Goat Vascular Endothelial Growth Factor ELISA Kit | VEGF elisa kit

Goat Vascular Endothelial Growth Factor ELISA Kit

Cat. Num. AAA744035

• Gene Names: VEGFA; VPF; VEGF; MVCD1
• Reactivity: Goat
• Synonyms: Vascular Endothelial Growth Factor; Goat Vascular Endothelial Growth Factor ELISA Kit; VEGF elisa kit

• Reactivity: Goat
• Specificity: This assay has high sensitivity and excellent specificity for detection of VEGF. No significant cross-reactivity or interference between VEGF and analogues was observed. NOTE: Limited by current skills and knowledge, it is impossible for us to complete the cross-reactivity detection between VEGF and all the analogues, therefore, cross reaction may still exist in some cases.

• Samples: Serum, plasma, cell culture supernatants, body fluid and tissue homogenate
• Assay Type: Quantitative Competitive
• Sensitivity: 1.0 pg/mL
• Preparation and Storage: Store all reagents at 2-8 degree C

Typical Testing Data/Standard Curve (for reference only)

Related Product Information for VEGF elisa kit

Intended Uses: This VEGF ELISA kit is a 1.5 hour solid-phase ELISA designed for the quantitative determination of Goat VEGF. This ELISA kit for research use only, not for therapeutic or test applications!

Principle of the Assay: VEGF ELISA kit applies the competitive enzyme immunoassay technique utilizing a polyclonal anti-VEGF antibody and an VEGF-HRP conjugate. The assay sample and buffer are incubated together with VEGF-HRP conjugate in pre-coated plate for one hour. After the incubation period, the wells are decanted and washed five times. The wells are then incubated with a substrate for HRP enzyme. The product of the enzyme-substrate reaction forms a blue colored complex. Finally, a stop solution is added to stop the reaction, which will then turn the solution yellow. The intensity of color is measured spectrophotometrically at 450nm in a microplate reader. The intensity of the color is inversely proportional to the VEGF concentration since VEGF from samples and VEGF-HRP conjugate compete for the anti-VEGF antibody binding site. Since the number of sites is limited, as more sites are occupied by VEGF from the sample, fewer sites are left to bind VEGF-HRP conjugate. A standard curve is plotted relating the intensity of the color (O.D.) to the concentration of standards. The VEGF concentration in each sample is interpolated from this standard curve.

Product Categories/Family for VEGF elisa kit

Cancer

NCBI and Uniprot Product Information

• NCBI GI #: 181971
• NCBI GeneID: 7422
• UniProt Accession #: P15692; O60720; O75875; Q074Z4; Q16889; Q5UB46; Q6P0P5; Q96KJ0; Q96L82; Q96NW5; Q9H1W8; B5BU86; Q59FH5; Q6WZM0; Q71S09; Q96FD9; Q9UNS8
• Molecular Weight: 27,042 Da
• NCBI Official Full Name: vascular endothelial growth factor
• NCBI Official Synonym Full Names: vascular endothelial growth factor A
• NCBI Official Symbol: VEGFA
• NCBI Official Synonym Symbols: VPF; VEGF; MVCD1
• NCBI Protein Information: vascular endothelial growth factor A; vascular permeability factor
• UniProt Protein Name: Vascular endothelial growth factor A
• Protein Family: Vascular endothelial growth factor
• UniProt Gene Name: VEGFA
• UniProt Synonym Gene Names: VEGF; VEGF-A; VPF
• UniProt Entry Name: VEGFA_HUMAN

NCBI Description

This gene is a member of the PDGF/VEGF growth factor family and encodes a protein that is often found as a disulfide linked homodimer. This protein is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis and endothelial cell growth, promoting cell migration, and inhibiting apoptosis. Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. Alternatively spliced transcript variants, encoding either freely secreted or cell-associated isoforms, have been characterized. There is also evidence for the use of non-AUG (CUG) translation initiation sites upstream of, and in-frame with the first AUG, leading to additional isoforms. [provided by RefSeq, Jul 2008]

Uniprot Description

VEGF iso14: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Defects in VEGFA are a cause of susceptibility to microvascular complications of diabetes type 1 (MVCD1). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Belongs to the PDGF/VEGF growth factor family. 13 isoforms of the human protein are produced by alternative promoter.

Protein type: Cytokine; Secreted, signal peptide; Secreted; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 6p12

Cellular Component: extracellular space; proteinaceous extracellular matrix; cell surface; membrane; cytoplasm; extracellular region; secretory granule

Molecular Function: heparin binding; identical protein binding; protein homodimerization activity; growth factor activity; extracellular matrix binding; cytokine activity; platelet-derived growth factor receptor binding; vascular endothelial growth factor receptor 1 binding; receptor agonist activity; vascular endothelial growth factor receptor binding; protein binding; vascular endothelial growth factor receptor 2 binding; protein heterodimerization activity; fibronectin binding; chemoattractant activity

Biological Process: heart morphogenesis; positive regulation of positive chemotaxis; positive regulation of cell adhesion; macrophage differentiation; positive regulation of leukocyte migration; positive regulation of receptor internalization; cell maturation; basophil chemotaxis; regulation of cell shape; positive regulation of MAP kinase activity; positive chemotaxis; positive regulation of mesenchymal cell proliferation; mesoderm development; kidney development; positive regulation of neuroblast proliferation; nervous system development; platelet activation; monocyte differentiation; positive regulation of blood vessel endothelial cell migration; activation of CREB transcription factor; positive regulation of protein amino acid autophosphorylation; positive regulation of vascular permeability; patterning of blood vessels; regulation of transcription from RNA polymerase II promoter; positive regulation of angiogenesis; positive regulation of peptidyl-tyrosine phosphorylation; eye photoreceptor cell development; camera-type eye morphogenesis; branching morphogenesis of a tube; cell migration during sprouting angiogenesis; cardiac muscle fiber development; positive regulation of cell division; positive regulation of axon extension involved in axon guidance; activation of protein kinase activity; positive regulation of endothelial cell proliferation; positive regulation of transcription from RNA polymerase II promoter; regulation of cGMP metabolic process; surfactant homeostasis; positive regulation of epithelial cell proliferation; negative regulation of apoptosis; lactation; post-embryonic camera-type eye development; negative regulation of caspase activity; negative regulation of transcription from RNA polymerase II promoter; positive regulation of vascular endothelial growth factor receptor signaling pathway; induction of positive chemotaxis; platelet degranulation; epithelial cell differentiation; ovarian follicle development; positive regulation of focal adhesion formation; positive regulation of cell proliferation; angiogenesis; vasculogenesis; in utero embryonic development; lumen formation; positive regulation of cell motility; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein complex assembly; response to hypoxia; artery morphogenesis; positive regulation of protein amino acid phosphorylation; vascular endothelial growth factor receptor signaling pathway; blood coagulation; positive regulation of cell migration; lung development; growth

Disease: Microvascular Complications Of Diabetes, Susceptibility To, 1