Description: The InstantOne™ ELISA is specifically engineered for accurate measurement of total and phosphorylated human, mouse, and hamster ERK 1/2 in cell lysates. Detection of rat ERK 1/2 is expected. The InstantOne™ ELISA kit allows for fast analysis of samples in approximately one hour. All reagents used in a traditional sandwich ELISA are added in solution to a plate followed by a wash step and detection with the TMB colorimetric substrate.
Extracellular signal-regulated kinase (ERK) is the founding member and a key component of the classical Mitogen-Activated Protein Kinase (MAPK) pathway. ERK1 (p44, MAPK3) and ERK2 (p42, MAPK2) are both activated via the MAPK/ERK pathway, which is downstream of various Receptor Tyrosine Kinases (RTKs) or GPCRs. In the classical MAPK pathway, ligand binding induces the activation of an RTK that initiates a signaling cascade that results in activation of the GTPase Ras and the Ser/Thr kinase Raf (MAPKKK). Raf then binds to and activates MEK (MAPKK) via phosphorylation. MEK, a Ser/Thr and Tyr kinase, activates ERK by phosphorylation of its TxY motifs, namely Thr202/Tyr204 and Thr185/Tyr187 of ERK1 and ERK2, respectively. Both phosphorylation sites are required for ERK activation and no known mutations exist that cause constitutive ERK1/2 activation. As such, detection of ERK1/2 phosphorylation is frequently used to assess its activation, as well as that of MEK, a popular drug target. Once activated, ERK phosphorylates a variety of proteins that regulate cellular processes such as cell division, proliferation, survival, differentiation, apoptosis, motility, and metabolism. Due to its established critical role in these processes, the MAPK signaling pathway is a frequent target for oncology-related drug development.