Technical Data
V2110-04V
Vascular Endothelial Growth Factor-121, aa207-327, Recombinant, Human (VEGF-121)
10ug
Molecular Biology Storage: -20CShipping: Blue Ice
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 cystine knot structure (4). Humans 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). VEGF121 is the only form that lacks a basic heparin-binding region and is freely diffusible (4). Mouse embryos expressing only the corresponding isoform (VEGF120) do not survive to term, and show defects in skeletogenesis (5). Human VEGF121 shares 87% aa sequence identity with corresponding regions of mouse and rat, 93% with feline, equine and bovine, and 91%, 95% and 96% with ovine, canine and porcine VEGF, respectively. VEGF binds the type I transmembrane 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). VEGF165 binds the semaphorin receptor, Neuropilin-1; VEGF121 binding has also been reported (6). 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 the female reproductive cycle (3). Pathologically, it is involved in tumor angiogenesis and vascular leakage (7, 8). Circulating VEGF levels correlate with disease activity in autoimmune diseases such as rheumatoid arthritis, multiple sclerosis and systemic lupus erythematosus (9). VEGF is induced by hypoxia and cytokines such as IL-1, IL-6, IL-8, oncostatin M and TNF-a (3, 4, 10).

A DNA sequence encoding the mature 121 amino acid residues of human VEGF (Ala 207-Arg 327; Accession # NP_001020541) was expressed in E. coli.

Calculated molecular mass of ~ 14kD.

Activity: Measured by its ability to stimulate proliferation in HUVE cell.

Storage and Stability:
Lyophilized powder may be stored at 4C for short-term only. Reconstitute to nominal volume by adding sterile PBS and store at -20C. Reconstituted product is stable for 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Source: Recombinant Human
Purity: 95%, as determined by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin: 1EU/1ug.
Concentration: As reported
Form: Supplied as a lyophilized powder in 30% CH3CN and 0.1% TFA containing 50ug of bovine serum albumin per 1ug of growth factor. Reconstitute with PBS containing at least 0.1% human serum albumin or bovine serum albumin be added to the vial to prepare a stock solution of no less than 10ug/ml.

Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
1. Leung, D.W. et al., 1989, Science 246:1306. 7. Weis, S.M. & D.A. Cheresh, 2005, Nature 437:497.
2. Keck, P.J. et al., 1989, Science 246:1309. 8. Thurston, G., 2002, J. Anat. 200:575.
3. Byrne, A.M. et al., 2005, J. Cell. Mol. Med. 9:777. 9. Carvalho, J.F. et al., 2007, J. Clin. Immunol. 27:246.
4. Robinson, C.J. and Stringer, S.E., 2001, J. Cell. Sci. 114:853. 10. Angelo, L.S. & R. Kurzrock, 2007, Clin. Cancer Res. 13:2825.
5. Zelzer, E. et al., 2002, Development 129:1893.
6. Pan, Q. et al., 2007, J. Biol. Chem. 282:24049.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.