SRP3183
VEGF-B human
recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture
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Synonym(s):
VEGF-related factor, VRF, Vascular Endothelial Growth Factor-B
UNSPSC Code:
12352202
NACRES:
NA.32
Recommended Products
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)
Related Categories
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.
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.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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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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