Active Recombinant human VEGF/PlGF

• Cat.No.: VEGFA&PIGF-28H
• Product Overview: Recombinant human VEGF/PlGF, expressed in E. coli. DNA sequences encoding the mature 165 amino acid residue variant of VEGF (Leung, P.W. et al., 1989, Science 246:1306) and the mature 129 amino acid residue form of placenta growth factor (PlGF) (Maglione, D. et al., 1993, Oncogene 8:925 - 931) were expressed in E. coli. Recombinant VEGF/PlGF heterodimer was dimerized in vitro.

Specification

• Description: The disulfidelinked homodimeric proteins vascular endothelial growth factor (VEGF) and placenta growth factor (PlGF) are both members of the VEGF family of growth factors. VEGF and PlGF proteins share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. In their PDGF like regions, VEGF and PlGF also share approximately 53% amino acid sequence similarity. E. coli expressed monomers of PlGF and VEGF can be refolded in vitro to form P lGF/VEGF heterodimers. The purified recombinant VEGF/PlGF heterodimers and VEGF homodimers have potent mitogenic effects on endothelial cells. However, VEGF/PlGF heterodimers display approximately 50 fold less mitogenic activity than VEGF homodimers. In contrast, PlGF homodimers have little or no mitogenic effect on endothelial cells. The presence of natural VEGF/PlGF heterodimers in the conditioned media of a number of human tumor cell lines has been demonstrated using a VEGF/PlGF heterodimer specific ELISA.
• Source: E. Coli
• Species: Human
• Form: Lyophilized from a 0.2 μm filtered solution in PBS containing 50 μg of bovine serum albumin per 1 μg of cytokine.
• Bio-activity: Measured by its ability to stimulate 3H-thymidine incorporation in HUVE cells (Conn, G. et al., 1990, Pr centigrade. Natl. Acad. Sci. USA 87:1323 - 1327).The ED50 for this effect is typically 100 - 200 ng/mL.
• Molecular Mass: The disulfide-linked heterodimeric VEGF/PlGF has a predicted molecular mass of approximately 28 kDa.
• Endotoxin: < 1.0 eu per 1 μg of the cytokine as determined by the lal
• Purity: >97%, as determined by SDS-PAGE and visualized by silver stain
• Usage: FOR RESEARCH USE ONLY
• Quality Control Test: Lyophilized samples are stable for up to six months at -20 centigrade to -70 centigrade. Upon reconstitution, this cytokine, in the presence of a carrier protein, can be stored under sterile conditions at 2 - 8 centigrade for one month or at -20 centigrade to -70 centigrade in a manual defrost freezer for three months without detectable loss of activity.
• Reconstitution: It is recommended that sterile PBS containing at least 0.1% human serum albumin or bovine serum albumin be added to the vial to prepare a st centigradek solution of no less than 5 μg/mL.
• Warning: Avoid repeated freeze-thaw cycles.

Gene Information

• Gene Name: VEGFA vascular endothelial growth factor A [ Homo sapiens ]; PIGF phosphatidylinositol glycan anchor biosynthesis, class F [ Homo sapiens ]
• Official Symbol: VEGFA; PIGF
• Synonyms: VEGFA; vascular endothelial growth factor A; vascular endothelial growth factor, VEGF; VEGF A; VPF; vascular permeability factor; VEGF; MVCD1; MGC70609; PIGF; phosphatidylinositol glycan anchor biosynthesis, class F; phosphatidylinositol glycan, class F; phosphatidylinositol-glycan biosynthesis class F protein; PIG-F; GPI11 homolog; MGC32646; MGC33136
• Gene ID: 7422; 5281
• mRNA Refseq: NM_001025366; NM_002643
• Protein Refseq: NP_001020537; NP_002634
• MIM: 192240; 600153
• UniProt ID: P15692; Q07326
• Chromosome Location: 6p12; 2p21-p16
• Pathway: Bladder cancer, organism-specific biosystem; Bladder cancer, conserved biosystem; Cytokine-cytokine receptor interaction, organism-specific biosystem; Cytokine-cytokine receptor interaction, conserved biosystem; Endochondral Ossification, organism-specific biosystem; Focal adhesion, organism-specific biosystem; Focal adhesion, conserved biosystem
• Function: cell surface binding; chemoattractant activity; cytokine activity; cytokine activity; extracellular matrix binding; fibronectin binding; growth factor activity; growth factor activity; heparin binding; heparin binding; platelet-derived growth factor receptor binding; protein binding; protein heterodimerization activity; protein homodimerization activity; receptor agonist activity; vascular endothelial growth factor receptor 1 binding; vascular endothelial growth factor receptor 2 binding; vascular endothelial growth factor receptor binding; ethanolaminephosphotransferase activity