CHIP, active 250ug

Active, full length, recombinant human CHIP. N-terminal 6His-tagged. For use in Enzyme Assays. Functions as an E3 ligase in ubiquitination assays.

Enzyme Assays

CHIP is an E3 ubiquitin-protein ligase which targets misfolded chaperone substrates for proteasomal degradation. It contains multiple domains, including a tetratricopeptide repeat (TPR) domain that allows interaction with molecular chaperones, such as Hsp70 and Hsp90 and a U-box domain that confers its E3 ubiquitin ligase function. It has been demonstrated that CHIP preferentially ubiquitinates chaperone-bound substrates, of which there are a diverse range including CFTR, ErbB2 and LRRK2, but also targets Hsp70 itself to the proteasome for degradation when misfolded substrates are not present. This sequential degradation of misfolded substrate and chaperone provides a homeostatic mechanism for regulating chaperone levels to reflect the status of protein folding within the cytoplasm.

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