C5617
Anti-CHIP antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-Carboxyl terminus of hsc70-interacting protein
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About This Item
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.
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
Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (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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