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SRP3183

Sigma-Aldrich

VEGF-B human

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

Synonym(s):

VEGF-related factor, VRF, Vascular Endothelial Growth Factor-B

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

potency

1.0-2.0 μg/mL ED50

mol wt

38.0 kDa

packaging

pkg of 20 μg

technique(s)

cell culture | mammalian: suitable

impurities

<0.1 EU/μg endotoxin, tested

color

white

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... VEGFB(7423)

General description

VEGFB (vascular endothelial growth factor B) is one of the seven members of the VEGF family, which also includes VEGF-A, VEGF-C, VEGF-D, VEGF-E, VEGF-F, and PIGF (placental growth factor). All these members contain a common VEGF homology domain. This domain forms the core region and contains a cystine knot motif composed of eight invariant cysteine residues. VEGFB, discovered in 1995, is highly expressed in adult myocardium, skeletal muscle, and pancreas. This gene contains seven exons and alternative splicing results in the synthesis of two isoforms VEGF-B167 of 21 kDa and VEGF-B186 of 32 kDa. These isoforms show differential level of expression with VEGF-B167 being the predominantly expressed isoform. VEGFB gene is localized to human chromosome 11q13.
Recombinant human VEGF-B is a 38.0 kDa disulfide-linked homodimeric protein consisting of two 167 amino acid polypeptide chains.

Biochem/physiol Actions

VEGF-B, a member of the VEGF family, is a potent growth and angiogenic cytokine. Recombinant human VEGF-B is a 38.0 kDa disulfide-linked homodimeric protein consisting of two 167 amino acid polypeptide chains.
VEGFB (vascular endothelial growth factor B) acts on the receptors VEGFR-1 (VEGF receptor) and NRP-1 (neuropilin). This protein induces coronary vessel growth and cardiac hypertrophy, which might confer protection to heart against ischemic damage and heart failure. It might have a role in metabolic functions as it shows high expression levels in tissues with highly active energy metabolism. VEGFB is also thought to be involved in neuroprotection. This protein is involved in fetal angiogenesis, functions as a mitogen for endothelial cells (ECs), survival factor for multiple types of cells such as neurons, vascular cells, and myocytes.

Sequence

PVSQPDAPGH QRKVVSWIDV YTRATCQPRE VVVPLTVELM GTVAKQLVPS CVTVQRCGGC CPDDGLECVP TGQHQVRMQI LMIRYPSSQL GEMSLEEHSQ CECRPKKKDS AVKPDSPRPL CPRCTQHHQR PDPRTCRCRC RRRSFLRCQG RGLELNPDTC RCRKLRR

Physical form

Lyophilized from 10 mM Acetic Acid.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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S Grimmond et al.
Genome research, 6(2), 124-131 (1996-02-01)
This paper describes the cloning and characterization of a new member of the vascular endothelial growth factor (VEGF) gene family, which we have designated VRF for VEGF-related-factor. Sequencing of cDNAs from a human fetal brain library and RT-PCR products from
Vascular endothelial growth factor-B in physiology and disease.
Bry M et al
Physiological Reviews, 94(3), 779-794 (2014)
Vascular endothelial growth factor and angiogenesis.
Hoeben A et al
Pharmacological Reviews, 56(4), 549-580 (2004)
Roles of vascular endothelial growth factor in amyotrophic lateral sclerosis.
Pronto-Laborinho AC et al
BioMed Research International, 2014, 947513-947513 (2014)
Fan Zhang et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(15), 6152-6157 (2009-04-17)
VEGF-B, a homolog of VEGF discovered a long time ago, has not been considered an important target in antiangiogenic therapy. Instead, it has received little attention from the field. In this study, using different animal models and multiple types of

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