兔抗STUB1多克隆抗体

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.

Applications:

WB

Name of antibody:

STUB1

Immunogen:

Fusion protein of human STUB1

Full name:

STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase

Synonyms：

STUB1; CHIP; HSPABP2; NY-CO-7; SDCCAG7; UBOX1

SwissProt:

Q9UNE7

WB Predicted band size:

35 kDa

WB Positive control:

HeLa, PC12, COS1, COS7 and OVCAR3 cells, muscle and liver tissue

WB Recommended dilution:

500-2000