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Key Documents

P1874

Sigma-Aldrich

Anti-Polyglutamines antibody, Mouse monoclonal

~2 mg/mL, clone 3B5H10, purified from hybridoma cell culture

Synonyma:

Anti-Huntingtin

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

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)

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)
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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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Navštívit knihovnu dokumentů

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
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
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
Caspase-6 does not contribute to the proteolysis of mutant huntingtin in the HdhQ150 knock-in mouse model of Huntington's disease.
Christian Landles et al.
PLoS currents, 4, e4fd085bfc9973-e4fd085bfc9973 (2012-08-25)
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

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