The PhosphoPlus® Elk-1 (Ser383) Antibody Kit provides reagents and protocols for the rapid analysis of the phosphorylation status of Elk-1. Bacterially expressed Elk-1 serves as a negative control. The same protein phosphorylated by p42 MAP Kinase (Erk2) serves as a positive control.
Elk-1 Antibody detects endogenous levels of total Elk-1 protein. Phospho-Elk-1 (Ser383) Antibody detects EIk-1 protein only when activated by phosphorylation at serine 383.
Polyclonal antibodies are produced by immunizing rabbits with a synthetic phosphopeptide corresponding to residues surrounding Ser383 of human Elk-1, or with a synthetic peptide derived from the sequence of human Elk-1. Antibodies are purified by protein A and peptide affinity chromatography.
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).
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