6xHis-CHIP

The carboxyl terminus of Hsc70-interacting protein (CHIP) is an E3 ubiquitin ligase. CHIP contains two domains, one is its TPR domain on the amino terminus and the other is its U-box domain on the carboxyl terminus. The TPR domain recognizes the chaperones, Hsp70 and Hsp90. While the U-box domain carries out its ubiquitin ligase activity. CHIP often ubiquitinates misfolded proteins bound on the chaperones.

Additional Information

Product Name: 6xHis-CHIP
Also Known As: STUB1; UBOX1; HSPABP2; NY-CO-7; SDCCAG7
Catalog No.: K1201
Size: 250 µg
Molecular Weight: 34.9 kDa
Species: Human
Source: Bacterial recombinant
Stock: 20 mM Tris, 150 mM NaCl, 2 mM βME, 10% Glycerol
Concentration: See tube label
Quality Assurance: ~95% by SDS-PAGE, see datasheet for gel image
Storage: Store at -80°C; avoid multiple freeze-thaw cycles
PDF Data Sheet: PDF DatasheetMSDS
NCBI RefSeq: NM_005861
Image(s): (Click image to enlarge)

Coomassie-stained SDS-PAGE
Lane 1: Molecular weight markers
Lane 2: 5 µg purified 6xHis-CHIP
Shipping Method: Dry ice shipping
References: 1. Ballinger CA, et al. (1999) Mol Cell Biol 19(6), 4535 – 4545.
2. Murata S, et al. (2003) Int J Biochem Cell Biol 35(5), 572 – 578.

Details

The carboxyl terminus of Hsc70-interacting protein (CHIP) is an E3 ubiquitin ligase. CHIP contains two domains, one is its TPR domain on the amino terminus and the other is its U-box domain on the carboxyl terminus. The TPR domain recognizes the chaperones, Hsp70 and Hsp90. While the U-box domain carries out its ubiquitin ligase activity. CHIP often ubiquitinates misfolded proteins bound on the chaperones.

Images:
(Click image to enlarge)

Coomassie-stained SDS-PAGE
Lane 1: Molecular weight markers
Lane 2: 5 µg purified 6xHis-CHIP