR 714.3
Description: Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via beta-catenin mediated Pdgfralpha and E-cadherin expression.

Dkk-1 Polyclonal Antibody

E44H07004 100ul
EUR 255
Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

DKK-3 ELISA Kit (Human) (OKBB00603)

OKBB00603 96 Wells
EUR 606
Description: Description of target: Dickkopf-related protein 3 is a protein that in humans is encoded by the DKK3 gene. This gene encodes a protein that is a member of the dickkopf family. It is mapped to 11p15.3. The secreted protein contains two cysteine rich regions and is involved in embryonic development through its interactions with the Wnt signaling pathway. The expression of this gene is decreased in a variety of cancer cell lines and it may function as a tumor suppressor gene. Members of the Dkk-related family display unique patterns of mRNA expression in human and mouse tissues, and are secreted when expressed in 293T cells. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease.;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: <= 10 pg/mL

Nori® Human DKK-1 ELISA Kit (2 plates)

GR106268-2 2 x 96-well
EUR 832

Dkk-2

GT15222 100 ug
EUR 631.2

Human DKK-2 Recombinant Protein Lyophilized

IHUDKK2RLY2UG each
EUR 317
Description: Human DKK-2 Recombinant Protein Lyophilized

Human DKK-3 Recombinant Protein Lyophilized

IHUDKK3RLY2UG each
EUR 317
Description: Human DKK-3 Recombinant Protein Lyophilized

Mouse Monoclonal anti-human Dkk-1

hAP-0246 100ug
EUR 250

Mouse Monoclonal anti-human Dkk-1

hAP-0246A 100ug
EUR 250

Sheep Polyclonal anti-Human Dkk-1

hAP-5846 50ug
EUR 400

Biotinylated Recombinant Human Dkk-3 Protein

RP02554 100μg
EUR 1423.5

Recombinant Human Dickkopf-Related Protein 1/DKK-1 (C-Fc)

PKSH034024-10ug 10ug
EUR 100
Description: Human

Recombinant Human Dickkopf-Related Protein 1/DKK-1 (C-Fc)

PKSH034024-50ug 50ug
EUR 300
Description: Human

Human Dkk-3 (R335G) Protein, His Tag

DK3-H5220 20ug
EUR 460.1
Description: Human Dkk-3 (R335G), His Tag (DK3-H5220) is expressed from human 293 cells (HEK293). It contains AA Ala 22 - Ile 350 (Accession # Q9UBP4-1 (R335G)).

DKK 1 Recombinant Protein

96-236 0.1 mg
EUR 752.1
Description: Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via β-catenin mediated Pdgfrα and E-cadherin expression.

DKK 1 Recombinant Protein

96-237 0.025 mg
EUR 619.8
Description: Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via β-catenin mediated Pdgfrα and E-cadherin expression.

Rat DKK-1 ELISA Kit

EK5668 96 tests
EUR 599

Mouse Dkk-1 ELISA Kit

E28L0661 96T
EUR 666.67

Mouse Dkk-1 ELISA KIT

E42EM-173 96T/48T Ask for price

OKRC00364-96W - Dkk-3 ELISA Kit (Human)

OKRC00364-96W 96Wells
EUR 525

OKRC00365-96W - Dkk-4 ELISA Kit (Human)

OKRC00365-96W 96Wells
EUR 525

OKBB00603-96W - DKK-3 ELISA Kit (Human)

OKBB00603-96W 96Wells
EUR 538

DKK-1 (CHO-expressed), Mouse

HY-P7154 50ug
EUR 914.4

Dkk-1 Rabbit Polyclonal Antibody

ES4292-100ul 100ul
EUR 124
Description: A Rabbit Polyclonal antibody against Dkk-1 from Human/Mouse/Rat. This antibody is tested and validated for WB, ELISA, IHC, WB, ELISA

Dkk-1 Rabbit Polyclonal Antibody

ES4292-50ul 50ul
EUR 74
Description: A Rabbit Polyclonal antibody against Dkk-1 from Human/Mouse/Rat. This antibody is tested and validated for WB, ELISA, IHC, WB, ELISA

Recombinant Human DKK-3/DKK3 Protein, His Tag

E40KMH988 20ug
EUR 495