Technical Data
EG-VEGF, Active, Recombinant, Human (Prokineticin-1, Endocrine-gland-derived Vascular Endothelial Growth Factor, Mambakine, PROK1, UNQ600/PRO1186)
Molecular Biology Storage: -20CShipping: Blue Ice
Embryonic vascular system undergoes a series of complex, highly regulated series of events involving differentiation, migration and association of primitive endothelial cells. This process is termed vasculogenesis. Study of tumor angiogenesis has led to the identification of several proteins including basic fibroblast growth factor (bFGF) and vascular endothelial growth factor. VEGF acts by interacting with a family of largely endothelial-specific receptor tyrosine kinases that includes VEGFR-1 (flt-1), VEGFR-2 (flk- 1/KDR), and VEGFR-3/Flt-4. Disruption of VEGFRs interferes with differentiation of endothelial cells and it is lethal for the embryo.

VEGF is a heparin-binding glycoprotein that is secreted as a homodimer of 45kD. There are several splice variants of VEGF-A. The major ones include: 121, 165, 189 and 206aa, each one comprising a specific exon addition. VEGF121 is acidic and freely secreted. VEGF165 is more basic, has heparin- binding properties and, although a signicant proportion remains cell-associated, most is freely secreted. VEGF189 is very basic; it is cell-associated after secretion and is bound avidly by heparin and the extracellular matrix, although it may be released as a soluble form by heparin, heparinase or plasmin. VEGF165 is the most predominant protein, but transcripts of VEGF121 may be more abundant. VEGF206 is rarely expressed and has been detected only in fetal liver. Recently, other splice variants of 145 and 183aa have also been described. The 165, 189 and 206aa splice variants have heparin-binding domains, which help anchor them in extracellular matrix and are involved in binding to heparin sulfate and presentation to VEGF receptors. This is a key factor for VEGF potency (i.e., the heparin-binding forms are more active). VEGF-A is regulated by growth factors, cytokines, gonadotropins, nitric oxide, hypoxia, hypoglycemia and oncogenic mutations.

Recombinant human EG-VEGF, produced in E.coli is a single, non-glycosylated, polypeptide chain containing 86aa.

Molecular Weight:
9605 dalton

Biological Activity:
Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 1.0-5.0ng/ml.

Storage and Stability:
Lyophilized powder may be stored at -20C. Stable for 12 months at -20C. Reconstitute with ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. Reconstituted product is stable for 6 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.

Molecular Weight:
Source: E.coli
Purity: ~95% (SDS-PAGE, HPLC). Endotoxin: 0.1ng/ug
Concentration: Not determined.
Form: Supplied as a lyophilized powder. Reconstitute with sterile dH2O or PBS to 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.
1. Keck PJ (1989) Science 246, 1309-1312. 2. Leung DW (1989) Science 246, 1306-1309. 3. Tischer E (1991) JBC 266, 11947- 11954. 4. Houck, KA (1991) Mol. Endocrinol. 5, 1806-1814. 5. Poltorak Z (1997) JBC 272, 7151-7158. 6. Lei J (1998) BBA 1443, 400-406. 7. Whittle C (1999) Clin. CSci. 97, 303-312.

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