Cell Signaling Technology

Product Pathways - MAPK Signaling

PhosphoPlus® Elk-1 (Ser383) Antibody Kit #9180

Kit Includes Quantity Applications Reactivity MW (kDa) Source
Phospho-Elk-1 (Ser383) Antibody # 9181 100 microliters W (H) (M) (R) (Mk) (Z) (Dg) 47-60 Rabbit
Elk-1 Antibody # 9182 100 microliters W H M R Z 47-60 Rabbit
Elk-1 Control Proteins # 9183 60 microliters 40 kDa nonphosphorylated, 50 kDa phosphorylated E. Coli
Elk-1 Control Proteins # 9183 60 microliters 40 kDa nonphosphorylated, 50 kDa phosphorylated E. Coli
Anti-rabbit IgG, HRP-linked Antibody # 7074 50 microliters Goat
Anti-biotin, HRP-linked Antibody # 7075 100 microliters Goat
Biotinylated Protein Ladder Detection Pack # 7727 100 microliters
20X LumiGLO® Reagent and 20X Peroxide # 7003 5 milliliters
20X LumiGLO® Reagent and 20X Peroxide # 7003 5 milliliters

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Z=Zebra Fish  Dg=Dog

Specificity / Sensitivity

Western Blotting

Western Blotting

Western analysis of Elk-1 fusion protein expressed from E. coli with or without phosphorylation with purified Erk2 enzyme using Phospho-Elk-1 (Ser383) (A) or Elk-1 Antibodies (B).

Source / Purification

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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