The following MAPK9 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

MAPK9 Antibodies

MAPK9 Antibodies for Homo sapiens (Human)

MAPK9 Proteins

MAPK9 Proteins for Gallus gallus (Chicken)

MAPK9 Proteins for Homo sapiens (Human)

MAPK9 Proteins for Rattus norvegicus (Rat)

MAPK9 Proteins for Mus musculus (Mouse)

MAPK9 Background

Mitogen-activated protein kinase 9 is a protein in humans that is encoded by the MAPK9 gene [1]. MAPK9 is also called JNK2 [1]. JNK2 is ubiquitously expressed [2]. JNK2 exhibits 83% identity and similar regulation to JNK1 [3]. Despite the close similarity, the two JNKs differ greatly in their ability to interact with c-Jun. JNK2 binds c-Jun approximately 25 times more efficiently than JNK1 [3]. And JNK1 and JNK2 have different, non-redundant roles during toxic liver injury. JNK2 is essential for TNF-mediated apoptosis, whereas JNK1 is not involved in this pathway at all [4]. As a serine/threonine-protein kinase, MAPK9/JNK2 is involved in various processes such as cell proliferation, differentiation, migration, transformation, and apoptosis. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates many transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity, eventually inducing cell proliferation, differentiation, and stress responses [5-8].

[1] Kallunki T, Su B, et al. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation [J]. Genes & Development. 1994, 8 (24): 2996–3007.
[2] Davis RJ. Signal transduction by the JNK group of MAP kinases. Cell 2000;103:239–252.
[3] T Kallunki, B Su, et al. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. Genes & Dev. 1994. 8: 2996-3007.
[4] Wang Y, Singh R, et al. Tumor necrosis factor-induced toxic liver injury results from JNK2-dependent activation of caspase-8 and the mitochondrial death pathway. J Biol Chem 2006;281:15258–15267.
[5] Gupta S, Barrett T, et al. Selective interaction of JNK protein kinase isoforms with transcription factors [J]. EMBO J. 1996, 15 (11): 2760–70.
[6] Dérijard B, Hibi M, et al. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 1994, 76: 1025–1037.
[7] Kyriakis J, Banerjee P, The stress-activated protein kinase subfamily of c-Jun kinases. Nature 1994, 369: 156–160.
[8] Nishina H, Wada T, et al. Physiological roles of SAPK/JNK signaling pathway. J Biochem. 2004 Aug;136(2):123-6.

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
7505 Fannin St., Ste 610, Room 322 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1