#P01106
4609
| Product Includes | Quantity | Reactivity | MW(kDa) | Isotype | |
|---|---|---|---|---|---|
| Phospho-c-Myc (Ser62) (E1J4K) Rabbit mAb 13748 | 100 µl | H M R | 62 | Rabbit IgG | |
| c-Myc (E5Q6W) Rabbit mAb 18583 | 100 µl | H M R | 57-65 | Rabbit IgG |
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Description
PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.
Storage
Background
Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior, including proliferation, differentiation, and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3, and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes, such as proliferation, transformation, and prevention of apoptosis by inhibiting transcription (3,4).
Phosphorylation of c-Myc at Thr58 and Ser62 can control proteasomal-dependent degradation of the transcription factor. Phosphorylation of c-Myc at these sites is a stepwise process, whereby mitogens, mitosis, or cellular stress induce phosphorylation at Ser62, which serves as a priming site for GSK-3 phosphorylation of Thr58 (5-9).
- Baudino, T.A. and Cleveland, J.L. (2001) Mol Cell Biol 21, 691-702.
- Blackwood, E.M. and Eisenman, R.N. (1991) Science 251, 1211-7.
- Henriksson, M. and Lüscher, B. (1996) Adv Cancer Res 68, 109-82.
- Grandori, C. et al. (2000) Annu Rev Cell Dev Biol 16, 653-99.
- Lutterbach, B. and Hann, S.R. (1994) Mol Cell Biol 14, 5510-22.
- Gregory, M.A. et al. (2003) J Biol Chem 278, 51606-12.
- Yada, M. et al. (2004) EMBO J 23, 2116-25.
- Seo, H.R. et al. (2008) J Biol Chem 283, 15601-10.
- Benassi, B. et al. (2006) Mol Cell 21, 509-19.
Background References
Trademarks and Patents
Limited Uses
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