JNK2 and JNK3 are members of the c-Jun N-terminal kinases (JNKs) which are part of the mitogen-activated protein (MAP) kinase family, and regulate signal transduction in response to environmental stress. JNK2 binds to the c-Jun transactivation domain and phosphorylates it on Ser-63 and Ser-73 (1). JNK2 has been shown to play an important role in disease processes. JNK2 plays a role in ventricular hypertrophy and is thought to be involved in hypertensive cardiac disease (2). JNK3 phosphorylates various transcription factors such as ATF2, Elk-1 and members of the Jun family (3). Activation and nuclear localization of JNK3, a neuronal-specific isoform of JNK, has been associated with hypoxic and ischemic damage of CA1 neurons in the hippocampus. Knockout mice lacking JNK3 showed reduced apoptosis of hippocampal neurons and reduced seizure induced by kainic acid, a glutamate-receptor agonist (4).
1. Sluss, H K. et al: Signal transduction by tumor necrosis factor mediated by JNK protein kinases. Mol Cell Biol. 1994 Dec;14(12):8376-84.
2. Vogel, V. et al: Cardiac hypertrophy in the Prague-hypertensive rat is associated with enhanced JNK2 but not ERK tissue activity. Kidney Blood Press Res. 2001;24(1):52-6.
3. Gupta, S. et al: Selective interaction of JNK protein kinase isoforms with transcription factors. EMBO J. 1996 Jun 3;15(11):2760-70.
4. Yang, D D. et al: Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature. 1997 Oct 23;389(6653):865-70.
Recognizes JNK2 and JNK3 protein
Western blot of human JNK2 and JNK3
ERK1 from other species may also be detectable.
C-terminal peptide of JNK3 conjugated to ovalbumin
Store at 4°C (add 0.1% NaN3) for several months, and at -20°C for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For optimal performance, avoid repeated handling and multiple freeze/thaw cycles.
Sample Western Blot:
Representative western blot (1:1000) using 10µg, 20µg, 30µg of Jurkat cell lysate and 20ng of JNK1, JNK2, and JNK3 recombinant protein.
Meter M Van et al., JNK Phosphorylates SIRT6 to Stimulate DNA Double-Strand Break Repair in Response to Oxidative Stress by Recruiting PARP1 to DNA Breaks. Cell Reports September 2016 10.1016/j.celrep.2016.08.006
Hong Park Sun et al., IRAK4 as a Molecular Target in the Amelioration of Innate Immunity?Related Endotoxic Shock and Acute Liver Injury by Chlorogenic Acid Journal of Immunology November 2014 10.4049/jimmunol.1402101
Selvaraja Nagarathinam et al., Extracellular Signal-Regulated Kinase Signaling Regulates the Opposing Roles of JUN Family Transcription Factors at ETS/AP-1 Sites and in Cell Migration Molecular and Cellular Biology January 2015 10.1128/MCB.00982-14
Ines Cervigni Romina et al., JNK2 controls fragmentation of the Golgi complex and G2/M transition trough phosphorylation of GRASP65 Journal of Cell Science June 2015 10.1242/jcs.164871
Prakasam A et al., JNK1/2 regulate Bid by direct phosphorylation at Thr59 in response to ALDH1L1 Cell Death & Disease July 2014 10.1038/cddis.2014.316
Apoptosis/Autophagy, Cardiovascular Disease, Cellular Stress, Inflammation, JNK/SAPK Pathway, Neurobiology, NfkB Pathway