Enzymes, Signaling Proteins, Extracellular Ligands, Signaling Reagents, Antibodies

Catalog No.	Pack Size	Price (USD)
M33-14G-20	20 ug	$215
M33-14G-50	50 ug	$435
M33-14G-BULK	BULK	Contact Us

Overview:

JNK1 is a member of the MAP kinase group that is activated by dual phosphorylation at thr and tyr residues during exposure to stress such as UV irradiation. JNK1 binds to the c-Jun transactivation domain and phosphorylates it on Ser-63 and Ser-73 (1). JNK1 has been shown to play an important role in disease processes. Activation of JNK1 results in defects in myotube viability and integrity leading to dystrophic myofiber destruction (2). JNK1 activity is also abnormally elevated in obesity and removal of JNK1 results in decreased adiposity and significantly improved insulin sensitivity.

Gene Aliases:

JNK; JNK1; PRKM8; SAPK1; JNK1A2; JNK21B1/2

Genbank Number:

NM_016700

References:

1. Derijard, B. et al: JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell. 1994 Mar 25;76(6):1025-37.

2. Kolodziejczyk, S M. et al: Activation of JNK1 contributes to dystrophic muscle pathogenesis. Curr Biol. 2001 Aug 21;11(16):1278-82.

Purity:

Sample Purity Data. For specific information on a given lot, see related technical data sheet.

Storage, Stability and Shipping:

Store product at –70^oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Molecular Weight:

~70 kDa

Product Datasheets

K089-2

G309-1

KH Su et al., HSF1 critically attunes proteotoxic stress sensing by mTORC1 to combat stress and promote growth. Nature Cell Biology May 2016 10.1038/ncb3335

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

Puri Puneet et al., Activation and Dysregulation of the Unfolded Protein Response in Nonalcoholic Fatty Liver Disease Gastroenterology October 2006 10.1053/j.gastro.2007.10.039

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

A. Dadaa Laura et al., High CO2 Leads to Na, K-ATPase Endocytosis via c-Jun Amino-Terminal Kinase-Induced LMO7b Phosphorylation Molecular and Cellular Biology September 2015 10.1128/MCB.00813-15

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

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

Liu Bin et al., ABL-N-induced apoptosis in human breast cancer cells is partially mediated by c-Jun NH2-terminal kinase activation Breast Cancer Research January 2010 10.1186/bcr2475

Nakatsu Daiki et al., JNK1/2-dependent phosphorylation of angulin-1/LSR is required for the exclusive localization of angulin-1/LSR and tricellulin at tricellular contacts in EpH4 epithelial sheet Genes to Cells June 2014 10.1111/gtc.12158

Selvaraj Nagarathinam et al., Comparison of MAPK specificity across the ETS transcription factor family identifies a high-affinity ERK interaction required for ERG function in prostate cells Cell Communcation & Signaling February 2015 10.1186/s12964-015-0089-7

JNK1, Unactive

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