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Merck

C5617

Sigma-Aldrich

Anti-CHIP antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(e):

Anti-Carboxyl terminus of hsc70-interacting protein

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

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

Speziesreaktivität

human

Methode(n)

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

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... STUB1(10273)

Allgemeine Beschreibung

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.

Immunogen

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

Biochem./physiol. Wirkung

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.

Physikalische Form

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.

Haftungsausschluss

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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Antikörper

Produkt-Nr.
Beschreibung
Preisangaben

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

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


Analysenzertifikate (COA)

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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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