ERK1 (Thr-202/Tyr-204) [conserved], Phosphospecific Antibody

Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs such as cell proliferation, differentiation, motility, and death. The ERK1/2 (p44/42) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines. Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK), a MAP kinase kinase (MAPKK), and a MAP kinase (MAPK) . Multiple ERK1/2 MAPKKKs have been identified, including members of the Raf family as well as Mos and Tpl2/Cot. MEK1 and MEK2 are the primary MAPKKs in this pathway. MEK1 and MEK2 activate ERK1 and ERK2 through phosphorylation of activation loop residues Thr-202/Tyr-204 and Thr-185/Tyr-187, respectively. ERK1/2 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases. Several downstream targets of ERK1/2 have been identified, including p90RSK and the transcription factor Elk-1.

Clone M206 was generated from a dual phosphorylated ERK1 (Thr-202/Tyr-204) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding Thr-202 and Tyr-204 in human ERK1.

The antibody detects 42 and 44 kDa* proteins corresponding to ERK1 and ERK2 on SDS-PAGE immunoblots of human A431 epithelial cells stimulated with EGF or calyculin A. It does not detect bands in control cells. This sequence is conserved in rat and mouse ERK1, and is highly conserved in ERK2.