P1874
Anti-Polyglutamines antibody, Mouse monoclonal
~2 mg/mL, clone 3B5H10, purified from hybridoma cell culture
Synonym(s):
Anti-Huntingtin
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About This Item
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biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified from hybridoma cell culture
antibody product type
primary antibodies
clone
3B5H10, monoclonal
form
buffered aqueous solution
species reactivity
human
packaging
antibody small pack of 25 μL
concentration
~2 mg/mL
technique(s)
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: 1-2 μg/mL using extract of HEK-293T cells transfected with an N-terminal 171 amino acid fragment of human Huntingtin with a 68 glutamine stretch
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... HTT(3064)
Related Categories
General description
Abnormal stretch of triplet CAG (or CAA) codon produces a homomeric repeat of glutamine residues beyond the critical threshold and will lead to neurodegenerative disease. Monoclonal mouse anti-polyglutamine antibody can be used to detect poly Q protein expression and in western blot. Monoclonal anti-polyglutamines antibody reacts specifically to homomeric polyglutamines independent of the species.
Immunogen
GST-human Huntingtin (N-terminal fragment of 171 amino acids containing 65Q).
Application
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)
Monoclonal anti-polyglutamines antibody may be used for ELISA, immunoblot and slot blot. It can also be used in immunoprecipitation and immunocytochemistry.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Legal Information
This product is for in vitro use only. It is not to be used for commercial purposes. Use of this product to produce products for sale or for diagnostic, therapeutic or drug discovery purposes is prohibited. In order to obtain a license to use this product for commercial purposes, contact the Regents of the University of California. This product is sold under license to U.S. Patent No. 6,291,652, owned by the Regents of the University of California.
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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recommended
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Nicholas R Franich et al.
Journal of neuroscience research, 97(12), 1590-1605 (2019-07-10)
Huntington's disease (HD) is a progressive neurodegenerative disorder caused by an expanded CAG repeat within the huntingtin (HTT) gene. The Q140 and HdhQ150 knock-in HD mouse models were generated such that HdhQ150 mice have an expanded CAG repeat inserted into
Xuan Zhang et al.
Cellular and molecular neurobiology, 36(3), 459-470 (2016-03-10)
In Huntington's disease (HD) the imperfect expanded CAG repeat in the first exon of the HTT gene leads to the generation of a polyglutamine (polyQ) protein, which has some neuronal toxicity, potentially mollified by formation of aggregates. Accumulated research, reviewed
Veena Prahlad et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(34), 14204-14209 (2011-08-17)
The consequence of chronic protein misfolding is the basis of many human diseases. To combat the deleterious effects of accumulated protein damage, all cells possess robust quality-control systems, specifically molecular chaperones and clearance machineries, that sense and respond to protein
Elizabeth Brooks et al.
Methods in molecular biology (Clifton, N.J.), 277, 103-128 (2004-06-18)
Expansion of a homomeric stretch of glutamine residues beyond a critical threshold can produce neurodegenerative disease. This observation led to the idea that abnormal polyglutamine stretches can alter protein structure in ways that contribute to disease. Because they are prone
Amy L Lee et al.
PloS one, 12(3), e0173644-e0173644 (2017-03-11)
Expanded polyglutamine repeats in different proteins are the known determinants of at least nine progressive neurodegenerative disorders whose symptoms include cognitive and motor impairment that worsen as patients age. One such disorder is Huntington's Disease (HD) that is caused by
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