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: Also Known As: Catalog No.: Size: Molecular Weight: Species: Source: Stock: Concentration: Quality Assurance: Storage: PDF Data Sheet: NCBI RefSeq: Image(s): Shipping Method: References:

6xHis-CHIP

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

K1200

50 µg

34.9 kDa

Human

Bacterial recombinant

20 mM Tris, 150 mM NaCl, 2 mM βME, 10% Glycerol

See tube label

~95% by SDS-PAGE, see datasheet for gel image

Store at -80°C; avoid multiple freeze-thaw cycles

PDF Datasheet， MSDS

NM_005861

(Click image to enlarge)

Coomassie-stained SDS-PAGELane 1: Molecular weight markersLane 2: 5 µg purified 6xHis-CHIP

Dry ice shipping

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-PAGELane 1: Molecular weight markersLane 2: 5 µg purified 6xHis-CHIP

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