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Merck

SAB4200198

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

clone 1C2, purified from hybridoma cell culture

Synonym(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

UNSPSC Code:
12352203
NACRES:
NA.43
MDL number:
MFCD00162392
Conjugate:
unconjugated
Clone:
1C2, monoclonal
Application:
WB
Citations:
7

Key Documents

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biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

1C2, monoclonal

form

buffered aqueous solution

mol wt

antigen ~45 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

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

isotype

IgG2b

UniProt accession no.

P01009

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SERPINA1(5265)

General description

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.

Immunogen

human AAT recombinant protein

Application

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000439639
0000439639
0000415589
0000415589
0000340632

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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)
Sequencing Alpha-1 MZ Individuals Shows Frequent Biallelic Mutations
Foil KE, et al.
Pulmonary medicine, 2018 (2018)
Chemically-blocked antibody microarray for multiplexed high-throughput profiling of specific protein glycosylation in complex samples
Lu C, et al.
Journal of Visualized Experiments, (63), e3791-e3791 (2012)
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)
Identification and characterization of eight novel SERPINA1 Null mutations
Ferrarotti I, et al.
Orphanet Journal of Rare Diseases, 9(1), 172-172 (2014)
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