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JNK2 is a stress-activated serine/threonine protein kinase and member of the MAPK family.1,2 It is composed of a short N-terminal helical domain, a flexible connector that contains the active site, and a large helical C-terminal domain.3 JNK2 is encoded by MAPK9, which produces four isoforms via alternative splicing.4 JNK2 is ubiquitously expressed and is found in the cytoplasm.1,4 JNKs are activated by phosphorylation at threonine 183 (Thr183) and tyrosine 185 (Tyr185) by MAP kinase kinase 7 (MKK7) and MKK4, respectively, in response to stress stimuli, such as cellular stress, radiation, inflammation, or oxidative stress.5,1 After activation, JNKs localize to the nucleus where they phosphorylate transcription factors, nuclear receptors, and adaptor proteins that broadly regulate cell proliferation, cell survival, and apoptosis.2 JNK2 α2 isoform has been found to be constitutively active in tumor samples isolated from patients with glioma.6 Cayman's JNK2 α2 Isoform (human, recombinant) protein consists of 435 amino acids. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 49.5 kDa.
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1. JNK pathway signaling: A novel and smarter therapeutic target for various biological diseases. Future Med. Chem. 7(15), 2065-2086 (2015).
2. Uses for JNK: The many and varied substrates of the c-
3. The crystal structure of JNK2 reveals conformational flexibility in the MAP kinase insert and indicates its involvement in the regulation of catalytic activity. J. Mol. Biol. 383(4), (2008).
4. Discovery of potent and selective covalent inhibitors of JNK. Chem. Biol. 19(1), 140-154 (2012).
5. Activation by phosphorylation and purification of human c-
6. Constitutively active forms of c-