Invitrogen™ Phospho-ERK1/ERK2 (Thr185, Tyr187) Polyclonal Antibody

Description

Purified from rabbit serum by sequential epitope-specific chromatography, this product contains enough material for 10 mini-blots. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the sites of phosphorylation to remove antibody that is reactive with non-phosphorylated ERK1&2. The final product is generated by affinity chromatography using an ERK1&2-derived peptide that is phosphorylated at threonine 202/185 and tyrosine 204/187, respectively, within the activation loop. This antibody has been used in western blotting and previous lots have been used in immunostaining. Other applications may work but have not been tested. The positive control used in western analysis were PC12 cells +/- Sorbitol; NIH3T3 +/- PDGF; and HEK293 +/- UV.

ERK1 and ERK2 are widely expressed and are involved in the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virus infection, ligands for heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors and transforming agents, activate the ERK1 and ERK2 pathways. When growth factors bind to the receptor tyrosine kinase, Ras interacts with Raf, the serine/threonine protein kinase and activates it as well. Once actived, Raf phosphorylates serine residue in 2 further kinases, MEK1/2, which in turn phosphorylates tyrosine/threonine in extracellular-signal regulated kinase (ERK) 1/2. Upon activation, the ERKs either phosphorylate a number of cytoplasmic targets or migrate to the nucleus, where they phosphorylate and activate a number of transcription factors such as c-Fos and Elk-1.