Product Pathways - Apoptosis / Autophagy

Phospho-c-Myc (Thr58/Ser62) Antibody #9401

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Applications	Reactivity	Sensitivity	MW (kDa)	Source
W F E-P	H M R Mk	Endogenous	57 to 70	Rabbit

Applications Key:  W=Western Blotting  F=Flow Cytometry  E-P=ELISA (Peptide)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-c-Myc (Thr58/Ser62) Antibody detects endogenous levels of c-Myc singly or doubly phosphorylated at threonine 58 and serine 62.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH-coupled) corresponding to residues around Thr58/Ser62 of human c-Myc. Antibodies are purified by protein A and peptide affinity chromatography.

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 Myc's ability 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 protein designated Mad1, Mad2 (Mxi1), Mad3 and Mad4 and 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).

1. Baudino, T.A. and Cleveland, J.L. (2001) Mol. Cell. Biol. 21, 691-702.
2. Blackwood, E.M. and Eisenman, R.N. (1991) Science 251, 1211-1217.
3. Henriksson, M. and Luscher, B. (1996) Adv. Cancer Res. 68, 109-182.
4. Grandori, C. et al. (2000) Annu. Rev. Cell Dev. Biol. 16, 653-699.

Application References

• Kamemura, K. et al. (2002) Dynamic interplay between 0-glycosylation and 0-phosphorylation of nucleocytoplasmatic proteins. J. Biol. Chem. 21, 19229-19235. This article references the use of Phospho-c-Myc (Thr58/Ser62) Antibody in the following applications: Western Blotting
• Noguchi, K. et al. (1999) Regulation of c-Myc through phosphorylation at Ser-62 and Ser-71 by c-Jun N-terminal kinase. J. Biol. Chem. 274, 32580-32587. This article references the use of Phospho-c-Myc (Thr58/Ser62) Antibody in the following applications: Western Blotting
• Sun, Y. and Clark, E.A. (1999) Expression of the c-myc proto-oncogene is essential for HIV-1 infection in activated T cells. J. Exp. Med. 189, 1391-1398. This article references the use of Phospho-c-Myc (Thr58/Ser62) Antibody in the following applications: Western Blotting
• Sears, R. et al. (2000) Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability. Genes Dev. 14, 2501-2514. This article references the use of Phospho-c-Myc (Thr58/Ser62) Antibody in the following applications: Western Blotting
• Watnick, R. S. et al. (2003) Ras modulates Myc activity to repress thrombospondin-1 expression and increase tumor angiogenesis. Cancer Cell 3, 219-231. This article references the use of Phospho-c-Myc (Thr58/Ser62) Antibody in the following applications: Western Blotting

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This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.