antibody

Anti-c-Cbl (C-terminal Region)

MBS470005

0.1 mL

280 USD

monoclonal

mouse

nonconjugated

human, mouse, rat

western blot, ELISA

Antibody

Anti-c-Cbl (C-terminal Region)

c-Cbl (C-terminal Region)

c-Cbl (C-terminal Region); E3 ubiquitin-protein ligase CBL; RING finger protein 55

c-cbl; E3 ubiquitin-protein ligase CBL; E3 ubiquitin-protein ligase CBL; oncogene CBL2; OTTHUMP00000232087; proto-oncogene c-Cbl; RING finger protein 55; signal transduction protein CBL; casitas B-lineage lymphoma proto-oncogene; Cas-Br-M (murine) ecotropic retroviral transforming sequence; Casitas B-lineage lymphoma proto-oncogene; Proto-oncogene c-Cbl; RING finger protein 55; Signal transduction protein CBL

CBL; CBL; CBL2; NSLL; C-CBL; RNF55; CBL2; RNF55

CBL_HUMAN

Monoclonal

IgG1

Mouse

Human, Rat, Mouse

The antibody detects a 120 kDa* protein in human Jurkat cells.

Protein A Purified

Mouse monoclonal antibody purified with protein A chromatography is supplied in 100ml phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide.

Store at -20 degree C. Do not aliquot. Stable for 1 year.

ELISA, Western Blot

ELISA: 1:2000. Western Blot: 1:1000

Immunogen: Clone (M159) was generated from a synthetic peptide (coupled to KLH) corresponding to amino acid residues in the C-terminal region of c-Cbl. This sequence is highly conserved in rat and mouse c-Cbl.

c-Cbl proto-oncogene is a ubiquitously expressed cytoplasmic adaptor protein that is especially predominant in hematopoietic cells. c-Cbl possesses a highly conserved amino-terminal phosphotyrosine binding domain and a C3HC4 RING finger motif. c-Cbl is rapidly tyrosine phosphorylated in response to stimulation of a variety of cell-surface receptors and becomes associated with a number of intracellular signaling molecules such as protein tyrosine kinases, phosphatidylinositol 3 kinase (PI3K), Crk and 14-3-3 proteins. In human cancer tissues, c-Cbl is frequently tyrosine phosphorylated in a tumor-specific manner. Src-family kinases primarily phosphorylate c- Cbl at Tyr-700, Tyr-731, and Tyr-774. These sites of phosphorylation provide docking sites for downstream signaling components, such as Grb-2, PI3K, and Fyn.

Blake, T. J. et al. (1991) Oncogene 6:653. Donovan, J.A., et al. (1994) J. Biol. Chem. 269:37. Rivero-Lezcano, O.M. et al. (1994) J. Biol. Chem. 269:26. Christine, B. F. et al. (2001) Nat. Rev. Mol. Cell Biol. 2:294.

29731

P22681

99,633 Da

B Cell Receptor Signaling Pathway (198909); Bacterial Invasion Of Epithelial Cells Pathway (149807); Bacterial Invasion Of Epithelial Cells Pathway (148661); CDC42 Signaling Events Pathway (137994); Chronic Myeloid Leukemia Pathway (83116); Chronic Myeloid Leukemia Pathway (528); Cytokine Signaling In Immune System Pathway (366171); EGFR Downregulation Pathway (106342); EGFR1 Signaling Pathway (198782); EPHA Forward Signaling Pathway (138041)

The cbl oncogene was first identified as part of a transforming retrovirus which induces mouse pre-B and pro-B cell lymphomas. As an adaptor protein for receptor protein-tyrosine kinases, it positively regulates receptor protein-tyrosine kinase ubiquitination in a manner dependent upon its variant SH2 and RING finger domains. Ubiquitination of receptor protein-tyrosine kinases terminates signaling by marking active receptors for degradation. [provided by RefSeq]

Function: Participates in signal transduction in hematopoietic cells. Adapter protein that functions as a negative regulator of many signaling pathways that start from receptors at the cell surface. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including PDGFA, EGF and CSF1, and terminates signaling. Essential for osteoclastic bone resorption. The Tyr-731 phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Ref.4 Ref.17. Pathway: Protein modification; protein ubiquitination. Subunit structure: Associates with NCK via its SH3 domain. The phosphorylated C-terminus interacts with CD2AP via its second SH3 domain. Binds to UBE2L3. Interacts with adapters SLA, SLA2 and with the phosphorylated C-terminus of SH2B2. Interacts with EGFR, SYK and ZAP70 via the highly conserved Cbl-N region. Also interacts with SORBS1 and INPPL1/SHIP2. Interacts with phosphorylated LAT2. May interact with CBLB. By similarity. Ref.6 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16. Subcellular location: Cytoplasm. Domain: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. Post-translational modification: Phosphorylated on tyrosine residues by EGFR, SYK, FYN and ZAP70. By similarity. Phosphorylated on tyrosine residues by INSR. Ref.5 Ref.7 Ref.9 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24. Involvement in disease: Defects in CBL are the cause of Noonan syndrome-like disorder (NSL) [. MIM:613563]. NSL is a syndrome characterized by a phenotype reminiscent of Noonan syndrome. Clinical features are highly variable, including facial dysmorphism, short neck, developmental delay, hyperextensible joints and thorax abnormalities with widely spaced nipples. The facial features consist of triangular face with hypertelorism, large low-set ears, ptosis, and flat nasal bridge. Some patients manifest cardiac defects. Ref.29. Miscellaneous: This protein has one functional calcium-binding site. Sequence similarities: Contains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain.Contains 1 RING-type zinc finger.Contains 1 UBA domain.

0.1 mL

280 USD