Cell Signaling Technology

Product Pathways - MAPK Signaling

Phospho-Elk-1 (Ser383) Antibody #9181

Applications Reactivity MW (kDa) Source
W (H) (M) (R) (Mk) (Z) (Dg) 47-60 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Z=Zebra Fish  Dg=Dog
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-Elk-1 (Ser383) Antibody detects less than 5 ng of phosphorylated Elk-1, and will not react with up to 1 µg of nonphosphorylated EIk-1 protein.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH coupled) corresponding to residues around Ser383 of human Elk-1. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of Elk-1 fusion protein expressed from E. coli with or without phosphorylation by purified Erk2 enzyme, using Phospho-Elk-1 (Ser383) Antibody (upper) or control Elk-1 Antibody #9182 (lower).

Background

The transcription factor Elk-1 is a component of the ternary complex that binds the serum response element (SRE) and mediates gene activity in response to serum and growth factors (1-3). Elk-1 is phosphorylated by MAP kinase pathways at a cluster of S/T motifs at its carboxy terminus; phosphorylation at these sites, particularly Ser383, is critical for transcriptional activation by Elk-1. Elk-1 appears to be a direct target of activated MAP kinase: (a) biochemical studies indicate that Elk-1 is a good substrate for MAP kinase; (b) the kinetics of Elk-1 phosphorylation and activation correlate with MAP kinase activity; (c) interfering mutants of MAP kinase block Elk-1 activation in vivo. Other studies have shown that Elk-1 (Ser383) is also a target of the stress-activated kinase SAPK/JNK (4,5).

  1. Marais, R. et al. (1993) Cell 73, 381-393.
  2. Kortenjann, M. et al. (1994) Mol. Cell. Biol. 14, 4815-4824.
  3. Hill, C.S. and Treisman, R. (1995) Cell 80, 199-211.
  4. Cavigelli, M. et al. (1995) EMBO J. 14, 5957-5964.
  5. Whitmarsh, A.J. et al. (1995) Science 269, 403-407.

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