Technical Data
V2110-07M
Vascular Endothelial Growth Factor, Recombinant, Rat (VEGF)
10ug
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Technical Data |
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V2110-07M |
Vascular Endothelial Growth Factor, Recombinant, Rat (VEGF) |
10ug |
| Growth Factors, Cytokines | Storage: -20°CShipping: RT |
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VEGF (Vascular Endothelial Growth Factor) is a homodimeric, disulfide-linked glycoprotein involved in angiogenesis which promotes tumor progression and metastasis. It exhibits potent mitogenic and permeablility inducing properties specific for the vascular endothelium. Multiple isoforms of VEGF containing 206-, 189-, 165-, and 121-amino acid residues have been described which arise from alternative splicing of a single gene. The smaller two isoforms, VEGF 165 and VEGF121, are secreted proteins and act as diffusible agents, whereas the larger two remain cell-associated. VEGF/VPF plays an important role in angiogenesis, which promotes tumor progression and metastasis. Source: Recombinant corresponding to 164aa from rat Vascular Endothelial Growth Factor expressed in E.coli. Molecular Weight: ~38.4kD Biological Activity: ED50 range=10-100ng/ml, determined by the dose dependent proliferation of human umbilical vein cells (HUVEC). Endotoxin: 0.1ng/ug Storage and Stability: Lyophilized powder may be stored at 4°C for short-term only. Reconstitute to nominal volume by adding sterile ddH2O or buffer, 0.1% BSA., aliquot and store at -20°C. Reconstituted product is stable for 12 months at -20°C. 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: E. coli Purity: ~95% (SDS-PAGE). Purified by Ion Exchange chromatography. Concentration: ~0.1mg/ml Form: Supplied as a lyophilized powder. BSA free. Reconstitute with sterile, ddH2O or buffer, 0.1% BSA. to a concentration of 0.1-1mg/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. |
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1. Barleon, B., et al. (1997) Mapping of the sites for ligand binding and receptor dimerization at the extracellular domain of the vascular endothelial growth factor receptor flt-1. J. Biol. Chem. 272:10382-10388.
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