Recombinant Human VEGF 145 (aa 27-171) Protein Summary
Product Specifications
Ala27-Arg171, with an N-terminal Met
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.
7626-VE
| Formulation | Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 100 μg/mL 4 mM HCl 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.
|
7626-VE/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in HCl. |
| Reconstitution | Reconstitute at 100 μg/mL in 4 mM HCl. |
| 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 VEGFA), 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 of proteins that is characterized by the presence of eight conserved cysteine residues that form a cystine knot structure (4). Humans express multiple alternatively spliced isoforms of VEGF that are 111, 121, 145, 165, 183, 189, and 206 amino acids (aa) in length (4, 5, 6). Isoforms other than VEGF111 and 121 contain basic heparin binding regions and are not freely diffusible (4, 5). VEGF165 appears to be the most abundant and potent isoform, followed by VEGF121 and VEGF189 (3-5). VEGF145 expression is relatively low, and is found mainly in female and male reproductive tissues, carcinomas of the female reproductive system, and other solid tumors (5, 7, 8). Expression of mouse VEGF144, the rodent ortholog to human VEGF145, is particularly enhanced by metabolic stress, such as that encountered during sustained exercise or starvation (8, 9). Human VEGF145 shares 89% aa sequence identity with mouse and rat VEGF144. VEGF145 binds to the type I transmembrane receptor tyrosine kinase VEGF R2/KDR/Flk1 on endothelial cells. This receptor appears to be the primary mediator of VEGF angiogenic activity (3-5, 7). Unlike VEGF165, VEGF145 does not bind VEGF R1/Flt1 or VEGF R3/Flt-4 (4, 5, 7). VEGF145 also binds the semaphorin receptor Neuropilin2 and promotes complex formation with VEGF R2, but unlike VEGF165 and VEGF121, it does not bind Neuropilin1 (10, 11). VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells (3, 4, 7). In adults, VEGF acts mainly during wound healing and the female reproductive cycle (3). Pathologically, isoforms that include VEGF145 are involved in tumor angiogenesis and vascular leakage (5, 12, 13).
- 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 S.E. Stringer (2001) J. Cell. Sci. 114:853.
- Woolard, J. et al. (2009) Microcirculation 16:572.
- Mineur, P. et al. (2007) J. Cell Biol. 179:1261.
- Poltorak, Z. et al. (1997) J. Biol. Chem. 272:7151.
- Zhang, L. et al. (2002) Biochem. Biophys. Res. Commun. 292:860.
- Ding, Y.H. et al. (2004) Curr. Neurovasc. Res. 1:411.
- Pan, Q. et al. (2007) J. Biol. Chem. 282:24049.
- Gluzman-Poltorak, Z. et al. (2000) J. Biol. Chem. 275:18040.
- Weis, S.M. and D.A. Cheresh (2005) Nature 437:497.
- Thurston, G. (2002) J. Anat. 200:575.
Citation for Recombinant Human VEGF 145 (aa 27-171) Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Aging impairs VEGF-mediated, androgen-dependent regulation of angiogenesis.
Authors: Lecce, Laura, Lam, Yuen Tin, Lindsay, Laura A, Yuen, Sui Chin, Simpson, Philippa, Handelsman, David J, Ng, Martin K
Mol Endocrinol, 2014-07-24;28(9):1487-501.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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