Myc Family Profiling Antibody Sampler Kit #26717
Product Information
Kit Usage Information
Protocols
- 7074: Western Blotting
- 13748: Western Blotting
- 18583: Western Blotting, Immunoprecipitation (Agarose), Immunofluorescence, Flow, ChIP Magnetic, Chromatin IP-seq
- 46650: Western Blotting
- 51705: Western Blotting, Immunoprecipitation (Magnetic), Immunohistochemistry (Paraffin), ChIP Magnetic, Chromatin IP-seq
- 76266: Western Blotting, Immunoprecipitation (Magnetic), ChIP Magnetic
Product Description
Specificity / Sensitivity
Each antibody in the Myc Family Profiling Antibody Sampler Kit detects endogenous levels of its target protein. Phospho-c-Myc (Ser62) (E1J4K) Rabbit mAb may not recognize c-Myc phosphorylated at Ser62 when Thr58 is also phosphorylated. Phospho-c-Myc (Thr58) (E4Z2K) Rabbit mAb may also react to c-Myc when dually phosphorylated at Thr58 and Ser62. The phosphorylation site at Thr58 is conserved in N-Myc.
Source / Purification
Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly38 of human N-Myc protein, recombinant proteins specific to the amino terminus of human c-Myc protein and the carboxyl terminus of human L-Myc protein, and synthetic phosphopeptides corresponding to Ser62 and Thr58 of human c-Myc protein.
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).
The Myc family is comprised of c-Myc, N-Myc, and L-Myc with often distinct patterns of expression during development as well as cancer (5). Amplification of each of the family members in cancer is frequently mutually exclusive with c-Myc being the most widely studied and most commonly amplified. N-Myc amplification, on the other hand, is found predominantly in neuroblastomas, and L-Myc amplification has been described in small cell lung cancer (6,7). 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 (8-12).
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- Gregory, M.A. et al. (2003) J Biol Chem 278, 51606-12.
- Yada, M. et al. (2004) EMBO J 23, 2116-25.
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