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Western blot analysis of c-Cbl (pY774) in human T leukemia. Lysates from control (Cat. No. 611451, left panel) and Pervanadate-treated (Cat. No. 611755, right panel) Jurkat cells were probed with purified mouse anti-c-Cbl (pY774) monoclonal antibody at concentrations of 1.0, 0.5, and 0.25 µg/ml (Lanes 1, 2, and 3, respectively). c-Cbl (pY774) is identified as a band of 120 kDa in the treated cells.
c-Cbl (pY774) staining on tonsil. Fresh human tonsil was incubated in 5 mM Pervanadate solution for 2 hours, then fixed in formalin and processed. Following antigen retrieval with BD Retrievagen A buffer (Cat. no. 550524), the sections were either left untreated (left panel) or treated with a phosphatase to eliminate all phosphorylation (right panel). The tissue sections were stained with purified mouse anti-c-Cbl (pY774) with Hematoxylin counterstaining. Original magnification: 20X.
BD Pharmingen™ Purified Mouse Anti-c-Cbl (pY774)
BD Pharmingen™ Purified Mouse Anti-c-Cbl (pY774)
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Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Companion Products
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.
Development References (2)
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Thien CBF, Langdon WY. CBL: Many adaptations to regulate protein tyrosine kinase. Nat Rev Mol Cell Biol. 2001; 2:294-307. (Biology).
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Tsygankov AY, Teckchandani AM, Feshchenko EA, Swaminathan G. Beyond the RING: CBL proteins as multivalent adapters. Oncogene. 2001; 20:6382-6402. (Biology).
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