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Merck

A0409

Sigma-Aldrich

Anti-α1-Antitrypsin antibody produced in rabbit

IgG fraction of antiserum

Sinónimos:

Alpha 1 Antitrypsin Antibody, Alpha 1 Antitrypsin Antibody - Anti-α1-Antitrypsin antibody produced in rabbit, anti-A1AT

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

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)
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


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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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