ERK1&2 (p44&42 MAPK) phospho Thr202&Tyr204 [MD356]

Mitogen-activated protein kinase (MAPK), also known as extracellular signal-regulated kinase (ERK), includes two closely related kinases ERK1 (p44) and ERK2 (p42). Growth factors, steroid hormones, G protein-coupled receptor ligands and neurotransmitters can initiate MAPK signaling pathways. Activation of ERK1 and ERK2 requires phosphorylation by upstream kinases such as MEK, MEK kinase and Raf-1. ERK1 and ERK2 phosphorylation can occur at specific tyrosine and threonine sites mapping within consensus motifs that include the threonine-glutamate-tyrosine motif. ERK activation leads to dimerization with other ERKs and subsequent localization to the nucleus. Active ERK dimers phosphorylate serine and threonine residues on nuclear proteins and influence a host of responses that include proliferation, differentiation, transcription regulation and development. The human ERK1 gene maps to chromosome 16p11.2 and encodes a 379 amino acid protein that shares 83% sequence identity to ERK2.