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 cross-reactivity is determined by Western blot.

Protocols

9401:: ELISA Peptide, Flow, Western Blotting

Specificity / Sensitivity

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

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.

Western Blotting

Western blot analysis of extracts from A431 cells, untreated or TPA-treated, using Phospho-c-Myc (Thr58/Ser62) Antibody.

Flow Cytometry

Flow cytometric analysis of untreated Jurkat cells, using Phospho-c-Myc (Thr58/Ser62) Antibody versus propidium iodide (DNA content). The boxed population indicates phospho-c-Myc-positive cells.

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).

Application References

Kamemura, K. et al. (2002) Dynamic interplay between 0-glycosylation and 0-phosphorylation of nucleocytoplasmatic proteins. J. Biol. Chem. 21, 19229-19235. 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. 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. Applications: Western Blotting
Sears, R. et al. (2000) Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability. Genes Dev. 14, 2501-2514. 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. Applications: Western Blotting

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This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.