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Human / Cynomolgus VEGF / VEGFA / VEGF165 Protein

MVCD1,VEGF,VEGF165,VPF

Catalog Number P11066-HNAB
Organism Species Human
Host Baculovirus-Insect Cells
Synonyms MVCD1,VEGF,VEGF165,VPF
Molecular Weight The recombinant human VEGF consists of 165 amino acids after removal of the signal peptide and predicts a molecular mass of 19.2 kDa. Due to different glycosylation, the apparent molecular mass of rhVEGF165 is approximately 20 and 22 kDa in SDS-PAGE under reducing conditions, corresponding to the monomer.
predicted N Ala 27
SDS-PAGE
Purity > 98 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human VEGF 165 isoform (P15692-4) (Met1-Arg191) was expressed. Human and Cynomolgus VEGF165 sequences are identical.
Bio-activity Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC).
The ED50 for this effect is typically 3-12 ng/ml .
Research Area Cardiovascular |Angiogenesis |Growth Factor & Receptor |Vascular Endothelial Growth Factor (VEGF) & Receptor |Vascular Endothelial Growth Factor (VEGF)
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF) and VEGF-A, is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult. It is a member of the platelet-derived growth factor (PDGF)/vascular endothelial growth factor (VEGF) family and often exists as a disulfide-linked homodimer. VEGF-A 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, inhibiting apoptosis and tumor growth. VEGF-A protein is also a vasodilator that increases microvascular permeability, thus it was originally referred to as vascular permeability factor.
Reference
  • Woolard J. et al. (2004) VEGF165b, an inhibitory vascular endothelial growth factor splice variant: mechanism of action, in vivo effect on angiogenesis and endogenous protein expression. Cancer Res. 64(21): 7822-7835.
  • Jia SF, et al. (2008) VEGF165 is necessary to the metastatic potential of Fas(-) osteosarcoma cells but will not rescue the Fas(+) cells. J Exp Ther Oncol. 7(2): 89-97.
  • Cimpean AM, et al. (2008) Vascular endothelial growth factor A (VEGF A) as individual prognostic factor in invasive breast carcinoma. Rom J Morphol Embryol. 49(3): 303-8.
  • Hamdollah Zadeh MA, et al. (2008) VEGF-mediated elevated intracellular calcium and angiogenesis in human microvascular endothelial cells in vitro are inhibited by dominant negative TRPC6. Microcirculation. 15(7): 605-14.
  • Eisenach PA, et al. (2010) MT1-MMP regulates VEGF-A expression through a complex with VEGFR-2 and Src. J Cell Sci. 123(Pt 23):4182-4193.
  • Claesson-Welsh L (2010) Gremlin: vexing VEGF receptor agonist. Blood. 116(18):3386-7.