Recombinant Human JNK1 Protein (GST Tag)

Name: Recombinant Human JNK1 Protein (GST Tag)
Brand: Beta LifeScience
SKU: BLPSN-3050
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NP_620637.1
Synonym	JNK, JNK-46, JNK1, JNK1A2, JNK21B1/2, PRKM8, SAPK1, SAPK1c
Background	Mitogen-activated protein kinase 8 (MAPK8), also known as JNK1, 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. The protein kinases JNK1 has been found to serve as critical molecular links between obesity, metabolic inflammation, and disorders of glucose homeostasis. It is critically involved in the promotion of diet-induced obesity, metabolic inflammation and beta-cell dysfunction. The selective deficiency of JNK1 in the murine nervous system is sufficient to suppress diet-induced obesity. Genetic analysis indicates that the effects of JNK1 can be separated from effects of JNK1 on obesity. JNK1 is a potential pharmacological target for the development of drugs that might be useful for the treatment of metabolic syndrome, and type 2 diabetes. Furthermore, JNK1 plays a major role in the hypoxic cellular damage. JNK1 protein might be an attractive target for antihypoxic therapy in increasing resistance to many pathological conditions and diseases, leading to the oxygen deficit.
Description	A DNA sequence encoding the full length of human MAPK8 isoform JNK1 alpha 2 (NP_620637.1) (Met 1-Arg 427) was expressed with the GST tag at the N-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met
AA Sequence	Met 1-Arg 427
Molecular Weight	The recombinant human MAPK8/GST chimera consists of 652 a.a. and predicts a molecular mass of 75 kDa. It migrates as an approximately 65 kDa band in SDS-PAGE under reducing conditions.
Purity	>90% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0, 25% glycerol.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. 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 MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates the heat shock transcription factor HSF1, suppressing HSF1-induced transcriptional activity. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation. Phosphorylates JUND and this phosphorylation is inhibited in the presence of MEN1. In neurons, phosphorylates SYT4 which captures neuronal dense core vesicles at synapses. Phosphorylates EIF4ENIF1/4-ET in response to oxidative stress, promoting P-body assembly.; JNK1 isoforms display different binding patterns: beta-1 preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms.
Subcellular Location	Cytoplasm. Nucleus. Cell junction, synapse.
Protein Families	Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
Database References	HGNC: 6881 OMIM: 601158 KEGG: hsa:5599 STRING: 9606.ENSP00000353483 UniGene: Hs.138211

Gene Functions References

results revealed that melatonin attenuated chemokine CCL24 levels through inhibition of the JNK pathway to hinder human osteosarcoma cell invasion, thereby highlighting the therapeutic potential of melatonin for osteosarcoma metastasis. PMID: 29766567
JNK acts as a key mediator of muscle remodeling during exercise via regulation of myostatin/SMAD signaling. PMID: 30072727
Data show that overexpression of protein-tyrosine phosphatase 1B (PTP1B) activated the c-Jun N-terminal kinase (JNK) signaling pathway. PMID: 29928877
HMBG2 overexpression promotes ischemia/reperfusion-induced cell apoptosis through activating the JNK1/2-NF-kappaBp65 signaling in AC16 cardiomyocytes. PMID: 30119172
JNK1 and VDR act as tumor suppressors, and their stromal expression levels are associated with prognosis in esophageal squamous cell carcinoma. PMID: 29423673
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. PMID: 29323102
CXCL12 activates the MEKK1/JNK signaling pathway, which in turn initiates SMAD3 phosphorylation, its translocation to nuclei, and recruitment of SMAD3 to the CTGF promoter, which ultimately induces CTGF expression in human lung fibroblasts. PMID: 29499695
Activation of the c-Jun NH2-terminal kinase pathway by coronavirus infectious bronchitis virus promotes apoptosis independently of c-Jun. PMID: 29238080
Inhibition of each TGFbeta receptor-I, glucocorticoid receptor 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 PMID: 28981109
JNK inhibitor prevents SIRT1 phosphorylation, leading to elevated SIRT1 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. PMID: 27883020
Findings suggest that during lipoapoptosis, HCV infection may enhance hepatocyte toxicity by increasing JNK phosphorylation. PMID: 28931802
High JNK expression is associated with non-small-cell lung cancer. PMID: 28104581
These data suggested that Annexin A2 induces cisplatin resistance of non-small cell lung cancer (NSCLC)via regulation of JNK/c-Jun/p53 signaling, and provided an evidence that blockade of Annexin A2 could serve as a novel therapeutic approach for overcoming drug resistance in NSCLCs PMID: 28886730
Data suggest that H2O2 regulates cell death in granulosa cells via the ROS-JNK-p53 pathway. PMID: 28445976
High expression of JNK is associated with invasion of gastric cancer. PMID: 28534988
JNK activation and signaling in extrahepatic cholangiocarcinoma is regulated by L1CAM.JNK role in cell migration in extrahepatic cholangiocarcinoma. PMID: 28535665
Thus, the present study indicated that parkin knockout inhibits neural stem cell differentiation by JNK-dependent proteasomal degradation of p21. PMID: 28656059
JNK activation contributes to glioma cell parthanatos caused by oxidative stress via increase of intracellular reactive oxygen species generation. PMID: 27181592
TGM2 is involved in amyloid-beta (1-42)-induced pro-inflammatory activation via AP1/JNK signaling pathways in cultured monocytes. PMID: 27864692
NleL-induced JNK ubiquitylation, particularly mono-ubiquitylation at the Lys 68 residue of JNK, impairs JNK's interaction with an upstream kinase MKK7, thus disrupting JNK phosphorylation and activation. PMID: 28753655
The surface immune molecule CD274 plays a critical role in the proliferation of leukemia-initiating cells, LICs. The CD274/JNK/Cyclin D2 pathway promotes the cell cycle entry of LIC. PMID: 27855694
These data implicate HTRA1 as a negative regulator of mesenchymal stem cell adipogenesis. PMID: 26864869
these data provide new evidence for an indispensable role for JNK/SAPK signaling to overcome the well-established molecular barriers in human somatic cell induced reprogramming. PMID: 26867034
Our findings indicate that GADD45 essentially suppresses the MKK7-JNK pathway and suggest that differentially expressed GADD45 family members fine-tune stress-inducible JNK activity. PMID: 29037961
Quantitative phosphoproteomic analysis identifies the critical role of JNK1 in neuroinflammation induced by Japanese encephalitis virus PMID: 27703031
post-translational modification facilitates the mobilization of SIRT6 to DNA damage sites and is required for efficient recruitment of poly (ADP-ribose) polymerase 1 (PARP1) to DNA break sites and for efficient repair of double-strand break. PMID: 27568560
PRDM5 promotes the proliferation and invasion of murine melanoma cells through up-regulating JNK expression and strategies targeting PRDM5 may be promising for the therapy of melanoma. PMID: 27485778
This study showed that the induction level of IL-32 was increased in chronic rhinosinusitis with nasal polyps compared to normal nasal mucosa and that LPS-induced IL-32 expression in nasal polyp-derived fibroblasts was regulated via the TLR4/JNK/AKT/CREB signaling pathway. PMID: 27173130
These results suggest that Bacteroides fragilis enterotoxin induced accumulation of autophagosomes in endothelial cells, but activation of a signaling pathway involving JNK, AP-1, and CHOP may interfere with complete autophagy. PMID: 28694294
The data suggested that JNK-enhanced Tudor-SN phosphorylation promotes the interaction between Tudor-SN and G3BP and facilitates the efficient recruitment of Tudor-SN into stress granules under conditions of sodium arsenite-induced oxidative stress. PMID: 28011284
Taken together, our data demonstrate that JNK regulates triple-negative breast cancer (TNBC)tumorigenesis by promoting CSC phenotype through Notch1 signaling via activation of c-Jun and indicate that JNK/c-Jun/Notch1 signaling is a potential therapeutic target for TNBC PMID: 27941886
Here, the authors show that the CDK inhibitor p21 (CDKN1A) maintains the viability of DNA damage-induced senescent cells. Upon p21 knockdown, senescent cells acquired multiple DNA lesions that activated ataxia telangiectasia mutated (ATM) and nuclear factor (NF)-kappaB kinase, leading to decreased cell survival. NF-kappaB activation induced TNF-alpha secretion and JNK activation to mediate death of senescent cells in a... PMID: 28607003
Results indicate that cordycepin promotes caveolin-1 (CAV1)upregulation to enhance c-jun N-terminal kinase (JNK)/forkhead box O3A protein (Foxo3a) signaling pathway activation, inducing apoptosis in lung cancer cells. PMID: 28099944
The combination of 2-deoxyglucose (2-DG) and ABT-199 initiated cell death through the reduction of myeloid cell leukemia sequence 1 protein (Mcl-1) expression and c-Jun N-terminal kinase 1 (JNK1) activation and subsequent Bcl-xL protein degradation. PMID: 28038464
identified the c-Jun N-terminal kinase 1 (JNK1) as the kinase involved in the phosphorylation of NEIL1 PMID: 27518429
The increase in c-Jun N-terminal kinase (c-Jun) and specificity protein 1 (SP1) expressions was positively correlated with transforming growth factor beta 1 (TGFbeta1) in both high glucose-treated renal mesangial cells (HRMCs) and diabetic kidneys. PMID: 27112839
JNK1 physically and functionally interacted with VDR and positively regulated VDR expression at transcriptional and translational levels, which influenced calcitriol-mediated inhibition of cancer cell proliferation. PMID: 27174721
In conclusion, our findings revealed DIP2 as a novel effector downstream of Bsk modulating the direction of axon projection. PMID: 28396149
The release of infectious respiratory syncytial virus (RSV) virions from infected cells was significantly reduced by JNK1/2 siRNA knockdown, implicating JNK1/2 as a key host factor for RSV virus production. PMID: 28062184
dMyc has an essential role in preventing JNK-mediated retinal glial activation PMID: 28267791
the results identify the JNK/S6K1 axis as a key molecular mechanism whereby a high fat/sucrose diet impairs insulin action in retina. PMID: 27965359
PXR regulates the intestinal epithelial barrier during inflammation by modulating cytokine-induced MLCK expression and JNK1/2 activation PMID: 27440420
hese results indicate that DHA induces apoptosis of BGC-823 cells through JNK1/2 and p38 MAPK signaling pathways and DHA could serve as a potential additional chemotherapeutic agent for treatment of gastric cancer. PMID: 27401020
MUC1 promotes hepatocellular carcinoma progression and tumorigenesis and mediates autocrine TGF-b signaling by activating the JNK/AP-1 pathway in hepatocellular carcinoma cells, and makes MUC1 and JNK as attractive targets for hepatocellular carcinoma therapy. PMID: 28012230
Allograft tumor assays in mice demonstrate that this mechanism contributes to tumorigenesis driven by mutant IDH1, a result confirmed by detection of JNK inactivation in human gliomas harboring IDH1-R132H mutations. PMID: 28402860
Pretreatment by IRE1 agonist tunicamycin or JNK agonist anisomycin attenuated the effect of psoralen on osteoporotic osteoblasts. Psoralen inhibited apoptosis of osteoporotic osteoblasts by regulating IRE1-ASK1-JNK pathway PMID: 28349059
Therapeutic interventions of potent and selective inhibitors of JNK might provide promising therapeutic approaches for the treatment of OS, and could improve the survival rate and quality of life of OS patients. PMID: 26669256
the results obtained from RRD, QPLD, IFD and MD simulations indicated that lead1 might be used as a potent antagonist toward human JNK1 in cancer therapeutics. PMID: 26906522
Data indicate that STK40 was a direct target of microRNA miR-130a, and overexpressing miR-130a significantly upregulated NF-kappaB p65, SOX9, JNK and p38MAPK proteins. PMID: 28085489
Results suggest that curcumin induced the apoptosis of retinoblastoma Y79 cells through the activation of c-Jun N-terminal kinase (JNK) and p38 mitogen-activated protein kinase (MAPK) pathways. PMID: 27432244

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