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G0516

Sigma-Aldrich

α2-hs-Glycoprotein from human plasma

≥90% (SDS-PAGE), lyophilized powder

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MDL number:
NACRES:
NA.61

biological source

human plasma

Quality Level

assay

≥90% (SDS-PAGE)

form

lyophilized powder

technique(s)

electrophoresis: suitable

solubility

H2O: soluble 1 mg protein/mL

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... AHSG(197)

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This Item
A8849F3879G9173
α2-Antiplasmin from human plasma lyophilized powder, ≥5 units/mg protein

A8849

α2-Antiplasmin from human plasma

Fibrinogen from human plasma 50-70% protein (≥80% of protein is clottable)

F3879

Fibrinogen from human plasma

biological source

human plasma

biological source

human plasma

biological source

human plasma

biological source

human plasma

assay

≥90% (SDS-PAGE)

assay

-

assay

-

assay

≥96% (SDS-GE)

form

lyophilized powder

form

lyophilized powder

form

powder

form

lyophilized

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

solubility

H2O: soluble 1 mg protein/mL

solubility

-

solubility

0.9% NaCl: soluble 10 mg/mL

solubility

-

General description

α2-HS glycoprotein (A2HS) is a glycoprotein (molecular weight 49,000) present in human plasma at levels ranging between 40 and 85 mg/dl. A2HS is a major protein component of the bone matrix and could be involved both in mineralization and bone resorption.

Application

Fetuin (α2-HS-glycoprotein) was used to confirm its role in enhancing the suppression of tumor necrosis factor (TNF) release from activated macrophages by CNI-1493. It was also used in 2-dimensional electrophoresis to detect glycosylation and influence spot pattern.

Packaging

Package size based on protein content

Physical form

Lyophilized from 20 mM Tris-HCl, pH 8.0, with 200 mM NaCl

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Customers Also Viewed

J P Lebreton et al.
The Journal of clinical investigation, 64(4), 1118-1129 (1979-10-01)
A nonspecific opsonin function has been ascribed to human alpha 2 HS glycoprotein. Its serum level has been shown to be decreased in trauma patients. Recent studies from this laboratory revealed a heterogeneity among the products obtained in the course
Klemens Löster et al.
Methods in molecular biology (Clifton, N.J.), 446, 199-214 (2008-04-01)
The detailed characterization of complex protein mixtures as in samples from biological sources cannot be sufficiently performed by separation of polypeptides according to their molecular weight as is done by conventional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) (1DE). For analysis
H Wang et al.
Proceedings of the National Academy of Sciences of the United States of America, 95(24), 14429-14434 (1998-11-25)
Macrophages become activated by bacterial endotoxin (lipopolysaccharide) and other stimuli to release proinflammatory cytokines and NO. To prevent release of toxic or potentially lethal quantities of these factors, the state of macrophage activation is counter-regulated by anti-inflammatory mediators (e.g., glucocorticoid
B Boutin et al.
American journal of human genetics, 37(6), 1098-1105 (1985-11-01)
The genetic polymorphism of human alpha 2-HS glycoprotein was studied by ultrathin-layer isoelectric focusing in a pH range 4.2-4.9 followed by immunoblotting using antisera specific for the protein. Three common phenotypes, HSGA1-1, HSGA2-2, and HSGA1-2, were easily recognized using this
Hanane Moustaoui et al.
Nanoscale, 11(8), 3665-3673 (2019-02-12)
The study of protein interactions with gold nanoparticles (GNP) is a key step prior to any biomedical application. These interactions depend on many GNP parameters such as size, surface charge, chemistry, and shape. In this work, we propose to use

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