ERK1 (T207) /ERK2 (T188) [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.

The antibody detects 42 and 44 kDa* proteins corresponding to ERK1 (Thr-207) and ERK2 (Thr-188) on SDS-PAGE immunoblots of human A431 epithelial cells stimulated with calyculin A. It does not detect these ERK proteins in control cells or in blots treated with lambda phosphatase. This sequence is conserved in human, rat, chicken, and fish ERK2, and is highly conserved in ERK1 (Thr-207), ERK5 (Thr-224), and ERK7 (Thr-180) .