|Detection of Human, Mouse, and Rat ERK1/ERK2 by Western Blot. Western blot shows lysates of MCF‑7 human breast cancer cell line, BaF3 mouse pro-B cell line, and PC‑12 rat adrenal pheochromocytoma cell line. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Human/Mouse/Rat ERK1/ERK2 Monoclonal Antibody (Catalog # MAB15761) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). Specific bands were detected for ERK1/ERK2 at approximately 42 and 44 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
ERK1 and ERK2 (also known as MAPK3 and MAPK1) are 44 and 42 kDa Ser/Thr kinases, respectively. They are part of the Ras-Raf-ERK signal transduction cascade often found downstream of growth factor receptor activation. ERK1 and ERK2 were initially isolated and cloned as kinases activated in response to insulin and NGF. They are expressed in most, if not all, mammalian tissues. Dual threonine and tyrosine phosphorylation activate both ERKs, at Thr202/Tyr204 for human ERK1 and Thr185/Tyr187 for human ERK2.
ERK5, also known as Big Mitogen-activated Protein Kinase 1 (BMK1) and MAPK7, is activated by several mechanisms, including receptor tyrosine kinases, G protein-coupled receptors, and osmotic stress. Like ERK1 and ERK2, ERK5 contains the conserved Thr-Glu-Tyr activation motif in its activation loop. Unlike these ERKs, however, ERK5 contains a unique C-terminal domain that regulates its activation and nuclear translocation.
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