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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-Human VEGFR-1/Flt-1
MBS690355-01mg 0.1mg
EUR 450

Mouse Anti-Human VEGFR-1/Flt-1
MBS690355-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1
MBS690361-01mg 0.1mg
EUR 450

Mouse Anti-Human VEGFR-1/Flt-1
MBS690361-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1
MBS690384-005mg 0.05mg
EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690384-5x005mg 5x0.05mg
EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1
MBS690483-005mg 0.05mg
EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690483-5x005mg 5x0.05mg
EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1
MBS690832-01mg 0.1mg
EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690832-5x01mg 5x0.1mg
EUR 1645

Anti-Human VEGFR-1/Flt-1 Antibody
101-MBi24 50 µg
EUR 246.75
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.

Anti-Human VEGFR-1/Flt-1 Antibody
101-MBi30 50 µg
EUR 189
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.

Anti-Human VEGFR-1/Flt-1 Antibody
102-PA20 200 µg
EUR 173.25
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.

Anti-Human VEGFR-1/Flt-1 Antibody
102-PABi20 50 µg
EUR 157.5
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.

anti- VEGFR-1/FLT-1 antibody
FNab09393 100µg
EUR 606.3
Description: Antibody raised against VEGFR-1/FLT-1

Mouse anti VEGFR-1/Flt-1-Biotin (#EWF) (human)
101-MBi28 50ug
EUR 297.6

Human VEGFR-1/Flt-1 (D5), soluble
MBS691664-002mg 0.02mg
EUR 380

Human VEGFR-1/Flt-1 (D5), soluble
MBS691664-5x002mg 5x0.02mg
EUR 1410

Human VEGFR-1/Flt-1 (D5), soluble
MBS691669-0005mg 0.005mg
EUR 265

Human VEGFR-1/Flt-1 (D5), soluble
MBS691669-5x0005mg 5x0.005mg
EUR 890

Human VEGFR-1/Flt-1 (D3), soluble
MBS691717-002mg 0.02mg
EUR 450

Human VEGFR-1/Flt-1 (D3), soluble
MBS691717-5x002mg 5x0.02mg
EUR 1725

Human VEGFR-1/Flt-1 (D4), soluble
MBS691847-0005mg 0.005mg
EUR 310

Human VEGFR-1/Flt-1 (D4), soluble
MBS691847-5x0005mg 5x0.005mg
EUR 1110

Human VEGFR-1/Flt-1 (D3), soluble
MBS692000-0005mg 0.005mg
EUR 310

Human VEGFR-1/Flt-1 (D3), soluble
MBS692000-5x0005mg 5x0.005mg
EUR 1110

Human VEGFR-1/Flt-1 (D4), soluble
MBS692119-002mg 0.02mg
EUR 450

Human VEGFR-1/Flt-1 (D4), soluble
MBS692119-5x002mg 5x0.02mg
EUR 1725

Human VEGFR-1/Flt-1 (native), soluble
MBS691505-0005mg 0.005mg
EUR 265

Human VEGFR-1/Flt-1 (native), soluble
MBS691505-5x0005mg 5x0.005mg
EUR 890

Human VEGFR-1/Flt-1 (native), soluble
MBS691991-002mg 0.02mg
EUR 380

Human VEGFR-1/Flt-1 (native), soluble
MBS691991-5x002mg 5x0.02mg
EUR 1410

Mouse anti VEGFR-3/Flt-4-Biotin (#1) (human)
101-MBi36 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.

Recombinant Human FLT-1/VEGFR-1 Protein
RP01137 50μg
EUR 308.75

Recombinant Human FLT-1/VEGFR-1 Protein
RP02099 100μg
EUR 205.47

Human VEGFR-1/Flt-1 (D3)-His, soluble
MBS692528-005mg 0.05mg
EUR 725

Human VEGFR-1/Flt-1 (D3)-His, soluble
MBS692528-5x005mg 5x0.05mg
EUR 2965

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-3/FLT-4 (#1) Antibody
MBS4158541-01mg 0.1mg
EUR 920

Anti-Human VEGFR-3/FLT-4 (#1) Antibody
MBS4158541-5x01mg 5x0.1mg
EUR 3880

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

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691483-005mg 0.05mg
EUR 395

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691483-5x005mg 5x0.05mg
EUR 1490

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691782-001mg 0.01mg
EUR 245

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691782-5x001mg 5x0.01mg
EUR 805

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

Biotinylated Recombinant Human FLT-1/VEGFR-1 Protein
RP02100 500μg
EUR 2843.75

Anti-Human VEGFR-l/Flt-1 (#EWC) Antibody
MBS4158536-01mg 0.1mg
EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWC) Antibody
MBS4158536-5x01mg 5x0.1mg
EUR 3880

Anti-Human VEGFR-l/Flt-1 (#EIC) Antibody
MBS4158537-01mg 0.1mg
EUR 920

Anti-Human VEGFR-l/Flt-1 (#EIC) Antibody
MBS4158537-5x01mg 5x0.1mg
EUR 3880

Anti-Human VEGFR-l/Flt-1 (#EWF) Antibody
MBS4158538-01mg 0.1mg
EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWF) Antibody
MBS4158538-5x01mg 5x0.1mg
EUR 3880

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.

Rabbit Anti-human FLT-1/VEGFR-1 IgG #1, aff pure
FLT11-A 100 ul
EUR 578.4

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.

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.

Human VEGFR-3/FLT-4, soluble
MBS691602-001mg 0.01mg
EUR 310

Human VEGFR-3/FLT-4, soluble
MBS691602-5x001mg 5x0.01mg
EUR 1110

Human VEGFR-3/FLT-4, soluble
MBS691970-005mg 0.05mg
EUR 465

Human VEGFR-3/FLT-4, soluble
MBS691970-5x005mg 5x0.05mg
EUR 1805

Human VEGFR-3/FLT-4, soluble
MBS692181-0005mg 0.005mg
EUR 250

Human VEGFR-3/FLT-4, soluble
MBS692181-5x0005mg 5x0.005mg
EUR 835

Anti-Human VEGFR-l/Flt-1 (#EWF) Biotin Antibody
MBS4158553-005mg 0.05mg
EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWF) Biotin Antibody
MBS4158553-5x005mg 5x0.05mg
EUR 3880

Anti-Human VEGFR-3/FLT-4 (CL 1) Biotin Antibody
MBS4158555-005mg 0.05mg
EUR 920

Anti-Human VEGFR-3/FLT-4 (CL 1) Biotin Antibody
MBS4158555-5x005mg 5x0.05mg
EUR 3880

Mouse Anti-Human VEGFR-3/FLT-4
MBS690017-01mg 0.1mg
EUR 450

Mouse Anti-Human VEGFR-3/FLT-4
MBS690017-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human VEGFR-3/FLT-4
MBS690153-01mg 0.1mg
EUR 450

Mouse Anti-Human VEGFR-3/FLT-4
MBS690153-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human VEGFR-3/FLT-4
MBS690532-005mg 0.05mg
EUR 450

Mouse Anti-Human VEGFR-3/FLT-4
MBS690532-5x005mg 5x0.05mg
EUR 1725

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.

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

Human Dkk-1 ELISA KIT
E42EH-269 96T/48T Ask for price

Human Dkk-1 ELISA Kit
E28L0566 96T
EUR 666.67

Human DKK-1 ELISA Kit
EK5390 96 tests
EUR 599

Human DKK-1 ELISA KIT
EF000090 96tests
EUR 566

Human Dkk-1 ELISA Kit
GWB-SKR221 96 Tests Ask for price

Human DKK-1 ELISA kit
LF-EK50797 1×96T
EUR 777.6

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.

Human Dkk-3
MBS691794-0002mg 0.002mg
EUR 300

Human Dkk-3
MBS691794-001mg 0.01mg
EUR 450

Human Dkk-3
MBS691794-5x001mg 5x0.01mg
EUR 1725

Human Dkk-2
MBS692245-0002mg 0.002mg
EUR 300

Human Dkk-2
MBS692245-001mg 0.01mg
EUR 450

Human Dkk-2
MBS692245-5x001mg 5x0.01mg
EUR 1725

Human Dkk-2
MBS692272-0005mg 0.005mg
EUR 250

Human Dkk-2
MBS692272-002mg 0.02mg
EUR 360

Human Dkk-2
MBS692272-5x002mg 5x0.02mg
EUR 1325

Dkk-1 (Human) LumiAb ELISA Kit
MBS9510975-10x96StripWells 10x96-Strip-Wells
EUR 4355

Dkk-1 (Human) LumiAb ELISA Kit
MBS9510975-5x96StripWells 5x96-Strip-Wells
EUR 2225

Dkk-1 (Human) LumiAb ELISA Kit
MBS9510975-96StripWells 96-Strip-Wells
EUR 500

Dkk-1 (Human) Sandwich ELISA Kit
OK-0326 1Kit
EUR 280
Description: Dkk-1 (Human) Colorimetric Sandwich ELISA Kit

Dkk-1 (Human) OmniKine ELISA Kit
MBS9502047-1x96Wells 1x96Wells
EUR 500

Dkk-1 (Human) OmniKine ELISA Kit
MBS9502047-5x96Wells 5x96Wells
EUR 2300

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).

Human DKK-1 PicoKine ELISA Kit
MBS176546-5x96StripWells 5x96-Strip-Wells
EUR 2755

Human DKK-1 PicoKine ELISA Kit
MBS176546-96StripWells 96-Strip-Wells
EUR 600

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

Human DKK Antibody
MBS857428-01mg 0.1mg
EUR 305

Human DKK Antibody
MBS857428-01mLAF405L 0.1mL(AF405L)
EUR 465

Human DKK Antibody
MBS857428-01mLAF405S 0.1mL(AF405S)
EUR 465

Human DKK Antibody
MBS857428-01mLAF610 0.1mL(AF610)
EUR 465

Human DKK Antibody
MBS857428-01mLAF635 0.1mL(AF635)
EUR 465

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 Recombinant Protein Lyophilized
MBS8431839-INQUIRE INQUIRE Ask for price

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
GT30000 50 ug
EUR 631.2

Dkk-1
MBS555901-005mg 0.05mg
EUR 610

Dkk-1
MBS555901-5x005mg 5x0.05mg
EUR 2590

OKAG00221-96W - Dkk-1 ELISA Kit (Human)
OKAG00221-96W 1plate:12x8-WellMicrostrips
EUR 475

OKRC00363-96W - Dkk-1 ELISA Kit (Human)
OKRC00363-96W 96Wells
EUR 525

Dkk-1, 32-266aa, Human, His tag, Baculovirus
MBS203274-001mg 0.01mg
EUR 375

Dkk-1, 32-266aa, Human, His tag, Baculovirus
MBS203274-005mg 0.05mg
EUR 1265

Dkk-1, 32-266aa, Human, His tag, Baculovirus
MBS203274-5x005mg 5x0.05mg
EUR 5460

Human DKK Antibody-HRP
E63C02402 100ug/100ul
EUR 275
Description: Available in various conjugation types.

Human DKK Antibody-HRP
MBS857208-01mg 0.1mg
EUR 345

Human DKK Antibody-HRP
MBS857208-5x01mg 5x0.1mg
EUR 1410

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

Recombinant Human DKK1 / Dkk-1 Protein (His tag)
MBS2546459-002mg 0.02mg
EUR 315

Recombinant Human DKK1 / Dkk-1 Protein (His tag)
MBS2546459-01mg 0.1mg
EUR 605

Recombinant Human DKK1 / Dkk-1 Protein (His tag)
MBS2546459-5x01mg 5x0.1mg
EUR 2715

Recombinant Human DKK1/Dkk-1 Protein (N-His)
MBS2557306-001mg 0.01mg
EUR 220

Recombinant Human DKK1/Dkk-1 Protein (N-His)
MBS2557306-005mg 0.05mg
EUR 505

Recombinant Human DKK1/Dkk-1 Protein (N-His)
MBS2557306-5x005mg 5x0.05mg
EUR 2270

Human DKK-3 ELISA KIT
EF000091 96tests
EUR 566

Mouse anti Human DKK1/Dkk-1 Monoclonal Antibody
MBS2543267-006mL 0.06mL
EUR 250

Mouse anti Human DKK1/Dkk-1 Monoclonal Antibody
MBS2543267-012mL 0.12mL
EUR 370

Mouse anti Human DKK1/Dkk-1 Monoclonal Antibody
MBS2543267-02mL 0.2mL
EUR 550

Human DKK Antibody-BIOTIN
E63C02403 100ug/100ul
EUR 275
Description: Available in various conjugation types.

Human DKK Antibody-BIOTIN
MBS857030-01mg 0.1mg
EUR 345

Human DKK Antibody-BIOTIN
MBS857030-5x01mg 5x0.1mg
EUR 1410

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

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

Sunlong Medical™ Human Dkk-1 ELISA Kit
EL0258Hu-48T 48T
EUR 398

Sunlong Medical™ Human Dkk-1 ELISA Kit
EL0258Hu-96T 96T
EUR 655

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).

Human Dkk-1 Protein, His Tag, premium grade
DK1-H5221-100ug 100ug
EUR 228.9
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).

Human Dkk-1 Protein, His Tag, premium grade
DK1-H5221-1mg 1mg
EUR 1384.3
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).

Human Dkk-1 Protein, His Tag, premium grade
DK1-H5221-20ug 20ug
EUR 141.7
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).

Human Dickkopf Related Protein 1, DKK-1 ELISA Kit
MBS1608151-10x96StripWells 10x96-Strip-Wells
EUR 3375

Human Dickkopf Related Protein 1, DKK-1 ELISA Kit
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Human Dickkopf Related Protein 1, DKK-1 ELISA Kit
MBS1608151-5x96StripWells 5x96-Strip-Wells
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