Mitogen-activated protein kinase (MAPK) superfamily of enzymes is involved in widespread signalling pathways. Members of this family include the ERK1/2 (extracellular signal-regulated protein kinase, also termed p42/p44 MAPK), JNK and p38 MAPK subfamilies. These are the terminal enzymes in a signalling cascade where each kinase phosphorylates and activates the next member in the sequence. Phosphorylation of both tyrosine and threonine is essential for the full activation of all MAPKs. Several kinases participate in activation of the ERK cascade. This cascade is initiated by the small G protein Ras, which upon stimulation causes activation Raf1 kinase. Raf1 continues the transmission by activating MEK. Activated MEK appears to be the only kinase capable of specifically phosphorylating and activating ERK. ERK appears to be an important regulatory molecule, which by can phosphorylate regulatory targets in the cytosol (phospholipase A2, PLA2), translocated into and phosphorylate substrates in the nucleus (ELK1). The activation of ERK cascade mediates and regulates the signal transduction pathways in response to stress, mitogenic signals and is important in development and differentiation, learning, memory and survival.
Anti-MAP Kinase 2 recognizes the 42 kDa MAPK2 encoded by the mapk gene. The antibody may weakly react with MAPK1 (ERK1) and only binds denatured MAP kinase.
recombinant mouse MAP kinase.
Monoclonal Anti-MAP Kinase 2 (ERK-2) antibody is suitable for detection by immunoblotting, at a working concentration of 0.5 μg/mL, using whole cell lysates of human A431, mouse 3T3 fibroblasts or rat L6 cells. Detection of MAPK2 (ERK-2) was possible in human colon adenocarcinoma cells, HT-29. Immunoprecipitation applications in mouse 3T3 fibroblasts require a concentration of 4 μg. The antibody may be suitable for protein microarray.
Solution in phosphate buffered saline containing 0.05% sodium azide
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