Monoclonal Anti-MAP Kinase, Monophosphorylated Threonine antibody produced in mouse

Monoclonal Anti-MAP Kinase, monophosphorylated threonine antibody may be used for detection in rat brain extract by immunoblotting at a working concentration of 5-20 μg/mL. In cardiomyocytes, immunoblotting may be performed using a working dilution of 1:10,000 of the antibody. The antibody is also suitable for ELISA, immunocytochemistry and protein microarray.

The antibody reacts with the monophosphorylated threonine MAP kinase (ERK-1 and ERK-2) proteins and weaker with the non-phosphorylated forms of MAP kinases. It does not recognize the diphosphorylated, and the monophosphorylated tyrosine forms of the ERK/MAPK proteins, or the JNK and p38 MAPK. The epitope recognized by the antibody contains the threonine residue within the regulatory site of MAP kinase (e.g.,Thr¹⁸³ in ERK-2).

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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.
Monoclonal Anti-MAP Kinase, monophosphorylated threonine (pT-ERK) reacts specifically with the monophosphorylated threonine. It weakly reacts with the nonphosphorylated forms of MAP kinase (ERK-1 and ERK-2, 44 kD and 42 kD, respectively). It does not recognize doubly-phosphorylated, and the mono-phosphorylated tyrosine forms of the MAPK molecule, or JNK or p38-MAPK.

synthetic peptide HTGFLTEYVAT, corresponding to the non-phosphorylated form of ERK-activation loop.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Prepared from a culture supernatant of bioreactor grown hybridoma.