A0409
Anti-α1-Antitrypsin antibody produced in rabbit
IgG fraction of antiserum
Synonym(s):
Alpha 1 Antitrypsin Antibody, Alpha 1 Antitrypsin Antibody - Anti-α1-Antitrypsin antibody produced in rabbit, anti-A1AT
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
mol wt
antigen ~50 kDa
species reactivity
human
packaging
vial of 2 mL lyophilized antiserum
technique(s)
immunoelectrophoresis: suitable
indirect ELISA: 1:30,000-1:60,000
UniProt accession no.
storage temp.
2-8°C
target post-translational modification
unmodified
Gene Information
human ... SERPINA1(5265)
General description
α-1-antitrypsin belongs to the serpin family and is a strong serine protease inhibitor. Its pivotal role is to protect lower respiratory tract against proteolytic destruction by human leukocyte elastase. Mutation in AAT gene will reduce the serum concentration of α-1-antitrypsin and hence increase the risk of emphysema. Anti-α1-antitrypsin antibody (diluted 1:9000) can be used as a capture antibody for determination of transgene expressions levels. It can also be used in immunoelectrophoresis. Rabbit anti-α1-antitrypsin antibody reacts specifically with α1-antitrypsin of human.
Immunogen
Purified human α-1-antitrypsin
Application
Anti-α1-antitrypsin antibody (diluted 1: 1000) can be used in ELISA. It can also be used for probing immunoblots to identify A1AT. Additionally, it can be used in Ouchterlony double diffusion.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Rabbit anti-α1-antitrypsin antibody can also be used in immunoelectrophoretic techniques.
Physical form
Lyophilized from 0.01 M phosphate buffered saline, pH 7.2.
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 Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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U Schmidt et al.
Cellular microbiology, 1(1), 61-67 (2001-02-24)
The acute-phase response is an immediate reaction of the host against invading microorganisms. We show here that oligodeoxynucleotides (ODNs) containing a CpG motif rapidly induce the major murine acute-phase proteins in vivo, i.e. serum amyloid A (SAA) and serum amyloid
Pedro E Cruz et al.
Laboratory investigation; a journal of technical methods and pathology, 87(9), 893-902 (2007-06-27)
alpha-1 Antitrypsin (AAT) deficiency is one of the most common genetic diseases in North America, with a carrier frequency of approximately 4% in the US population. Homozygosity for the most common mutation (Glu342Lys, PI(*)Z) leads to the synthesis of a
Joseph E Chambers et al.
Science advances, 8(14), eabm2094-eabm2094 (2022-04-09)
Misfolding of secretory proteins in the endoplasmic reticulum (ER) features in many human diseases. In α1-antitrypsin deficiency, the pathogenic Z variant aberrantly assembles into polymers in the hepatocyte ER, leading to cirrhosis. We show that α1-antitrypsin polymers undergo a liquid:solid
Katarina Hajdin et al.
PloS one, 5(5), e10445-e10445 (2010-05-11)
Rhabdomyosarcoma (RMS) is the most common soft tissue sarcoma in children. Improvement of treatment efficacy and decreased side effects through tumor-targeted drug delivery would be desirable. By panning with a phage-displayed cyclic random peptide library we selected a peptide with
M A Niemann et al.
Matrix (Stuttgart, Germany), 12(3), 233-241 (1992-06-01)
alpha 1-Antitrypsin (AAT) is a potent fluid-phase inhibitor of serine proteases. It forms a tightly bound, stoichiometric complex with these enzymes and is inactivated by cleavage within its reactive center. Evidence is here presented, that the 44-residue C-terminal fragment of
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