Vascular Endothelial Growth Factor, Recombinant Protein

VEGF Human; Vascular Endothelial Growth Factor Human Recombinant; Vascular endothelial growth factor A; VEGF-A; Vascular permeability factor; VPF; VEGF; MGC70609

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

E Coli

Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

The VEGF protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Sterile Filtered White lyophilized (freeze-dried) powder.

Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18 degree C. Upon reconstitution VEGF should be stored at 4 degree C between 2-7 days and for future use below -18 degree C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

Small volumes of VEGF 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 Human Recombinant produced in E Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38231 Dalton.The VEGF is purified by proprietary chromatographic techniques.

Introduction: Vascular endothelial growth factor (VEGF) is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells). VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.Elevated levels of the VEGF protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in the VEGF gene have been associated with proliferative and nonproliferative diabetic retinopathy.

CYTOKINES AND GROWTH FACTORS; Growth Factors; VEGF

34,406 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_HUMAN

This gene is a member of the PDGF/VEGF growth factor family and encodes a protein that is often found as a disulfide linked homodimer. This protein is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis and endothelial cell growth, promoting cell migration, and inhibiting apoptosis. Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. Alternatively spliced transcript variants, encoding either freely secreted or cell-associated isoforms, have been characterized. There is also evidence for the use of non-AUG (CUG) translation initiation sites upstream of, and in-frame with the first AUG, leading to additional isoforms. [provided by RefSeq, Jul 2008]

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.

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