Cas-Br-M (Murine) Ecotropic Retroviral Transforming Sequence (CBL) (pTyr774) antibody

Antigen: Cas-Br-M (Murine) Ecotropic Retroviral Transforming Sequence (CBL)

Synonyms: cbl, Cbl-2, c-Cbl, 4732447J05Rik, CBL2, C-CBL, RNF55

Binding Site: pTyr774

Clonality: Monoclonal (29)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (Formalin-fixed Sections) (IHC (f))

Catalog no.: ABIN967577

Additional Information

Alternative name: c-Cbl

Immunogen: Phosphorylated Human c-Cbl Peptide

Format: Liquid

Isotype: IgG1

Clone: 29

Description: 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.

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. 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.

Comments:

Related Products: ABIN967389, ABIN968537, ABIN968656

Application Details

Concentration: 0.5 mg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at 4°C.

Restrictions: For Research Use only

Images

Western blot analysis of c-Cbl (pY774) in human T leukemia. Lysates from control (ABIN968537, left panel) and Pervanadate-treated (ABIN968656, 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 myg/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 Retrievagen A buffer, 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.

Publications

Product: Thien, Langdon: "Cbl: many adaptations to regulate protein tyrosine kinases." in: Nature reviews. Molecular cell biology, Vol. 2, Issue 4, pp. 294-307, 2001 (PubMed).

Tsygankov, Teckchandani, Feshchenko et al.: "Beyond the RING: CBL proteins as multivalent adapters." in: Oncogene, Vol. 20, Issue 44, pp. 6382-402, 2001 (PubMed).