pGEX4T1-CBL-B Vector
Invented by Dr Danny Huang from Cancer Research UK Glasgow: The Beatson Institute
Invented at Cancer Research UK Glasgow: The Beatson Institute
- Datasheet
- References (2)
- Inventor Info
Info
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: 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