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Merck
모든 사진(1)

문서

SRP3183

Sigma-Aldrich

VEGF-B human

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

동의어(들):

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

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About This Item

UNSPSC 코드:
12352202
NACRES:
NA.32

생물학적 소스

human

재조합

expressed in E. coli

분석

≥98% (HPLC)
≥98% (SDS-PAGE)

형태

lyophilized

효능

1.0-2.0 μg/mL ED50

분자량

38.0 kDa

포장

pkg of 20 μg

기술

cell culture | mammalian: suitable

불순물

<0.1 EU/μg endotoxin, tested

색상

white

UniProt 수납 번호

배송 상태

wet ice

저장 온도

−20°C

유전자 정보

human ... VEGFB(7423)

일반 설명

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.

생화학적/생리학적 작용

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.

서열

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

물리적 형태

Lyophilized from 10 mM Acetic Acid.

재구성

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


시험 성적서(COA)

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문서 라이브러리 방문

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)
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
Vascular endothelial growth factor and angiogenesis.
Hoeben A et al
Pharmacological Reviews, 56(4), 549-580 (2004)

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