Product Pathways - Tyrosine Kinase / Adaptors
Phospho-c-Cbl (Tyr700) (D16D7) Rabbit mAb #8869
|8869S||100 µl (10 western blots)||---||In Stock||---|
|8869P||40 µl (40 western blots)||---||In Stock||---|
|8869||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Species predicted to react based on 100% sequence homology: Mouse.
Specificity / Sensitivity
Phospho-c-Cbl (Tyr700) (D16D7) Rabbit mAb recognizes endogenous levels of c-Cbl protein only when phosphorylated at Tyr700.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr700 of human c-Cbl protein.
Western blot analysis of extracts from Jurkat cells, untreated (-) or treated with pervanadate (1 mM; +), using Phospho-c-Cbl (Tyr700) (D16D7) Rabbit mAb (upper) or c-Cbl (D4E10) Rabbit mAb #8447 (lower).
Immunoprecipitation (IP) of phosphorylated c-Cbl from Jurkat cell extracts, untreated (-) or treated with pervanadate (1 mM; +), using Phospho-c-Cbl (Tyr700) (D16D7) Rabbit mAb (lanes 4 and 6). Western blot detection was performed using the same antibody. Lanes 1 and 2 are 10% input. Lanes 3 and 5 are IPs performed with Rabbit (DA1E) mAb IgG XP® Isotype Control #3900.
Western blot analysis of extracts from Jurkat cells, untreated (-) or treated with pervanadate (1 mM; +), using Phospho-c-Cbl (Tyr700) (D16D7) Rabbit mAb (left). The phospho-specificity of the antibody was verified by preincubating the antibody with c-Cbl (Tyr700) phosphopeptide (center) or with c-Cbl (Tyr700) nonphosphopeptide prior to incubation with the membrane (right).
The c-Cbl proto-oncogene is a ubiquitously expressed cytoplasmic adaptor protein that is especially predominant in hematopoietic cells (1,2). 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, Crk, and 14-3-3 proteins (3,4). c-Cbl possesses a highly conserved amino-terminal phosphotyrosine binding domain (TKB) and a C3HC4 RING finger motif. The TKB recognizes phosphorylated tyrosines on activated receptor tyrosine kinases (RTKs) as well as other nonreceptor tyrosine kinases. The RING finger motif recruits ubiquitin-conjugating enzymes. These two domains are primarily responsible for the ubiquitin ligase activity of c-Cbl and downregulation of RTKs (3). Research studies have indicated that in human cancer tissues, c-Cbl is frequently tyrosine-phosphorylated in a tumor-specific manner (5). Phosphorylation of Tyr731 of c-Cbl provides a docking site for downstream signaling components such as p85 and Fyn (6).
It has been demonstrated that c-Cbl is phosphorylated at Tyr700 by Fyn, Yes, and Syk (4) and that Vav, a hematopoietic-restricted Rac guanine nucleotide exchange factor, undergoes c-Cbl-dependent ubiquitination upon recruitment to phospho-Tyr700 (5).
- Blake, T.J. et al. (1991) Oncogene 6, 653-657.
- Thien, C.B. and Langdon, W.Y. (1998) Immunol. Cell Biol. 76, 473-482.
- Christine, B.F. et al. (2001) Nat. Rev. Mol. Cell Biol. 2, 294-307.
- Feshchenko, E.A. et al. (1998) J. Biol. Chem. 273, 8323-8331.
- Kamei, T. et al. (2000) Int. J. Oncol. 17, 335-339.
- Hunter, C. et al. (1999) J. Biol. Chem. 274, 2097-2106.
- Miura-Shimura, Y. et al. (2003) J Biol Chem 278, 38495-504.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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