Recombinant Porcine VEGF Protein

$99.00$285.00

DataSheet   

The recombinant porcine VEGF-A protein is derived from in vitro expression of porcine VEGF-A gene in E. coli and purified using his-tag affinity column and can be used in multiple applications such as cell culture, ELISA and western blot.

Alternative names for VEGF: Vascular endothelial growth factor, vascular permeability factor (VPF) or vasculotropin, VEGFA

This product is for Laboratory Research Use Only not for diagnostic and therapeutic purposes or any other purposes.

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Description

Genorise Recombinant Porcine VEGF Protein Summary

Alternative names for VEGF: Vascular endothelial growth factor, vascular permeability factor (VPF) or vasculotropin, VEGFA

 

Product Specifications

Purity > 97%, by SDSPAGE under reducing conditions and visualized by silver stain.
Endotoxin Level < 1.0 EU per 1 μg of the protein by the LAL method.
Activity Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. Conn, G. et al. (1990) Proc Natl Acad Sci USA 87:1323. The ED50 for this effect is typically 1-5 ng/mL.

Background: 

Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF) or vasculotropin, is a homodimeric 34 – 42 kDa, heparin-binding glycoprotein with potent angiogenic, mitogenic and vascular permeability-enhancing activities specific for endothelial cells. VEGF is a sub-family of platelet-derived growth factor family of cystine-knot growth factors. The most important member is VEGF-A. Other members are Placenta growth factor (PlGF), VEGF-B, VEGF-C and VEGF-D. The amino acid sequence of VEGF exhibits primary structural, as well as limited amino acid sequence, homology with that of the A and B chains of PDGF. All eight cysteine residues involved in intra- and inter-chain disulfide bonds are conserved among these growth factors. Two receptor tyrosine kinases have been described as putative VEGF receptors. Flt-1 (fms-like tyrosine kinase), and KDR (kinase-insert-domain-containing receptor) proteins have been shown to bind VEGF with high affinity (1).  VEGF acts directly on the endothelium and does not degranulate mast cells. It promotes extravasation of plasma fibrinogen, leading to fibrin deposition which alters the tumor extracellular matrix. The modified extracellular matrix subsequently promotes the migration of macrophages, fibroblasts and endothelial cells. VEGF plays important roles in inflammation and during normal and pathological angiogenesis, a process that is associated with wound healing, embryonic development, and growth and metastasis of solid tumors. Elevated levels of VEGF have been reported in synovial fluids of rheumatoid arthritis patients and in sera from cancer patients (2, 3).

References

  1. Katherine H, et al. (2007). Cell Signal. 19 (10): 2003
  2. Amo, Y, et al. (2004). Br J Dermato. 150 (1): 160
  3. Bergers G, et al. (2008). Nat. Rev. Cancer 8 (8): 592

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