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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About This Item
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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
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Mingming Gao et al.
Scientific reports, 9(1), 13427-13427 (2019-09-19)
Obesity and associated metabolic comorbidities represent a growing public health problem. In this study, we demonstrate the use of a newly created fusion gene of exendin-4 and α1-antitrypsin to control obesity and obesity-associated metabolic disorders including insulin resistance, fatty liver
Ronnie Lum et al.
The Journal of biological chemistry, 291(37), 19631-19641 (2016-07-15)
Calreticulin is a lectin chaperone of the endoplasmic reticulum that interacts with newly synthesized glycoproteins by binding to Glc1Man9GlcNAc2 oligosaccharides as well as to the polypeptide chain. In vitro, the latter interaction potently suppresses the aggregation of various non-glycosylated proteins.
James K Stoller et al.
American journal of respiratory and critical care medicine, 185(3), 246-259 (2011-10-01)
α(1)-Antitrypsin (AAT) deficiency is an underrecognized genetic condition that affects approximately 1 in 2,000 to 1 in 5,000 individuals and predisposes to liver disease and early-onset emphysema. AAT is mainly produced in the liver and functions to protect the lung
Joerg Schuettrumpf et al.
Molecular therapy : the journal of the American Society of Gene Therapy, 13(1), 88-97 (2005-10-19)
Identifying factors that influence gene transfer efficacy is critical for a successful gene-based clinical study. Here we demonstrate that in vivo AAV-2-mediated gene transfer is efficiently inhibited by unfractionated heparin, but not by a heparin preparation containing mainly low-molecular-weight forms
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
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