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Contributor Information

  • Name Danny Huang
  • Institute Cancer Research UK, Glasgow: The Beatson Institute

Tool Details

  • Tool name: pGEX4T1-CBL-B Vector
  • Alternate names: C-CBL, CBL-B, CBL-C, C-CBL2, FRA11B, NSLL, RNF55, Cbl proto-oncogene, Casitas B-lineage Lymphoma
  • Tool type: Vector
  • Tool sub-type: pGEX4T1
  • Description: 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
  • Bacterial resistance: Ampicillin

  • For Research Use Only

Target Details

  • Target: CBL-B fragment encompassing the TKBD, LHR and RING domain: residues 36–427

Application Details


  • Storage conditions: -20°C
  • Shipping conditions: Dry Ice


  • Available on request


  •   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.