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Key Documents

SRP3183

Sigma-Aldrich

VEGF-B human

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

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in E. coli

Pureté

≥98% (HPLC)
≥98% (SDS-PAGE)

Forme

lyophilized

Puissance

1.0-2.0 μg/mL ED50

Poids mol.

38.0 kDa

Conditionnement

pkg of 20 μg

Technique(s)

cell culture | mammalian: suitable

Impuretés

<0.1 EU/μg endotoxin, tested

Couleur

white

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

human ... VEGFB(7423)

Description générale

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.

Actions biochimiques/physiologiques

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.

Séquence

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

Forme physique

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.

Pictogrammes

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Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Eye Irrit. 2 - Skin Irrit. 2

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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 and angiogenesis.
Hoeben A et al
Pharmacological Reviews, 56(4), 549-580 (2004)
Vascular endothelial growth factor-B in physiology and disease.
Bry M et al
Physiological Reviews, 94(3), 779-794 (2014)
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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