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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.

Q8IW75

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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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
Vaspin as a Prognostic Marker in Patients with Acute Myocardial Infarction.
Zhang B
Heart, Lung & Circulation, 25(3), 257-264 (2016)
Vaspin: a novel adipokine, member of the family of serine protease inhibitors
Ekaterini Koiou
Aristotle University Medical Journal, 38.3, 7-18 (2011)
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
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