SAB4200198
Anti-Alpha-1-Antitrypsin (AAT) antibody,Mouse monoclonal
clone 1C2, purified from hybridoma cell culture
동의어(들):
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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모든 사진(1)
About This Item
추천 제품
생물학적 소스
mouse
결합
unconjugated
항체 형태
purified from hybridoma cell culture
항체 생산 유형
primary antibodies
클론
1C2, monoclonal
양식
buffered aqueous solution
분자량
antigen ~45 kDa
종 반응성
human
농도
~1.0 mg/mL
기술
western blot: 1-2 μg/mL using whole extracts of human HepG2 cells
동형
IgG2b
UniProt 수납 번호
배송 상태
dry ice
저장 온도
−20°C
타겟 번역 후 변형
unmodified
유전자 정보
human ... SERPINA1(5265)
일반 설명
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.
면역원
human AAT recombinant protein
애플리케이션
Monoclonal Anti-Alpha-1-Antitrypsin (AAT) antibody has been used in immunoblotting and microarray.
생화학적/생리학적 작용
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.
물리적 형태
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
면책조항
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 Code
10 - Combustible liquids
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
가장 최신 버전 중 하나를 선택하세요:
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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