VEGF165 Protein, Human / Cynomolgus, Recombinant

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VEGF165 Protein, Human / Cynomolgus, Recombinant: Product Information

Purity
> 97 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
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
.
Protein Construction
A DNA sequence encoding the human VEGF 165 isoform (P15692-4) (Met1-Arg191) was expressed. Human and Cynomolgus VEGF165 sequences are identical.
Accession#
Expressed Host
Baculovirus-Insect Cells
Species
Human
Predicted N Terminal
Ala 27
Molecule Mass
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.
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.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

VEGF165 Protein, Human / Cynomolgus, Recombinant: Images

Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC). The ED50 for this effect is typically 3-12 ng/ml .

VEGF165 Protein, Human / Cynomolgus, Recombinant: Alternative Names

MVCD1 Protein, Human; VEGF Protein, Human; VEGF165 Protein, Human; VPF Protein, Human

VEGFA Background Information

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.
Full Name
vascular endothelial growth factor A
References
  • 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.
  • Xanthatin, a novel potent inhibitor of VEGFR2 signaling, inhibits angiogenesis and tumor growth in breast cancer cells
    Author
    Yu, Y;Yu, J;Pei, CG;Li, YY;Tu, P;Gao, GP;
    Year
    2015
    Journal
    Int J Clin Exp Pathol.
    Application
    cell-based
  • Automating hESC differentiation with 3D printing and legacy liquid handling solutions
    Author
    Zluhan, E;Kelly, K;LeClair, N;Wortel, D;Moody, K;
    Year
    2016
    Journal
    MethodsX
    Application
    culture
  • Oxidized low-density lipoprotein decreases VEGFR2 expression in HUVECs and impairs angiogenesis
    Author
    ZHANG, M;JIANG, L;
    Year
    2016
    Journal
    EXPERIMENTAL AND THERAPEUTIC MEDICINE
    Application
    cell-based
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