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Name :
Human VEGF Protein, Isoform 165, Recombinant

Description :
VEGF, also known as VEGF-A (vascular endothelial growth factor A) and VPF (vascular permeability factor), is the founding member of the VEGF family, including VEGF-A, VEGF-B, VEGF-C, VEGF-D, VEGF-E, and PIGF. VEGFs are secreted polypeptides with a highly conserved receptor-binding cystine-knot structure similar to that of the platelet-derived growth factors (PDGF). VEGF plays important roles in vascular development and in diseases involving abnormal growth of blood vessels such as tumor-related angiogenesis. VEGF is a growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. It induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and increases permeabilization of blood vessels. VEGF is involved in normal and pathological angiogenesis, a process that is associated with inflammation, wound healing, embryonic development, growth and metastasis of solid tumors. Elevated levels of VEGF have been detected in patients with cancer and autoimmune diseases, such as rheumatoid arthritis, multiple sclerosis, and systemic lupus erythematosus. VEGF is known to bind to the FLT1 (VEGFR1) and KDR (VEGFR2) receptors, heparan sulfate and heparin. Targeting VEGF signaling pathway has shown therapeutic benefits in multiple cancer types. Alternately spliced VEGF isoforms of 121, 145, 165, 183, 189, and 206 amino acids in length exist in human. VEGF165 appears to be the most abundant isoform, followed by VEGF121 and VEGF189. Isoforms other than VEGF121 contain basic heparin­binding regions and are thus not freely diffusible. Human and cynomolgus VEGF165 are identical.

Gene Symbol :

NCBI Gene ID :
7422 (human), 22339 (mouse)

Uniprot Entry :
P15692 (human), Q00731 (mouse)

Construct Details :
Human VEGF165, also known as VEGF, is expressed as a 176-amino acid protein consisting of the region Ala27- Arg191 of VEGF (UniProt Accession #P15692-4, isoform VEGF165) and a C-terminal His-tag. It contains 1 potential sites for N-linked glycosylation and exists as a dimer under non-reducing condition (see the gel image inserted).

Source :
Mammalian cells stably expressing human VEGF165 and growing in chemical-defined media with no animal components or antibiotics

Amino Acid Sequence: :
APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRC GGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQE NPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRRSTGHHH HHHHH

M.W. :
Calculated molecular mass (kDa): 20.5; Estimated by SDS-PAGE under reducing condition (kDa): ~30 (probably due to glycosylation)

Calculated PI :
7.66

Calculated Extinction Coefficients :
(M-1 cm-1, at 280nm): 6960

Endotoxin Level :
>95% judged by SDS-PAGE under reducing condition (see the gel image above, labeled as “DTT: +”)

Formulation :
Supplied at 0.5 mg/ml in sterile PBS pH7.4 (carrier & preservative free).

Endotoxin Level :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method

Biological Activity :
Binds its receptors (FLT1, KDR) and anti-VEGF monoclonal antobodies (SKU#MAB0345, MAB0337 ) with high affinity (KD

Molecule Class :
Angiogenic Growth Factor (secreted)

Gene Synonym :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method

Gene Family :
VEGFA; VEGF-A; VPF; MVCD1

Research Area :
Angiogenesis

Pathway/Disease :
VEGF Signaling Pathway

Species :
Human

CD Antigen :

References :
1. Science 246:1306-1309, 1989

MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
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