Cell Signaling Technology

Product Pathways - MAPK Signaling

Phospho-MEF2A (Ser408) Antibody #9737

Applications Reactivity Sensitivity MW (kDa) Source
W H (M) Transfected Only 54 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-MEF2A (Ser408) Antibody detects transfected levels of MEF2A only when phosphorylated at Ser408. The antibody has also been shown to detect phospho-MEF2A (Ser408) in granule neurons (see application reference).

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser408 of human MEF2A. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from COS-7 cells transfected with wild-type GAL4-MEF2A or mutant GAL4-MEF2A (S408A), using Phospho-MEF2A (Ser408) Antibody (top) and MEF2A Antibody #9736 (bottom).

Background

MEF2A is a member of the MEF2 (myocyte enhancer factor 2) family of transcription factors. In mammals, four MEF2A-related genes (MEF2A, MEF2B, MEF2C and MEF2D) encode proteins which exhibit significant amino acid sequence similarity within their DNA binding domains and to a lesser extent throughout the remaining proteins (1). The MEF2 family members were originally described as muscle-specific DNA binding proteins that recognize MEF2 motifs found within the promoters of many muscle-specific genes (2,3). Phosphorylation of MEF2A at Thr312 and Thr319 within the transcription activation domain by p38 MAP kinase enhances MEF2A-MEF2D heterodimer-dependent gene expression (4). On the other hand, apoptotic stimuli (e.g. neurotoxic insult) result in CDK5-dependent phosphorylation of MEF2A at Ser408 within the activation domain, inhibiting MEF2A pro-survival function (5).

  1. Shore, P. et al. (1995) Eur. J. Biochem. 229, 1-13.
  2. Martin, J.F. et al. (1994) Mol. Cell. Biol. 14, 1647-1656.
  3. Yu, Y.T. et al. (1992) Genes Dev. 6, 1783-1798.
  4. Zhao, M. et al. (1999) Mol. Cell. Biol. 19, 21-30.
  5. Gong, X. et al. (2003) Neuron 38, 33-46.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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