c-Cbl Protein, active, 10 µg

Intracellular signals mediated by receptor tyrosine kinases play a pivotal role in morphogenesis, cell fate determination and pathogenesis. c-Cbl is a ubiquitin ligase (E3) that facilitates the regulation of these pathways, attenuating signalling through ubiquitination and subsequent protein degradation. c-Cbl contains several functional domains, including a tyrosine kinase-binding domain that associates with a number of protein tyrosine kinases in a phosphorylation-dependent manner, a catalytic RING-finger domain that interacts with E2s and is essential for E3 activity and a C-terminal proline rich domain which mediates interactions with SH3 containing proteins. Mutations in the gene for c-Cbl have been implicated in a number of human cancers, particularly acute myeloid leukaemia.

N-terminal cMyc and GST-tagged, recombinant human IKKγ full length, expressed by baculovirus in Sf21 insect cells.

Ubiquitination Cascade Comoponent: E3

Purified using glutathione sepharose.

For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.

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