購物車
幫助
021-54845833/15800441009
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Background: |
The carboxy terminus of Hsc70-interacting protein (CHIP, STUB1) is a co-chaperone protein and functional E3 ubiquitin ligase that links the polypeptide binding activity of Hsp70 to the ubiquitin proteasome system. Cytoplasmic CHIP protein contains three 34-amino acid TPR (tetratricopeptide repeat) domains at its amino terminus and a carboxy-terminal U-box domain. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain, while E3 ubiquitin ligase activity is confined to the U-box domain. The binding of CHIP to Hsp70 can stall the folding of Hsp70 client proteins and concomitantly facilitate the U-box dependent ubiquitination of Hsp70-bound substrates. CHIP appears to play a central role in cell stress protection and is responsible for the degradation of disease-related proteins that include cystic fibrosis transmembrane conductance regulator, p53, huntingtin and Ataxin-3, Tau protein, and α-synuclein. |
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Applications: |
WB |
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Name of antibody: |
STUB1 |
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Immunogen: |
Fusion protein of human STUB1 |
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Full name: |
STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase |
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Synonyms： |
STUB1; CHIP; HSPABP2; NY-CO-7; SDCCAG7; UBOX1 |
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SwissProt: |
Q9UNE7 |
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WB Predicted band size: |
35 kDa |
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WB Positive control: |
HeLa, PC12, COS1, COS7 and OVCAR3 cells, muscle and liver tissue |
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WB Recommended dilution: |
500-2000 |
