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C5617

Sigma-Aldrich

Anti-CHIP antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-Carboxyl terminus of hsc70-interacting protein

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About This Item

MDL number:
MFCD02262541
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

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

species reactivity

human

technique(s)

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

UniProt accession no.

Q9UNE7

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... STUB1(10273)

General description

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 Actions

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.

Physical 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.

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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Antibody

Referencia del producto
Descripción
Precios

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

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Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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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