ERK1 is a protein serine/threonine kinase that is a member of the extracellular signal-regulated kinases (ERKs), which are activated in response to numerous growth factors and cytokines. Activation of ERK1 requires both tyrosine and threonine phosphorylation that is mediated by MEK. ERK1 is ubiquitously distributed in tissues with the highest expression in heart, brain and spinal cord. In vitro studies indicate that ERK1 phosphorylate both nuclear and cytoplasmic proteins. Activated ERK1 translocates into the nucleus where it phosphorylates various transcription factors (e.g., Elk-1, c-Myc, c-Jun, c-Fos, and C/EBP b). The consensus primary sequence for substrate phosphorylation by ERK1 has been identified as -Pro-Leu-Ser/Thr-Pro-. ERK1 has been implicated in the control of a broad spectrum of cellular events in many types of cells. In somatic cells, ERK1 activation seems to be triggered after exit from a quiescent state only and then inactivated by entry into a proliferative state.
Source:
Recombinant protein corresponding to human ERK1 expressed in Sf 9 insect cells.
Molecular Weight:
~45.0kD
Biological Activity:
383nmol phosphate incorporated into MBP per minute per mg protein at 30 degrees C for 15 minutes using a final concentration of 50um ATP, 0.83uCi/assay.
Storage and Stability:
Aliquot to avoid repeated freezing and thawing and store at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
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