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SAB4200198

Sigma-Aldrich

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

clone 1C2, purified from hybridoma cell culture

Sinônimo(s):

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

Número MDL:
MFCD00162392
Código UNSPSC:
12352203
NACRES:
NA.43

fonte biológica

mouse

conjugado

unconjugated

forma do anticorpo

purified from hybridoma cell culture

tipo de produto de anticorpo

primary antibodies

clone

1C2, monoclonal

Formulário

buffered aqueous solution

peso molecular

antigen ~45 kDa

reatividade de espécies

human

concentração

~1.0 mg/mL

técnica(s)

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

Isotipo

IgG2b

nº de adesão UniProt

P01009

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... SERPINA1(5265)

Descrição geral

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.

Imunogênio

human AAT recombinant protein

Aplicação

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

Ações bioquímicas/fisiológicas

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.

forma física

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

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

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Certificados de análise (COA)

Lot/Batch Number
049M4772V
070M4781
078M4852V

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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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