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A9024

Sigma-Aldrich

α1-Antitrypsin from human plasma

salt-free, lyophilized powder

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Synonym(s):
α1-Proteinase inhibitor
CAS Number:
9041-92-3
EC Number:
232-924-7
MDL number:
MFCD00130469
NACRES:
NA.77

biological source

human plasma

Quality Level

200

Assay

≥70% protein basis (biuret)

form

salt-free, lyophilized powder

UniProt accession no.

P01009
P08246

storage temp.

2-8°C

Gene Information

human ... ELA2(1991) , SERPINA1(5265)

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Biochem/physiol Actions

Serine protease inhibitor; inhibits trypsin, chymotrypsin and pancreatic and granulocytic elastase, and acrosin. Effective concentration equimolar with proteinase.The effects of hereditary α1-antitrypsin deficiency and certain autoimmune states result from uncontrolled proteolysis in vivo. Direct α1-antitrypsin replacement therapy has shown promise in animal models of Type 1 diabetes.
1-4 mg will inhibit 1.0 mg of trypsin with activity of approx. 10,000 BAEE units per mg protein. 1-6 mg will inhibit 1.0 mg of α-chymotrypsin with activity of >=40 BTEE units per mg protein.

Caution

Aqueous stock solutions containing 0.01% NaN3 are stable for several months. Solutions can be stored at −80 °C, but should not be refrozen. Unstable below pH 5.5. Inactivated by some non-serine proteinases and by oxidation of active site methionine residue.

Preparation Note

Chromatographically prepared and partially purified.

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

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  5. What is the carbohydrate content of human alpha-1-Antitrypsin?

    We have found the information on alpha-1-antitrypsin in a reference book:The Plasma Proteins, F.W. Putnam, ed, volume 2, chapter 4, Table II.The alpha-1-antitrypsin is 12 percent carbohydrate, citing K. Heide and H.G. Schwick, Chemistry and Significance of the Carbohydrate Moieties of Human Serum Glycoproteins, Angew. Chem., Int. Ed. Eng., 12, 721-733 (1973).The table also gives information on the percentage of each type of monosaccharide that is present.

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M Wasil et al.
The Biochemical journal, 243(3), 867-870 (1987-05-01)
Thiourea and dimethylthiourea are powerful scavengers of hydroxyl radicals (.OH), and dimethylthiourea has been used to test the involvement of .OH in several animal models of human disease. It is shown that both thiourea and dimethylthiourea are scavengers of HOCl
O I Aruoma et al.
The Biochemical journal, 264(3), 863-869 (1989-12-15)
Carnosine, homocarnosine and anserine have been proposed to act as antioxidants in vivo. Our studies show that all three compounds are good scavengers of the hydroxyl radical (.OH) but that none of them can react with superoxide radical, hydrogen peroxide
O I Aruoma et al.
The Biochemical journal, 256(1), 251-255 (1988-11-15)
It has been suggested that taurine, hypotaurine and their metabolic precursors (cysteic acid, cysteamine and cysteinesulphinic acid) might act as antioxidants in vivo. The rates of their reactions with the biologically important oxidants hydroxyl radical (.OH), superoxide radical (O2.-), hydrogen
O I Aruoma et al.
FEBS letters, 244(1), 76-80 (1989-02-13)
The elastase-inhibitory activity of alpha 1-antiproteinase is inactivated by hydroxyl radicals (.OH) generated by pulse radiolysis or by reaction of iron ions with H2O2 in the presence of superoxide or ascorbate. Uric acid did not protect alpha 1-antiproteinase against inactivation
Roy B Lefkowitz et al.
Analytical chemistry, 82(19), 8251-8258 (2010-09-11)
The ability to measure protease activity in the blood is important for the development of future diagnostics and for biomedical research. Presently, protease assays require sample preparation, making them time-consuming, costly, less accurate, and unsuitable for point-of-care (POC) diagnostics. Recently
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