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Key Documents

A6150

Sigma-Aldrich

α1-Antitrypsin from human plasma

salt-free, lyophilized powder

Synonym(s):

α1-Proteinase inhibitor

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.77

biological source

human plasma

Quality Level

form

salt-free, lyophilized powder

concentration

≥60% (biuret)

technique(s)

inhibition assay: suitable

UniProt accession no.

storage temp.

2-8°C

Gene Information

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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.
≤10 mg will inhibit 1.0 mg of trypsin with activity of 10,000 BAEE units per mg protein. ≤10 mg will inhibit approx. 1.0 mg of ·α-chymotrypsin with activity of 40-50 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


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Tian-Hui Yang et al.
Journal of immunology (Baltimore, Md. : 1950), 201(5), 1389-1399 (2018-07-20)
Proteinase 3 (P3), a serine protease expressed by myeloid cells, localized within azurophil granules, and also expressed on the cellular membrane of polymorphonuclear neutrophils (PMN), is the target of autoimmunity in granulomatosis with polyangiitis. PR1, an HLA-A2 restricted nonameric peptide
Cynthia L Bristow et al.
Journal of immunology (Baltimore, Md. : 1950), 180(1), 492-499 (2007-12-22)
To identify positive or negative factors for HIV-1 infectivity, clones from the U937 promonocytic cell line that express similar levels of CD4 and CXCR4, but differ in HIV-1 susceptibility, were compared. In contrast to HIV-1 permissive clone 10 (plus), nonpermissive
Kathirvel Alagesan et al.
Analytical and bioanalytical chemistry, 409(2), 529-538 (2016-12-03)
Glycopeptide enrichment is a crucial step in glycoproteomics for which hydrophilic interaction chromatography (HILIC) has extensively been applied due to its low bias towards different glycan types. A systematic evaluation of applicable HILIC mobile phases on glycopeptide enrichment efficiency and
Ekaterina Mindel et al.
Journal of neuroscience research, 99(3), 966-976 (2020-12-10)
Many coagulation factor proteases are increased in the brain during ischemic stroke. One of these proteases is plasmin. In this study we established a novel method for direct quantitative measurement of plasmin activity in male mouse brain slices using a
C M de Bont et al.
Clinical and experimental immunology, 199(1), 1-8 (2019-10-30)
Neutrophils can form neutrophil extracellular traps (NETs) to capture microbes and facilitate their clearance. NETs consist of decondensed chromatin decorated with anti-microbial proteins. Here, we describe the effect of neutrophil proteases on the protein content of NETs. We show that

Articles

Enzyme Explorer Product Application Index for Elastase. Leukocyte elastase is a 29KDa serine endoprotease of the Proteinase S1 Family. It exists as a single 238 amino acid-peptide chain with four disulfide bonds.

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

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Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

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