Anti-CHIP antibody produced in rabbit

CHIP (carboxyl terminus of hsc70-interacting protein) is a cytoplasmic protein has a molar mass of 35kDa. It is expressed predominantly in striated muscle in vivo and brain. It contains a U-box domain that is a modified RING finder domain for recruiting E2 ubiquitinating enzymes, a coiled-coil region, and three TPR (tetratricopeptide) domains that interact with the heat-shock proteins HSP70 and HSP90. The gene encoding this protein is referred to as STUB1 (STIP1 homology and U-box containing protein 1) and is mapped to human chromosome 16p13.3.

synthetic peptide V(218)DEKRKKRDIPDYLC(232) corresponding to amino acid residues 218-232 from human CHIP.

CHIP (carboxyl terminus of hsc70-interacting protein) is an interacting partner of the constitutive form of hsc70 and the stress inducible form of hsp70. It participates in the ubiquitin-proteasome system. It functions as a E3 ubiquitin-ligase up on binding to hsc70 and hsp90 and ubiquitylates unfolded protein. Mutations in this gene have been linked to spinocerebellar ataxia.

Provided as 100 μg of affinity purified IgG (1 mg/mL) in phosphate buffered saline containing 1 mg/mL bovine serum albumin and 0.05% sodium azide.

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