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Human JNK Protein expressed in Wheat germ - ABIN1310303
Prause, Christensen, Billestrup, Mandrup-Poulsen: JNK1 protects against glucolipotoxicity-mediated beta-cell apoptosis. in PLoS ONE 2014
Human JNK Protein expressed in Baculovirus infected Insect Cells - ABIN593493
Sury, McShane, Hernandez-Miranda, Birchmeier, Selbach et al.: Quantitative proteomics reveals dynamic interaction of c-Jun N-terminal kinase (JNK) with RNA transport granule proteins splicing factor proline- and glutamine-rich (Sfpq) and non-POU ... in Molecular & cellular proteomics : MCP 2015
These findings further validated the involvement of P. acnes in the pathology of intervertebral disc degeneration (IVDD) and provided evidence that P. acnes-induced apoptosis of NPCs via the TLR2/JNK pathway is likely responsible for the pathology of IVDD.
CXCL12 (show CXCL12 Proteins) activates the MEKK1 (show MAP3K1 Proteins)/JNK signaling pathway, which in turn initiates SMAD3 (show SMAD3 Proteins) phosphorylation, its translocation to nuclei, and recruitment of SMAD3 (show SMAD3 Proteins) to the CTGF (show CTGF Proteins) promoter, which ultimately induces CTGF (show CTGF Proteins) expression in human lung fibroblasts.
Activation of the c-Jun NH2-terminal kinase pathway by coronavirus infectious bronchitis virus promotes apoptosis independently of c-Jun (show JUN Proteins).
Inhibition of each TGFbeta (show TGFB1 Proteins) receptor-I, glucocorticoid receptor (show NR3C1 Proteins) or JNK signaling partially reversed the dexamethasone-mediated effects, suggesting a complex signaling network. These data reveal that dexamethasone mediates progression by membrane effects and binding to glucocorticoid receptor (show NR3C1 Proteins)
JNK inhibitor prevents SIRT1 (show SIRT1 Proteins) phosphorylation, leading to elevated SIRT1 (show SIRT1 Proteins) protein levels even in the presence of H2O2. Taken together, our results indicate that CHFR plays a crucial role in the cellular stress response pathway by controlling the stability and function of SIRT1 (show SIRT1 Proteins).
Findings suggest that during lipoapoptosis, HCV infection may enhance hepatocyte toxicity by increasing JNK phosphorylation.
High JNK expression is associated with non-small-cell lung cancer.
These data suggested that Annexin A2 (show ANXA2 Proteins) induces cisplatin resistance of non-small cell lung cancer (NSCLC)via regulation of JNK/c-Jun/p53 (show TP53 Proteins) signaling, and provided an evidence that blockade of Annexin A2 (show ANXA2 Proteins) could serve as a novel therapeutic approach for overcoming drug resistance in NSCLCs
Data suggest that H2O2 regulates cell death in granulosa cells via the ROS (show ROS1 Proteins)-JNK-p53 (show TP53 Proteins) pathway.
High expression of JNK is associated with invasion of gastric cancer.
Findings indicate the MIG-15/JNK-1 pathway can restrict both glutamatergic synapse formation and short-term learning.
Our genetic study unravelled the underlying pathway where JNK-1 is acting independently of insulin (show INS Proteins)-IGF-1 (show IGF1 Proteins) signalling (IIS) pathway to modulate longevity. In support of in vivo results in silico docking study of UA with C. elegans JNK-1 ATP-binding site suggested promising binding affinity exhibiting binding energy of -8.11 kcalmol(-1). UA induced JNK-1 activation in wild-type animals underlie the importance of pharmacologi
JNK-1 directly interacts with and phosphorylates DAF-16. Moreover, in response to heat stress, JNK-1 promotes the translocation of DAF-16 into the nucleus.
The present study shows in Caenorhabditis elegans that ambient temperature (1-37 degrees C) specifically influences the activation (phosphorylation) of the MAP kinase JNK-1 as well as the nuclear translocation of DAF-16.
the stress response is controlled by a c-Jun N-terminal kinase (JNK)-like mitogen-activated protein kinase (show MAPK1 Proteins) (MAPK (show MAPK1 Proteins)) signaling pathway, which is regulated by MLK-1 (show MAP3K9 Proteins) MAPK (show MAPK1 Proteins) kinase kinase (MAPKKK), MEK-1 (show MAP2K1 Proteins) MAPK (show MAPK1 Proteins) kinase (MAPKK), and KGB-1 (show KCNJ3 Proteins) JNK-like MAPK (show MAPK1 Proteins).
High JNK expression is associated with cerebral ischaemia reperfusion injury.
Noise exposure led to enhanced JNK phosphorylation and IRS1 (show IRS1 Proteins) serine phosphorylation as well as reduced Akt (show AKT1 Proteins) phosphorylation in skeletal muscles in response to exogenous insulin (show INS Proteins) stimulation.
Prdx1 (show PRDX1 Proteins) knockout can aggravate the oxidative stress and lung injury by increasing the level of Reactive Oxygen Species (ROS (show ROS1 Proteins)), and also activate P38 (show CRK Proteins)/JNK signaling pathway.
Data identify a unique signal crosstalk between Wnt (show WNT2 Proteins) signaling and the MAP3K1 (show MAP3K1 Proteins)-JNK pathway in epithelial morphogenesis.
Therefore, APP (show APP Proteins) modulates Nav1.6 (show SCN8A Proteins) sodium channels through a Go-coupled JNK pathway, which is dependent on phosphorylation of APP (show APP Proteins) at Thr668.
These interactions are required for SRC (show SRC Proteins)-induced activation of VAV (show VAV1 Proteins) and the subsequent engagement of a JIP1 (show MAPK8IP1 Proteins)-tethered JNK signaling module.
this study establishes that JNK1 is a key mediator of osteoblast function in vivo and in vitro.
Jnk1 deficiency inhibits the development of neural stem cells/precursors
Suppressing P38 (show CRK Proteins) promoted adipogenic trans-differentiation and intensified adipolytic metabolism in differentiated cells. However, inhibition of ERK1/2 had the opposite effects on adipogenesis and no effect on adipolysis. Blocking JNK weakly blocked trans-differentiation but stimulated adipolysis and induced apoptosis.
Cell fusion during wound healing in Drosophila larval epidermis occurred primarily in the wound vicinity, where JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins) activation was suppressed by fusion-inducing JNK signaling.
aken together, these results reveal that inactivation of Rpd3 (show HDAC1 Proteins) independently regulates JNK and Yki (show YAP1 Proteins) activities and that both Hippo and JNK signaling pathways contribute to Rpd3 (show HDAC1 Proteins) RNAi-induced apoptosis.
Data show that JNK signalling inhibits the growth of losers, while JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins) signalling promotes competition-induced winner cell proliferation.
Here we uncover a cell non-autonomous requirement for the Epidermal growth factor receptor (Egfr (show EGFR Proteins)) pathway in the lateral epidermis for sustained dpp (show TGFb Proteins) expression in the LE. Specifically, we demonstrate that Egfr (show EGFR Proteins) pathway activity in the lateral epidermis prevents expression of the gene scarface (scaf), encoding a secreted antagonist of JNK signaling
n addition to significantly increasing the number of JNK target genes identified so far, our results reveal that the LE is a highly heterogeneous morphogenetic organizer, sculpted through crosstalk between JNK, segmental and AP signalling. This fine-tuning regulatory mechanism is essential to coordinate morphogenesis and dynamics of tissue sealing
malignant transformation of the ras(V12)scrib(1 (show SCRIB Proteins)) tumors requires bZIP protein Fos, the ETS (show ETS1 Proteins)-domain factor Ets21c and the nuclear receptor Ftz-F1 (show NR5A2 Proteins), all acting downstream of Jun-N-terminal kinase.
Diminished MTORC1-dependent JNK activation underlies the neurodevelopmental defects associated with lysosomal dysfunction.
ROS (show ROS1 Proteins)/JNK/p38 (show MAPK14 Proteins)/Upd (show UROD Proteins) stress responsive module restores tissue homeostasis. This module is not only activated after cell death induction but also after physical damage and reveals one of the earliest responses for imaginal disc regeneration.
Significantly, the JNK pathway is responsible for the majority of the phenotypes and transcriptional changes downstream of Notch (show NOTCH1 Proteins)-Src (show SRC Proteins) synergy.
This study demonstrated that the mechanism by which Bsk (show FRK Proteins) is required for pruning is through reducing the membrane levels of the adhesion molecule (show NCAM1 Proteins) Fasciclin II (show NCAM2 Proteins) (FasII)
Porcine reproductive and respiratory syndrome virus -activated TAK-1 (show NR2C2 Proteins) was essential for the activation of JNK and NF-kappaB (show NFKB1 Proteins) pathways and IL-8 (show IL8 Proteins) expression.
Data show that proinflammatory cytokines induction was ERK1/2 and JNK1/2 dependent.
These data suggest that the p38 (show MAPK14 Proteins) and JNK signaling pathways play pivotal roles in PRRSV replication and may regulate immune responses during virus infection.
based on the data, we can conclude that JNK plays an active role in fragmentation of pig oocytes and that p38 MAPK (show MAPK14 Proteins) is not involved in this process
Retinal ischemia-reperfusion alters expression of mitogen-activated protein kinases, particularly ERK1/2, in the neuroretina and retinal arteries.
PP2A (show PPP2R2B Proteins) and AIP1 (show PDCD6IP Proteins) cooperatively induce activation of ASK1 (show MAP3K5 Proteins)-JNK signaling and vascular endothelial cell apoptosis.
Phorbol 12-myristate 13-acetate activation of ERK (show MAPK1 Proteins) and JNK signaling is relevant in the regulation of gene expression during follicular development, ovulation, and luteinization.
study reports MPK8 connects protein phosphorylation, Ca(2 (show CA2 Proteins))+ and ROS (show ROS1 Proteins) in wound-signaling pathway; suggests 2 major activation modes, Ca(2 (show CA2 Proteins))+/CaMs and MAP kinase (show MAPK1 Proteins) phosphorylation cascade, converge at MPK8 to monitor or maintain an essential part of ROS (show ROS1 Proteins) homeostasis
The results of this study suggest that JNK has a role in the disassembly adherens junctions by means of endocytosis that is required during buccopharyngeal membrane perforation.
Hyperosmotic Shock Engages Two Positive Feedback Loops through Caspase-3 (show CASP3 Proteins)-dependent Proteolysis of JNK1-2 and Bid (show BID Proteins).
JNK signaling is required to establish microtubule stability and maintain tissue cohesion in the gut (show GUSB Proteins).
Data show that the death pathway is independent of ERK (show MAPK1 Proteins) but relies on activating Bad phosphorylation through the control of both kinases Cdk1 (show CDK1 Proteins) and JNK.
our data provide strong evidence that Jip3 in fact serves as an adapter protein linking these cargos to dynein
P38 (show MAPK14 Proteins) and JNK have opposing effects on persistence of in vivo leukocyte migration in zebrafish.
A dorsalization pathway that is exerted by Axin (show AXIN1 Proteins)/JNK signaling and its inhibitor Aida (show AIDA Proteins) during vertebrate embryogenesis, is defined.
JNK-Mmp13 (show MMP13 Proteins) signaling pathway plays an essential role in regulating the innate immune cell migration in response to severe injury in vivo
Suggest that hypoxia-induced modified cells engage the PDGFbeta-R-JNK1 axis to confer distinctively heightened proliferation and adventitial remodelling in pulmonary hypertension.
These data suggest a differential requirement of JNK1 and p38 MAPK (show MAPK14 Proteins) in TNF (show TNF Proteins) regulation of E2F1 (show E2F1 Proteins). Targeted inactivation of JNK1 at arterial injury sites may represent a potential therapeutic intervention for ameliorating TNF (show TNF Proteins)-mediated EC dysfunction.
PKD (show PRKD1 Proteins) is a critical mediator in H2O2- but not TNF (show TNF Proteins)-induced ASK1 (show MAP3K5 Proteins)-JNK signaling
ATF3 (show ATF3 Proteins) induction by acute hypoxia is mediated by nitric oxide and the JNK pathway in endothelial cells
JNK plays an important role in the induction of apoptosis in transformed bovine brain endothelial cells stimulated by LPS (show IRF6 Proteins)
The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various cell stimuli, and targets specific transcription factors, and thus mediates immediate-early gene expression in response to cell stimuli. The activation of this kinase by tumor-necrosis factor alpha (TNF-alpha) is found to be required for TNF-alpha induced apoptosis. This kinase is also involved in UV radiation induced apoptosis, which is thought to be related to cytochrom c-mediated cell death pathway. Studies of the mouse counterpart of this gene suggested that this kinase play a key role in T cell proliferation, apoptosis and differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
JUN N-terminal kinase
, MAP kinase 8
, c-Jun N-terminal kinase 1
, mitogen-activated protein kinase 8 isoform JNK1 alpha1
, mitogen-activated protein kinase 8 isoform JNK1 beta2
, stress-activated protein kinase 1
, stress-activated protein kinase 1c
, JNK1 beta1 protein kinase
, MAPK 8
, mitogen activated protein kinase 8
, protein kinase mitogen-activated 8
, stress-activated protein kinase JNK1
, SAPK gamma
, c-jun NH2-terminal kinase
, p54 gamma
, JUN kinase
, Jun N-terminal kinase
, Jun NH2-terminal kinase
, Jun-N-terminal kinase
, c-Jun N-terminal kinase
, c-Jun aminoterminal kinase
, c-Jun-N-terminal kinase
, drosophila JNK
, janus kinase 1
, mitogen-activated protein kinase 8
, LOW QUALITY PROTEIN: mitogen-activated protein kinase 8B-like
, MAP kinase 8B
, MAPK 8B
, Mitogen-activated protein kinase 8B
, Stress-activated protein kinase JNKb
, c-Jun N-terminal kinase B