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Merck

A9024

Sigma-Aldrich

α1-Antitrypsin from human plasma

salt-free, lyophilized powder

Sinónimos:

α1-Proteinase inhibitor

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About This Item

Número de CAS:
Número CE:
Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.77

origen biológico

human plasma

Nivel de calidad

Ensayo

≥70% protein basis (biuret)

Formulario

salt-free, lyophilized powder

Nº de acceso UniProt

temp. de almacenamiento

2-8°C

Información sobre el gen

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Acciones bioquímicas o fisiológicas

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.
Serine protease inhibitor; inhibits trypsin, chymotrypsin and pancreatic and granulocytic elastase, and acrosin. Effective concentration equimolar with proteinase.
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.

Precaución

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.

Nota de preparación

Chromatographically prepared and partially purified.

Cláusula de descargo de responsabilidad

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.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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B Halliwell et al.
FEBS letters, 213(1), 15-17 (1987-03-09)
Ascorbic acid, at physiological concentrations, can scavenge the myeloperoxidase-derived oxidant hypochlorous acid at rates sufficient to protect alpha 1-antiprotease against inactivation by this molecule. The rapid depletion of ascorbic acid at sites of inflammation, as in the inflamed rheumatoid joint
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
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
B M Bany et al.
Biology of reproduction, 47(4), 514-519 (1992-10-01)
The objective of this study was to investigate the uterine uptake of plasma alpha 1-proteinase inhibitor (53,000 Da) and alpha 2-macroglobulin (725,000 Da) from the blood during implantation in the mouse using isotopic methods. The uterine uptake of albumin (67,000
M Reist et al.
FEBS letters, 423(2), 231-234 (1998-03-25)
Sulphite is toxic to the lung and can cause allergic reactions, the most common of which is bronchoconstriction in asthmatics. We show that sulphite can considerably potentiate the inactivation of alpha1-antiproteinase caused by peroxynitrite. Addition of peroxynitrite to sulphite generated

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Protocolos

Thrombin is an endolytic serine protease that selectively cleaves the Arg–Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.

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