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Key Documents

SAB1300354

Sigma-Aldrich

Anti-CHIP (STUB1) (C-term) antibody produced in rabbit

saturated ammonium sulfate (SAS) precipitated, buffered aqueous solution

Synonym(s):

Anti-CLL-associated antigen KW-8, Anti-Carboxy terminus of HSP70-interacting protein, Anti-STIP1 homology and U-Box containing protein 1, Anti-STUB1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

saturated ammonium sulfate (SAS) precipitated

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

immunohistochemistry: 1:50-1:100
indirect ELISA: 1:1000
western blot: 1:100-1:500

NCBI accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... CHIP(10273)

General description

CHIP (C-terminus of HSP70-interacting protein) gene is located in human chromosome 16p13.3. This gene codes for a E3 ubiquitin ligase. The bioactive site of the protein includes three tandem repeats of the tetratricopeptide motif at the N-terminal, a C-terminal U-box domain and a charged coiled-coil region in between the two. CHIP is ubiquitously expressed.
CHIP is an E3 ligase for nNOS whose action is facilitated by (and possibly requires) its interaction with nNOS-bound hsp70. Co-chaperone CHIP, possibly with another E3 ligase(s), modulates the ubiquitylation of mutant Cu/Zn-superoxide dismutase and renders them more susceptible for proteasomal degradation. CHIP functions as a negative regulator of AR transcriptional activity by promoting AR degradation. CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. CHIP can interact with the Smad1/Smad4 proteins and block BMP signal transduction through the ubiquitin-mediated degradation of Smad proteins. CHIP E3 controls both the association of Hsp70/Hsp90 chaperones with ErbB2 and the down-regulation of ErbB2 induced by inhibitors of Hsp90. CHIP is associated with Parkin and enhances its ubiquitin ligase activity related to Parkinson′s disease.

Immunogen

CHIP (Q969U2, 208-242)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide at the C-term of human CHIP (STUB1).

Biochem/physiol Actions

CHIP (C-terminus of HSP70-interacting protein) induces ubiquitination and proteasomal degradation of proteins sent by chaperone partners for removal via endocytic-lysosomal machinery. CHIP interacts with molecular chaperones and degradation machineries to maintain protein homeostasis within the cell. Lack of CHIP increases the process of aging, indicating that the gene might mediate long living. CHIP prevents the accumulation of protein aggregates in age-related disease conditions. CHIP is responsible for the degradation of CD166, a cancer stem-like cell (CSC) marker in head and neck cancer. Therefore, CHIP is suggested as an option for the diagnosis of head and neck cancer.

Physical form

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) 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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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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Identification of CHIP as a novel causative gene for autosomal recessive cerebellar ataxia.
Shi Y
PLoS ONE, 101, 236-244 (2013)
The Ubiquitin Ligase CHIP Integrates Proteostasis and Aging by Regulation of Insulin Receptor Turnover.
Tawo R
Cell, 169(3), 470-482 (2017)
Cancer stem-like cell related protein CD166 degrades through E3 ubiquitin ligase CHIP in head and neck cancer.
Xiao M
Experimental Cell Research, 353(1), 46-53 (2017)
BAG2 Interferes with CHIP-Mediated Ubiquitination of HSP72.
Schonbuhler B
International Journal of Molecular Sciences, 18(1), 1-10 (2016)
Molecular Chaperone HSP90 Is Necessary to Prevent Cellular Senescence via Lysosomal Degradation of p14ARF.
Han SY
Cancer Research, 77(2), 343-354 (2017)

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