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Casitas B-lineage lymphoma proto-oncogene C (Cbl-c) is a member of the Cbl RING-type E3 ubiquitin ligase family.1 It is composed of an N-terminal tyrosine kinase-binding domain, which contains a helix bundle, an EF hand calcium-binding motif, and a variant Src homology 2 (SH2) domain, a linker region, a RING finger domain, and a proline-rich region.2,3 Cbl-c is autoinhibited by its EF hand and SH2 domain but is activated following Tyr341 phosphorylation by Src.2 It is expressed in colon, small intestine, pancreas, placenta, liver, kidney, and prostate.3 Cbl-c is involved in the negative regulation of receptor tyrosine kinases, including EGFR and Fyn.1,3 Intratumoral levels of Cbl-c are increased in patients with colorectal cancer and loss-of-function mutations in CBLC are associated with several cancers.4,5 Cayman’s Cbl-c (human, recombinant) protein can be used for enzyme activity assays, structural biology, and biophysical applications and has a calculated molecular weight of 52.4 kDa.
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1. Negative regulation of receptor tyrosine kinases by ubiquitination: Key roles of the Cbl family of E3 ubiquitin ligases. Front. Endocrinol. (Lausanne) 13, 971162 (2022).
2. The N terminus of Cbl-
3. Molecular cloning and characterization of a novel cbl-
4. CBLC promotes the development of colorectal cancer by promoting ABI1 degradation to activate the ERK signaling pathway. Transl. Oncol. 45, 101992 (2024).
5. Loss of function Cbl-