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Key Documents

SAB4200198

Sigma-Aldrich

Anti-Alpha-1-Antitrypsin (AAT) antibody,Mouse monoclonal

clone 1C2, purified from hybridoma cell culture

Sinonimo/i:

Anti-A1A, Anti-A1AT, Anti-AAT, Anti-Alpha-1 protease inhibitor, Anti-Alpha-1-antiproteinase, Anti-Alpha-1-antitrypsin, Anti-PI1, Anti-Protease inhibitor 1 (anti-elastase), Anti-SERPINA1, Anti-Serpin peptidase inhibitor, clade A, member 1

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.43

Origine biologica

mouse

Coniugato

unconjugated

Forma dell’anticorpo

purified from hybridoma cell culture

Tipo di anticorpo

primary antibodies

Clone

1C2, monoclonal

Forma fisica

buffered aqueous solution

PM

antigen ~45 kDa

Reattività contro le specie

human

Concentrazione

~1.0 mg/mL

tecniche

western blot: 1-2 μg/mL using whole extracts of human HepG2 cells

Isotipo

IgG2b

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... SERPINA1(5265)

Descrizione generale

Monoclonal Anti-Alpha-1-Antitrypsin (AAT) (mouse IgG2b isotype) is derived from the hybridoma 1C2 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a human AAT recombinant protein. Alpha-1-Antitrypsin (AAT), also named SERPINA1 (serine proteinase inhibitor, clade a, member 1), is a member of the protease inhibitor (serpin) family. It is encoded by the gene SERPINA1. AAT is a glycoprotein synthesized mainly in the liver and secreted to the bloodstream. This gene consists of four coding exons (II, III, IV, and V) and three untranslated exons (Ia, Ib, and Ic) in the 5′ region and six introns.

Immunogeno

human AAT recombinant protein

Applicazioni

Monoclonal Anti-Alpha-1-Antitrypsin (AAT) antibody has been used in immunoblotting and microarray.

Azioni biochim/fisiol

Serpin peptidase inhibitor clade a member 1 (SerpinA1) is considered as a biomarker for the progression of cutaneous squamous cell carcinoma. It serves as an effective inhibitor of neutrophil elastase. AAT is a major serine protease inhibitor whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Through circulation AAT reaches the lungs where it blocks the effects of neutrophil elastase. Defects in this gene can cause emphysema or liver disease.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Codice della classe di stoccaggio

10 - Combustible liquids

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Identification and characterization of eight novel SERPINA1 Null mutations
Ferrarotti I, et al.
Orphanet Journal of Rare Diseases, 9(1), 172-172 (2014)
Chen Lu et al.
Journal of visualized experiments : JoVE, (63), e3791-e3791 (2012-05-17)
In this study, we describe an effective protocol for use in a multiplexed high-throughput antibody microarray with glycan binding protein detection that allows for the glycosylation profiling of specific proteins. Glycosylation of proteins is the most prevalent post-translational modification found
Sequencing Alpha-1 MZ Individuals Shows Frequent Biallelic Mutations
Foil KE, et al.
Pulmonary medicine, 2018 (2018)
Serpin peptidase inhibitor clade A member 1 (SerpinA1) is a novel biomarker for progression of cutaneous squamous cell carcinoma
Farshchian M, et al.
The American Journal of Pathology, 179(3), 1110-1119 (2011)
Elena Plessa et al.
Nature communications, 12(1), 6447-6447 (2021-11-10)
During biosynthesis, proteins can begin folding co-translationally to acquire their biologically-active structures. Folding, however, is an imperfect process and in many cases misfolding results in disease. Less is understood of how misfolding begins during biosynthesis. The human protein, alpha-1-antitrypsin (AAT)

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