Vascular Endothelial Growth Factor, Recombinant Protein

VEGF C Rat; Vascular Endothelial Growth Factor Related Protein Rat Recombinant; VEGF-C; Vascular endothelial growth factor C; VRP; Flt4 ligand; Flt4-L

For Research Use Only. Not for use in diagnostic procedures.

Sf9 Insect Cells

Greater than 90.0% as determined by(a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

Each mg of VEGF-C Rat contains 50mg BSA and PBS as buffer.
Sterile Filtered White lyophilized (freeze-dried) powder.

Lyophilized Vascular Endothelial Growth Factor-C although stable at room temperature for 3 weeks, should be stored desiccated below -18 degree C. Upon reconstitution VEGF-C should be stored at 4 degree C between 2-7 days and for future use below -18 degree C.Please prevent freeze-thaw cycles.

Small volumes of rVEGFC recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Description: Vascular Endothelial Growth Factor C Rat Recombinant contains 129 amino acids residues and was fused to a His- tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 18-24 kDa protein in SDS-PAGE under reducing conditions.

Introduction: VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. The rat VEGFC cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In *****s, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant rat VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT -4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant rat VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.

CYTOKINES AND GROWTH FACTORS; Growth Factors; VEGF

17,189 Da

vascular endothelial growth factor A

vascular endothelial growth factor A; vascular permeability factor

Vascular endothelial growth factor A

Vegf; VEGF-A; VPF  [Similar Products]

VEGFA_RAT

This gene product is a member of the PDGF/VEGF growth factor family. It is a mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis, endothelial cell growth, promoting cell migration, and inhibiting apoptosis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. Also, alternative translation initiation from non-AUG (CUG) and AUG start sites in some transcript variants, give rise to additional isoforms. The expression of some isoforms derived from AUG start codon is affected by a small upstream open reading frame, which is located within an internal ribosome entry site. [provided by RefSeq, Nov 2013]

VEGF: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Defects in VEGFA are a cause of susceptibility to microvascular complications of diabetes type 1 (MVCD1). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic *****s. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Belongs to the PDGF/VEGF growth factor family. 13 isoforms of the human protein are produced by alternative promoter.

Protein type: Secreted, signal peptide; Cytokine; Motility/polarity/chemotaxis; Secreted

Cellular Component: extracellular space; cell surface; membrane; cytoplasm; extracellular region; basement membrane; secretory granule

Molecular Function: heparin binding; identical protein binding; protein homodimerization activity; growth factor activity; extracellular matrix binding; cytokine activity; platelet-derived growth factor receptor binding; vascular endothelial growth factor receptor 1 binding; vascular endothelial growth factor receptor binding; receptor agonist activity; vascular endothelial growth factor receptor 2 binding; protein heterodimerization activity; fibronectin binding; receptor binding; chemoattractant activity

Biological Process: heart morphogenesis; positive regulation of cell adhesion; positive regulation of positive chemotaxis; macrophage differentiation; cell maturation; positive regulation of receptor internalization; female pregnancy; response to vitamin A; basophil chemotaxis; positive regulation of MAP kinase activity; regulation of cell shape; positive chemotaxis; response to folic acid; positive regulation of mesenchymal cell proliferation; mesoderm development; negative regulation of neuron apoptosis; kidney development; nervous system development; positive regulation of neuroblast proliferation; T-helper 1 type immune response; positive regulation of signal transduction; monocyte differentiation; mRNA stabilization; positive regulation of blood vessel endothelial cell migration; activation of CREB transcription factor; positive regulation of protein amino acid autophosphorylation; regulation of endothelial cell differentiation; positive regulation of vascular permeability; regulation of transcription from RNA polymerase II promoter; patterning of blood vessels; positive regulation of peptidyl-tyrosine phosphorylation; eye photoreceptor cell development; positive regulation of angiogenesis; camera-type eye morphogenesis; branching morphogenesis of a tube; cell migration during sprouting angiogenesis; cardiac muscle fiber development; positive regulation of cell division; positive regulation of axon extension involved in axon guidance; activation of protein kinase activity; neuron development; blood vessel morphogenesis; endothelial cell migration; positive regulation of transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; regulation of cGMP metabolic process; response to progesterone stimulus; surfactant homeostasis; alveolus development; positive regulation of epithelial cell proliferation; negative regulation of apoptosis; lactation; post-embryonic camera-type eye development; wound healing; positive regulation of smooth muscle cell proliferation; negative regulation of caspase activity; negative regulation of transcription from RNA polymerase II promoter; response to estradiol stimulus; positive regulation of vascular endothelial growth factor receptor signaling pathway; induction of positive chemotaxis; epithelial cell differentiation; positive regulation of focal adhesion formation; vasculature development; ovarian follicle development; positive regulation of cell proliferation; lymphangiogenesis; negative regulation of programmed cell death; angiogenesis; cell differentiation; negative regulation of bone resorption; aging; blood vessel development; cell migration; in utero embryonic development; lumen formation; positive regulation of cell motility; positive regulation of peptidyl-serine phosphorylation; cell proliferation; positive regulation of protein kinase B signaling cascade; positive regulation of protein complex assembly; response to hypoxia; artery morphogenesis; blood vessel remodeling; negative regulation of cell-cell adhesion; sprouting angiogenesis; response to cold; positive regulation of protein amino acid phosphorylation; vascular endothelial growth factor receptor signaling pathway; hyaluronan metabolic process; positive regulation of cell migration; growth; lung development

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