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Key Documents

P1874

Sigma-Aldrich

Anti-Polyglutamines antibody, Mouse monoclonal

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

Synonyme(s) :

Anti-Huntingtin

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified from hybridoma cell culture

Type de produit anticorps

primary antibodies

Clone

3B5H10, monoclonal

Forme

buffered aqueous solution

Espèces réactives

human

Conditionnement

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... HTT(3064)

Description générale

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.

Immunogène

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.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Informations légales

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.

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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
Jennifer L Wacker et al.
Nature structural & molecular biology, 11(12), 1215-1222 (2004-11-16)
Protein conformational changes that result in misfolding, aggregation and amyloid fibril formation are a common feature of many neurodegenerative disorders. Studies with beta-amyloid (Abeta), alpha-synuclein and other amyloid-forming proteins indicate that the assembly of misfolded protein conformers into fibrils is
Kirupa Sathasivam et al.
Human molecular genetics, 19(1), 65-78 (2009-10-15)
Huntington's disease (HD) is a late-onset neurodegenerative disorder that is characterized neuropathologically by the presence of neuropil aggregates and nuclear inclusions. However, the profile of aggregate structures that are present in the brains of HD patients or of HD mouse
Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer.
Wacker JL, Zareie MH
Nature Structural and Molecular Biology, 11(12), 1215-1222 (2001)
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

Articles

Huntington's disease (HD) is an autosomal dominant, late-onset neurodegenerative disorder characterized by a selective neuronal cell death in the cortex and striatum leading to cognitive dysfunction, motor impairment and behavioral changes.

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