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Immunofluorescence analysis of JNK1/2 [pT183/pT185] was done on 70% confluent log phase A549 cells treated with Anisomycin (25 µg/mL for 30 min). The cells were fixed with 4% paraformaldehyde for 15 minutes, permeabilized with 0.25% Triton™ X-100 for 10 minutes, and blocked with 5% BSA for 1 hour at room temperature. The cells were labeled with JNK1/2 [pT183/pT185] Rabbit polyclonal Antibody (44682G) at 2 µg/mL in 1% BSA and incubated for 3 hours at room temperature and then labeled with Alexa Flour 488 Goat Anti-Rabbit IgG Secondary Antibody (A11008) at a dilution of 1:400 for 30 minutes at room temperature (Panel a: green). Nuclei (Panel b: blue) were stained with SlowFade® Gold Antifade Mountant with DAPI (S36938). F-actin (Panel c: red) was stained with Alexa Fluor 594 Phalloidin (A12381). Panel d is a merged image showing translocation of JNK1/2 [pT183/pT185] to the nucleus upon Anisomycin treatment. Panel e is untreated cells showing cytoplasmic localization. Panel f shows no primary antibody control. The images were captured at 20X magnification.
|Tested species reactivity||Human, Mouse, Rat|
|Published species reactivity||Primate, Human, Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||The antiserum was produced against a chemically synthesized phosphopeptide derived from a region of human JNK1&2 that contains threonine 183 and tyrosine 185. This region is conserved among many species including mouse, rat, chicken, nematode, fruit fly, and in JNK3.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3, with 50% glycerol, 1mg/ml BSA|
|Contains||0.05% sodium azide|
|Tested Applications||Dilution *|
|Immunohistochemistry (IHC)||Assay Dependent|
|Western Blot (WB)||1:200-1:2000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
C-Jun N-terminal Kinase (JNK) is also known as Mitogen-activated protein kinase (MAPK8). It belongs to the MAPK superfamily of stress-activated protein kinases. MAPKs are Serine-threonine protein kinases that are activated in response to a variety of extracellular stimuli, and mediate signal transduction from the cell surface to the nucleus. JNK is involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. JNK pathways are activated by stress and inflammatory signals. JNK is expressed as ten different isoforms due to differential mRNA splicing. The predominant forms are JNK1 and JNK2.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
RNF4 negatively regulates NF-κB signaling by down-regulating TAB2.
44-682G was used in western blot to identify negative regulators of NF-κB signaling.
|Tan B,Mu R,Chang Y,Wang YB,Wu M,Tu HQ,Zhang YC,Guo SS,Qin XH,Li T,Li WH,Zhang XM,Li AL,Li HY||FEBS letters (589:2850)||2015|
Interleukin-1 Acts via the JNK-2 Signaling Pathway to Induce Aggrecan Degradation by Human Chondrocytes.
44-682G was used in western blot to identify the intracellular signaling pathways by which IL- causes aggrecan degradation by human chondrocytes and investigate how aggrecanase activity is regulated in chondrocytes.
|Ismail HM,Yamamoto K,Vincent TL,Nagase H,Troeberg L,Saklatvala J||Arthritis & rheumatology (Hoboken, N.J.) (67:1826)||2015|
Functional comparison of herpes simplex virus 1 (HSV-1) and HSV-2 ICP27 homologs reveals a role for ICP27 in virion release.
44-682G was used in western blot to compare ICP27t2 and ICP27 from herpes simplex virus
|Park D,Lalli J,Sedlackova-Slavikova L,Rice SA||Journal of virology (89:2892)||2015|
Synergistic anticancer effect of cisplatin and Chal-24 combination through IAP and c-FLIPL degradation, Ripoptosome formation and autophagy-mediated apoptosis.
44-682G was used in western blot to investigate if Chal-24 can be combined with cisplatin for better cancer therapy.
|Shi S,Wang Q,Xu J,Jang JH,Padilla MT,Nyunoya T,Xing C,Zhang L,Lin Y||Oncotarget (6:1640)||2015|
Dual oxidase 2 in lung epithelia is essential for hyperoxia-induced acute lung injury in mice.
44-682G was used in western blot to study ROS production induced by hyperoxia in type II alveolar epithelial cells and acute lung injury
|Kim MJ,Ryu JC,Kwon Y,Lee S,Bae YS,Yoon JH,Ryu JH||Antioxidants & redox signaling (21:1803)||2014|
A JNK-mediated autophagy pathway that triggers c-IAP degradation and necroptosis for anticancer chemotherapy.
44-682G was used in western blot to identify a novel anticancer mechanism that functions through autophagy-mediated necroptosis
|He W,Wang Q,Srinivasan B,Xu J,Padilla MT,Li Z,Wang X,Liu Y,Gou X,Shen HM,Xing C,Lin Y||Oncogene (33:3004)||2014|
Increased ERK and JNK activation and decreased ERK/JNK ratio are associated with long-term organ damage in patients with systemic lupus erythematosus.
44-682G was used in western blot to test if extracellular signal-regulated kinase and c-Jun N-terminal kinase are associated with long-term organ damage in SLE patients.
|Bloch O,Amit-Vazina M,Yona E,Molad Y,Rapoport MJ||Rheumatology (Oxford, England) (53:1034)||2014|
SARM regulates CCL5 production in macrophages by promoting the recruitment of transcription factors and RNA polymerase II to the Ccl5 promoter.
44-682G was used in western blot to examine TLR-induced cytokine production by SARM-deficient murine macrophages
|Gürtler C,Carty M,Kearney J,Schattgen SA,Ding A,Fitzgerald KA,Bowie AG||Journal of immunology (Baltimore, Md. : 1950) (192:4821)||2014|
Retaining MKP1 expression and attenuating JNK-mediated apoptosis by RIP1 for cisplatin resistance through miR-940 inhibition.
44-682G was used in western blot to study the role of receptor-interacting protein 1 in cancer's response to chemotherapy
|Wang Q,Shi S,He W,Padilla MT,Zhang L,Wang X,Zhang B,Lin Y||Oncotarget (5:1304)||2014|
Supplementation with α-lipoic acid, CoQ10, and vitamin E augments running performance and mitochondrial function in female mice.
44-682G was used in western blot to assess the effects of an antioxidant cocktail (α-lipoic acid, vitamin E and coenzyme Q0) on exercise performance, muscle function, and training adaptations in mice.
|Abadi A,Crane JD,Ogborn D,Hettinga B,Akhtar M,Stokl A,Macneil L,Safdar A,Tarnopolsky M||PloS one (8:null)||2013|
|Mouse||Not Cited||p38γ and p38δ kinases regulate the Toll-like receptor 4 (TLR4)-induced cytokine production by controlling ERK1/2 protein kinase pathway activation.||Risco A,del Fresno C,Mambol A,Alsina-Beauchamp D,MacKenzie KF,Yang HT,Barber DF,Morcelle C,Arthur JS,Ley SC,Ardavin C,Cuenda A||Proceedings of the National Academy of Sciences of the United States of America (109:11200)||2012|
|Human||Not Cited||Molecular pathway profiling of T lymphocyte signal transduction pathways; Th1 and Th2 genomic fingerprints are defined by TCR and CD28-mediated signaling.||Smeets RL,Fleuren WW,He X,Vink PM,Wijnands F,Gorecka M,Klop H,Bauerschmidt S,Garritsen A,Koenen HJ,Joosten I,Boots AM,Alkema W||BMC immunology (13:null)||2012|
The death domain-containing protein Unc5CL is a novel MyD88-independent activator of the pro-inflammatory IRAK signaling cascade.
44-682G was used in western blot to study the role of Unc5CL in the pro-inflammatory IRAK signaling cascade
|Heinz LX,Rebsamen M,Rossi DC,Staehli F,Schroder K,Quadroni M,Gross O,Schneider P,Tschopp J||Cell death and differentiation (19:722)||2012|
zVAD-induced necroptosis in L929 cells depends on autocrine production of TNFα mediated by the PKC-MAPKs-AP-1 pathway.
44-682G was used in western blot to study the role of TNF in zVAD-induced necroptosis in L929 cells
|Wu YT,Tan HL,Huang Q,Sun XJ,Zhu X,Shen HM||Cell death and differentiation (18:26)||2011|
|Mouse||Not Cited||Critical role of c-jun (NH2) terminal kinase in paracetamol- induced acute liver failure.||Henderson NC,Pollock KJ,Frew J,Mackinnon AC,Flavell RA,Davis RJ,Sethi T,Simpson KJ||Gut (56:982)||2007|
|Human||Not Cited||Molecular mechanisms involved in interleukin-4-induced human neutrophils: expression and regulation of suppressor of cytokine signaling.||Ratthé C,Pelletier M,Chiasson S,Girard D||Journal of leukocyte biology (81:1287)||2007|
|Human||Not Cited||The mitogen-activated protein kinases (MAPK) p38 and JNK are markers of tumor progression in breast carcinoma.||Davidson B,Konstantinovsky S,Kleinberg L,Nguyen MT,Bassarova A,Kvalheim G,Nesland JM,Reich R||Gynecologic oncology (102:453)||2006|
|Human||Not Cited||Matrix metalloproteinases (MMP), EMMPRIN (extracellular matrix metalloproteinase inducer) and mitogen-activated protein kinases (MAPK): co-expression in metastatic serous ovarian carcinoma.||Davidson B,Givant-Horwitz V,Lazarovici P,Risberg B,Nesland JM,Trope CG,Schaefer E,Reich R||Clinical & experimental metastasis (20:621)||2003|
JNK1 controls dendritic field size in L2/3 and L5 of the motor cortex, constrains soma size, and influences fine motor coordination.
44-682G was used in immunocytochemistry to investigate the role of JNK-1 signaling in prevalent dendrite disorders
|Komulainen E,Zdrojewska J,Freemantle E,Mohammad H,Kulesskaya N,Deshpande P,Marchisella F,Mysore R,Hollos P,Michelsen KA,Mågard M,Rauvala H,James P,Coffey ET||Frontiers in cellular neuroscience (8:null)||2014|
||p38γ and p38δ kinases regulate the Toll-like receptor 4 (TLR4)-induced cytokine production by controlling ERK1/2 protein kinase pathway activation.||Risco A,del Fresno C,Mambol A,Alsina-Beauchamp D,MacKenzie KF,Yang HT,Barber DF,Morcelle C,Arthur JS,Ley SC,Ardavin C,Cuenda A||Proceedings of the National Academy of Sciences of the United States of America (109:11200)||2012|
||Critical role of c-jun (NH2) terminal kinase in paracetamol- induced acute liver failure.||Henderson NC,Pollock KJ,Frew J,Mackinnon AC,Flavell RA,Davis RJ,Sethi T,Simpson KJ||Gut (56:982)||2007|
c-Jun kinase 2; c-Jun N-terminal kinase 1; c-Jun N-terminal kinase 2; JNK; JNK/SAPK alpha; JNK1; JNK1 beta1 protein kinase; JNK1A2; JNK2; JNK21B1/2; Jun kinase; JUN N-terminal kinase; MAP kinase 8; MAP kinase 9; MAPK 8; MAPK 9; MAPK8; MAPK9; mitogen activated protein kinase 8; mitogen activated protein kinase 9; mitogen-activated protein kinase 8; mitogen-activated protein kinase 8 isoform JNK1 alpha1; mitogen-activated protein kinase 8 isoform JNK1 beta2; mitogen-activated protein kinase 9; p54-alpha; PRKM8; PRKM9; protein kinase mitogen-activated 8; protein kinase, mitogen-activated 9; SAPK-alpha; SAPK1; SAPK1A; SAPK1c; stress activated protein kinase alpha II; stress-activated protein kinase 1; stress-activated protein kinase 1a; stress-activated protein kinase 1c; stress-activated protein kinase JNK1; stress-activated protein kinase JNK2
AI849689; AI851083; JNK; JNK-46; JNK-55; JNK1; JNK1A2; JNK2; JNK21B1/2; JNK2A; JNK2ALPHA; JNK2B; JNK2BETA; MAPK8; MAPK9; p54a; p54aSAPK; PRKM8; PRKM9; SAPK; SAPK1; SAPK1A; SAPK1C