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SRP4915

Sigma-Aldrich

Vaspin human

recombinant, expressed in E. coli, ≥90% (SDS-PAGE), ≥90% (HPLC)

Sinónimos:

OL-64, SERPINA12, Serpin A12 precursor, Vaspin, Visceral adipose tissue- derived serine protease inhibitor, Visceral adipose-specific serpin

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

assay

≥90% (HPLC)
≥90% (SDS-PAGE)

form

lyophilized powder

mol wt

~47.0 kDa

packaging

pkg of 25 μg

storage condition

avoid repeated freeze/thaw cycles

impurities

endotoxin, tested

NCBI accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... SPA12(145264)

General description

Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, is a member of serine protease inhibitor family. It is also known as serpin family A member 12 (SERPINA12). The gene encoding this protein is localized on human chromosome 14q32.13. Recombinant human Vaspin produced in E. coli is a single, non-glycosylated polypeptide chain containing 415 amino acids and having a molecular mass of 47kDa.

Biochem/physiol Actions

Vaspin (visceral adipose-specific SERPIN) is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism. This protein may be useful as a biomarker with patients with acute myocardial infarction. It is a ligand of the 78kDa glucose-regulated protein/murine transmembrane protein (GRP78/MTJ-1) complex and has indirect effects on endoplasmic reticulum stress-induced metabolic disorders.

Physical form

1 mg/ml in 20 mM Tris pH-8, 0.2 mM PMSF and 10% glycerol.

Reconstitution

Centrifuge the vial prior to opening. Avoid freeze-thaw cycles.

Storage Class

13 - Non Combustible Solids

wgk_germany

nwg


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Visite la Librería de documentos

Feihong Yang et al.
Biochemical and biophysical research communications, 503(2), 501-507 (2018-05-08)
Visceral adipose tissue-derived serine protease inhibitor (vaspin), as a secretory adipokine, was reported to exert a protective role on insulin resistance. Recent studies showed that serum vaspin level was downregulated in patients with coronary artery disease. However, whether vaspin exerted
The role of vaspin in the development of metabolic and glucose tolerance disorders and atherosclerosis.
Dimova R and Tankova T
BioMed Research International, 823481-823481 (2015)
S Kameshima et al.
Acta physiologica (Oxford, England), 216(2), 203-210 (2015-08-13)
Visceral adipose tissue-derived serine protease inhibitor (vaspin) is an adipocytokine with insulin-sensitizing activity originally identified in visceral adipose tissues of obesity-related type II diabetic rats. We previously showed that vaspin inhibits vascular cell migration and apoptosis as well as inflammatory
Jan Pippel et al.
Biological chemistry, 397(2), 111-123 (2015-11-04)
The adipokine vaspin (serpinA12) is mainly expressed in white adipose tissue and exhibits various beneficial effects on obesity-related processes. Kallikrein 7 is the only known target protease of vaspin and is inhibited by the classical serpin inhibitory mechanism involving a
Association between vaspin level and coronary artery disease in patients with type 2 diabetes.
Hao F
Diabetes Research and Clinical Practice, 113, 26-32 (2016)

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