U box domain E3 ubiquitin ligase. CHIP E3 controls both the association of Hsp70/Hsp90 chaperones with ErbB2 and the down-regulation of ErbB2 induced by inhibitors of Hsp90. CHIP-induced degradation was observed for mutant and wild-type p53, which transiently associate with molecular chaperones Hsc70 and Hsp90 and can be diverted onto a degradation pathway through this association. Also, CHIP can interact with the Smad1/Smad4 proteins and block BMP signal transduction through the ubiquitin-mediated degradation of Smad proteins.
Immunogen
Peptide with sequence DAFISENGWVEDY, from the C-terminus of the protein sequence according to NP_005852.
Application
This Anti-CHIP/STUB1 Antibody is validated for use in ELISA, WB for the detection of CHIP/STUB1.
Physical form
Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin.
Analysis Note
Control Positive Control: Highly expressed in brain, heart, skelatal muscle, pancreas and placenta. Weak expression in kidney, liver and lung.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Chembiochem : a European journal of chemical biology, 23(6), e202100633-e202100633 (2022-01-22)
The ubiquitin ligase C-terminus of Hsc70 interacting protein (CHIP) is an important regulator of proteostasis. Despite playing an important role in maintaining proteostasis, little progress has been made in developing small molecules that regulate ubiquitin transfer by CHIP. Here we
The Journal of biological chemistry, 293(8), 2735-2743 (2018-01-11)
The accumulation of misfolded proteins promotes protein aggregation and neuronal death in many neurodegenerative diseases. To counteract misfolded protein accumulation, neurons have pathways that recognize and refold or degrade aggregation-prone proteins. One U-box-containing E3 ligase, C terminus of Hsc70-interacting protein
Cell biochemistry and function, 31(8), 724-735 (2013-04-05)
The carboxyl terminus of Hsp70-interacting protein (CHIP) is a ubiquitin ligase/cochaperone critical for the maintenance of cardiac function. Mice lacking CHIP (CHIP-/-) suffer decreased survival, enhanced myocardial injury and increased arrhythmias compared with wild-type controls following challenge with cardiac ischaemia
American journal of cancer research, 7(9), 1948-1958 (2017-10-06)
Cancer cachexia is a severe wasting syndrome characterized by the progressive loss of lean body mass and systemic inflammation. Up to 80% of cancer patients experience cachexia, with 20-30% of cancer-related deaths directly linked to cachexia. Despite efforts to identify
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