Recombinant Human VEGF 111 Protein Summary
Product Specifications
Ala27-Arg137, with an N-terminal Met & Pro28-Arg137
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
5336-VE
Formulation | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 ug/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
5336-VE/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. |
Reconstitution | Reconsitute at 100 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: VEGF
Vascular endothelial growth factor (VEGF or VEGF-A), also known as vascular permeability factor (VPF), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult (1-3). It is a member of the PDGF family that is characterized by the presence of eight conserved cysteine residues and a cysteine-knot structure (4). Humans normally express alternately spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) in length (4). VEGF165 appears to be the most abundant and potent isoform, followed by VEGF121 and VEGF189 (3, 4). Additionally, an active ~18 kDa form, VEGF111, can be induced in tumor cells by treatment with genotoxic agents and ultraviolet (UV-B) irradiation (5). Like VEGF121, VEGF111 lacks the basic heparin-binding region encoded by exons 6 and 7, and is freely diffusible (4, 5). VEGF111 also lacks major proteolytic cleavage sites encoded by exon 5, giving it additional stability. Human VEGF111 shares 87% aa sequence identity with corresponding regions of mouse and rat VEGF, 93% with feline, equine and bovine VEGF, and 91%, 95% and 96% with ovine, canine and porcine VEGF, respectively. All VEGF forms bind the single pass receptor tyrosine kinases VEGF R1 (also called Flt-1) and VEGF R2 (Flk-1/KDR) on endothelial cells (4). Although VEGF affinity is highest for binding to VEGF R1, VEGF R2 appears to be the primary mediator of VEGF angiogenic activity (3, 4). VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells (3, 4). In adults, VEGF functions mainly in wound healing and in female during reproductive cycle (3). Pathologically, it is involved in tumor angiogenesis and vascular leakage (6, 7).
- Leung, D.W. et al. (1989) Science 246:1306.
- Keck, P.J. et al. (1989) Science 246:1309.
- Byrne, A.M. et al. (2005) J. Cell. Mol. Med. 9:777.
- Robinson, C.J. and Stringer, S.E. (2001) J. Cell. Sci. 114:853.
- Mineur, P. et al. (2007) J. Cell Biol. 179:1261.
- Weis, S.M. and D.A. Cheresh (2005) Nature 437:497.
- Thurston, G. (2002) J. Anat. 200:575.
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