c-Cbl (pY774) Mouse anti-Human, Alexa Fluor 647, Clone: 29/C-CBL, BD

Cbl (Casitas B-lineage lymphoma) was identified in the genome of a transforming retrovirus from a mouse pre-B lymphoma. The cellular gene product c-Cbl is one of numerous Cbl-related proteins found in vertebrate and invertebrate organisms. It is an 120-kDa adapter protein that contains multiple functional domains, including a RING finger motif, a tyrosine kinase-binding (TKB) domain, and a proline-rich region. The TKB domain directly interacts with specific auto-phosphorylation sites in activated protein-tyrosine kinases (PTK). Through the RING finger motif, c-Cbl recruits and activates an E2 ubiquitin-conjugating enzyme, thus targeting the activated PTK for protein degradation. The proline-rich region contains SH3 domain-binding and 14-3-3 protein-binding motifs. c-Cbl is also phosphorylated at tyrosines 700, 731, and 774 (Y774) by Syk- and Src-family kinases after the stimulation of some integrins and a wide variety of receptors for antigens, immunoglobulins, growth factors, cytokines, and hormones. In turn, the phosphorylated Y774 site interacts with the SH2 domain of the CRK adapter protein. The c-Cbl adapter protein is expressed in the cytoplasm in all tissues, with especially high levels of expression in hematopoietic cells. Through its many functional sites, c-Cbl plays key roles in the positive and negative regulation of vital cell functions, including T Cell Receptor-mediated cellular immune responses.

The 29/c-Cbl monoclonal antibody recognizes the Y774-phosphorylated form of human c-Cbl.