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Key Documents

C5617

Sigma-Aldrich

Anti-CHIP antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-Carboxyl terminus of hsc70-interacting protein

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About This Item

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

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 35 kDa (also non-specific band at ~85 kDa)

Espèces réactives

human

Technique(s)

western blot: 1 μg/mL using using COS-1 cells overexpressing the human gene

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 ... STUB1(10273)

Description générale

CHIP (carboxyl terminus of hsc70-interacting protein) is a cytoplasmic protein has a molar mass of 35kDa. It is expressed predominantly in striated muscle in vivo and brain. It contains a U-box domain that is a modified RING finder domain for recruiting E2 ubiquitinating enzymes, a coiled-coil region, and three TPR (tetratricopeptide) domains that interact with the heat-shock proteins HSP70 and HSP90. The gene encoding this protein is referred to as STUB1 (STIP1 homology and U-box containing protein 1) and is mapped to human chromosome 16p13.3.

Immunogène

synthetic peptide V(218)DEKRKKRDIPDYLC(232) corresponding to amino acid residues 218-232 from human CHIP.

Actions biochimiques/physiologiques

CHIP (carboxyl terminus of hsc70-interacting protein) is an interacting partner of the constitutive form of hsc70 and the stress inducible form of hsp70. It participates in the ubiquitin-proteasome system. It functions as a E3 ubiquitin-ligase up on binding to hsc70 and hsp90 and ubiquitylates unfolded protein. Mutations in this gene have been linked to spinocerebellar ataxia.

Forme physique

Provided as 100 μg of affinity purified IgG (1 mg/mL) in phosphate buffered saline containing 1 mg/mL bovine serum albumin and 0.05% sodium azide.

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

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Consulter la Bibliothèque de documents

Chantal Depondt et al.
Neurology, 82(19), 1749-1750 (2014-04-11)
Autosomal recessive ataxias affect about 1 person in 20,000. Friedreich ataxia accounts for one-third of the cases in Caucasians; the others are due to a growing list of very rare molecular defects, including mild forms of metabolic diseases. In nearly
S Murata et al.
EMBO reports, 2(12), 1133-1138 (2001-12-18)
The ubiquitin-proteasome system catalyses the immediate destruction of misfolded or impaired proteins generated in cells, but how this proteolytic machinery recognizes abnormality of cellular proteins for selective elimination remains elusive. Here, we report that the C-terminus of Hsc70-interacting protein (CHIP)
F Bertucci et al.
Oncogene, 27(40), 5359-5372 (2008-05-21)
Invasive ductal carcinomas (IDCs) and invasive lobular carcinomas (ILCs) are the two major pathological types of breast cancer. Epidemiological and histoclinical data suggest biological differences, but little is known about the molecular alterations involved in ILCs. We undertook a comparative
C A Ballinger et al.
Molecular and cellular biology, 19(6), 4535-4545 (1999-05-18)
The chaperone function of the mammalian 70-kDa heat shock proteins Hsc70 and Hsp70 is modulated by physical interactions with four previously identified chaperone cofactors: Hsp40, BAG-1, the Hsc70-interacting protein Hip, and the Hsc70-Hsp90-organizing protein Hop. Hip and Hop interact with
Amelia B Karlsson et al.
Molecular biology of the cell, 25(8), 1355-1365 (2014-02-14)
Troyer syndrome is an autosomal recessive hereditary spastic paraplegia (HSP) caused by frameshift mutations in the SPG20 gene that results in a lack of expression of the truncated protein. Spartin is a multifunctional protein, yet only two conserved domains--a microtubule-interacting

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