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Catalogue Number 153456
Backbone Size (bp) 4969
Bacterial Resistance Ampicillin
Vector Type pGEX4T1
Synonyms C-CBL, CBL-B, CBL-C, C-CBL2, FRA11B, NSLL, RNF55, Cbl proto-oncogene, Casitas B-lineage Lymphoma
Antigen/Gene or Protein Targets CBL-B fragment encompassing the TKBD, LHR and RING domain: residues 36–427.
Relevance Over 600 E3 ligases have been identified in mammals and most are part of the RING family of E3 ligases. The monomeric family of CBL RING E3 ligases (c-CBL, CBL-B and CBL-C) attenuate nonreceptor and receptor tyrosine kinase signalling through ubiquitination and direct the receptor tyrosine kinases for degradation through the endocytic or proteasomal pathways.

Members of the CBL family share a highly conserved N terminus comprising of a tyrosine kinase binding domain, a linker helix region and a RING domain. The more variable C terminus possessing a proline-rich region and a string of terminal amino acids or 'extension'. Mutations in this gene have been implicated in several human cancers including acute myeloid leukaemia.

The protein CBL is a ubiquitously expressed 982 amino acid E3 ubiquitin-protein ligase involved in cell signalling and protein ubiquitination.
Research Area Cancer, Cell Signaling & Signal Transduction, Epigenetics & Nuclear Signalling

References

There are 2 reference entries for this reagent.

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References: 2 entries

Dou et al. 2013. Nat Struct Mol Biol. 20(8):982-6. PMID: 23851457.

Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3.

Europe PMC ID: 23851457


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References: 2 entries

Dou et al. 2013. Nat Struct Mol Biol. 20(8):982-6. PMID: 23851457.

Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3.


Add a reference