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Questions? Please consult our answers to frequently asked questions at http://www.ebioscience.com/faq. DescriptionThis is a peptide mapping to the carboxy terminal domain of human Cbl p120. The proto-oncogene c-Cbl was initially identified as the cellular homologue of v-Cbl oncogene that induces pre-B cell lymphomas and myeloid leukemias in mice (1&2). In more recent studies Cbl has been shown to be a negative regulator of tyrosine kinase signaling (2-4). The ubiquitin ligase activity of Cbl leads to the degradation of tyrosine kinases, thus attenuating the signal of receptors (3&4). Targets of Cbl include activated protein tyrosine kinases belonging to the Src and Syk/Zap-70 families (3). An additional mechanism to attenuate receptor signaling is thought to be achieved by Cbl?s interaction with downstream targets of tyrosine kinases, such as PI-3K and Vav (1&3). Applications ReportedFor research use only, not for diagnostic or therapeutic use. This blocking peptide has been reported for use in competition studies. References
1. Liu YC, Altman A. 1998. Cbl: complex formation and functional implications. Cell Signal 10(6):377-385. 2. Miyake S, Lupher ML, Andoniou CE, Lill NL, Ota S, Douillard P, Rao N, Band H. 1997. The Cbl protooncogen product: from an enigmatic oncogene to center stage of signal transduction. Crit Rev Oncog 8(2-3):189-218. 3. Rao N, Dodge I, Band H. 2002. The Cbl family of ubiquitin ligases: critical negative regulators of tyrosine kinase signaling in the immune system. J Leukoc Biol 71(5):753-763. 4. Sanjay A, Horne WC, Baron R. 2001. The Cbl family: ubiquitin ligases regulating signaling by tyrosine kinase. Sci STKE 2001(110):PE40. Related ProductsCat. 14-6760 Purified anti-mouse/human/rat Cbl polyclonal (clone Polyclonal) |
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