Swine Elisa Testing

Description: Description of target: Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6. ;Species reactivity: Pig | Swine;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 1.17 ng/mL

Description: Description of target: AM and PAMP are potent hypotensive and vasodilatator agents. ;Species reactivity: Pig | Swine;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 9.7 pg/mL

Description: Description of target: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. ;Species reactivity: Pig | Swine;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.39 pg/mL.

Description: Description of target: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins.;Species reactivity: Pig | Swine;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.078 ng/mL.

Description: Description of target: The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development. Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.;Species reactivity: Pig | Swine;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.156 ng/mL

Description: Description of target: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.;Species reactivity: Pig | Swine;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 3.9 pg/mL

Description: Description of target: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity.;Species reactivity: Pig | Swine;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 5.86 ng/mL

Description: Description of target: Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation. ;Species reactivity: Pig | Swine;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 7.81 ng/mL

Description: Description of target: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling.;Species reactivity: Pig | Swine;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 1.95 ng/mL

Description: Swine H1N1 Hemagglutinin Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups. This antibody is specific for the novel swine influenza Hemagglutinin and will not recognize the corresponding Hemagglutinin sequence from the seasonal H1N1 influenza (A/Brisbane/59/2007 (H1N1)).

Description: Swine H1N1 Hemagglutinin Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups. This antibody is specific for the novel swine influenza Hemagglutinin and will not recognize the corresponding Hemagglutinin sequence from the seasonal H1N1 influenza (A/Brisbane/59/2007 (H1N1)).

Description: Swine H1N1 Hemagglutinin peptide

Description: Swine H1N1 Hemagglutinin Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups.

Description: Swine H1N1 Hemagglutinin Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups.

Description: Swine H1N1 Hemagglutinin peptide