Recombinant Human Mitogen-Activated Protein Kinase 9 (MAPK9) Protein (His-SUMO)

Name: Recombinant Human Mitogen-Activated Protein Kinase 9 (MAPK9) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04240P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Mitogen-Activated Protein Kinase 9 (MAPK9) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P45984
Target Symbol	MAPK9
Synonyms	c Jun kinase 2; C Jun N terminal kinase 2; c-Jun N-terminal kinase 2; JNK 55; JNK-55; JNK2 alpha; JNK2; JNK2 beta; JNK2A; JNK2alpha; JNK2B; JNK2BETA; Jun kinase; MAP kinase 9; MAPK 9; Mapk9; Mitogen activated protein kinase 9; Mitogen-activated protein kinase 9; MK09_HUMAN; P54a; p54aSAPK; PRKM9; Protein kinase, mitogen-activated, 9; SAPK alpha; SAPK; SAPK1a; Stress activated protein kinase 1a; Stress-activated protein kinase JNK2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVVKDQPSDAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR
Expression Range	1-424aa
Protein Length	Full Length
Mol. Weight	64.1kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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 MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation.; MAPK9 isoforms display different binding patterns: alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
Database References	HGNC: 6886 OMIM: 602896 KEGG: hsa:5601 STRING: 9606.ENSP00000389338 UniGene: Hs.484371

Gene Functions References

Taken together, the silencing of H4R inhibited the H4R mediated Mast cell functions and SAPK/JNK phosphorylation. Furthermore, the H4R activation utilized SAPK/JNK signaling pathway for IL-1beta release in HMC-1 cells. PMID: 29863427
RhoGDIbeta overexpression led to downregulation of miR-200c, whereas miR-200c was able directly to target 3'-UTR of jnk2mRNA and attenuated JNK2 protein translation, which resulted in attenuation of Sp1mRNA and protein expression in turn, inhibiting Sp1-dependent MMP-2 transcription. PMID: 28846829
The MAP kinase JNK2 mediates cigarette smoke-induced tissue factor activation, arterial thrombosis and reactive oxygen species production. PMID: 27761579
We found p-JNK2 up-regulation in AUC and its early down-regulation in UC-CRC and CRC carcinogenesis. PMID: 28383667
JNK2 was a novel direct target of miR-20a-5p. PMID: 27494776
Interleukin-1 acts via the JNK-2 signaling pathway to induce aggrecan degradation by human chondrocytes. PMID: 25776267
miR200c attenuates P-gp-mediated MDR and metastasis by targeting JNK2/c-Jun signaling pathway in colorectal cancer. PMID: 25205654
JNK2 activates pro-survival autophagy and inhibits palmitic acid lipotoxicity in hepatocytes. PMID: 24608675
Our findings demonstrate that AKT/mTOR and JNK2 signaling pathways are required for chrysotile asbestos-induced autophagy PMID: 24735948
These results indicate that JNK2 is essential for maintenance of normal intestinal epithelial homeostasis and maturation under biological conditions by differentially modulating HuR and CUGBP1. PMID: 24740539
After overexpression and knockdown of XIAP, the AKT, pAKT, JNK2 and GSK3beta levels were determined in periodontal ligament cells. PMID: 24802394
This study demonstrates that cyclic stretch disrupts tight junctions and adherens junctions by a JNK2, c-Src, and MLCK-dependent mechanism. PMID: 24722904
Poly(ADP-ribose) polymerase family member 14 (PARP14) is a novel effector of the JNK2-dependent pro-survival signal in multiple myeloma. PMID: 23045269
SREBP-1c is a novel insulin/JNK2-regulated gene and that the JNK2/SREBP-1c pathway mediates insulin-induced fatty acid synthesis, which may lead to enlargement of LDs in human adipocytes. PMID: 23515281
JNK2 is activated during endoplasmic reticulum stress and promotes cell survival. PMID: 23171849
Data indicate that WDR62 dimerization is required for JNK2 and MKK7beta1 recruitment. PMID: 23341463
We observed that the phosphorylated expression of JNK2 was upregulated in the skin of patients with hypospadias compared with that in the normal prepuce in the levels of mRNA and protein. PMID: 23273084
the effect of APRIL is mediated via BCMA, which does not activate the classical NF-kappaB pathway, whereas it induces a novel signaling pathway, which involves JNK2 phosphorylation, FOXO3A activation, and GADD45 transcription PMID: 23071284
JNK2 regulated nucleolin expression and might in turn stabilize hif-1alpha mRNA. PMID: 22910906
SEPW1 silencing increases MKK4, which activates p38gamma, p38delta, and JNK2 to phosphorylate p53 on Ser-33 and cause a transient G(1) arrest. PMID: 22730327
ulinastatin inhibits the proliferation of human breast cancer cells and the growth of xenografted tumors.This mechanism might be related to decreasing signal transduction of JNk-2 and NF-kappaB. PMID: 22217202
up-regulation of hepatic MRP3/ABCC3 expression in human obstructive cholestasis is likely triggered by TNFalpha, mediated by activation of JNK/SAPK and SP1. PMID: 22105759
JNK/SAPK signal pathway plays an important role in regulating bFGF-mediated angiogenesis in HUVECs PMID: 21572099
WDR62 signaling association with JNK2 requires both the JNK2 Cys-Asp (CD) and Glu-Asp (ED) domains. PMID: 21749326
critical role for JNK2 and EPS8 in receptor tyrosine kinase signaling and trafficking to convey distinctly different effects on cell migration. PMID: 21357683
JNK2alpha3 and JNK2beta3 showed different levels of substrate phosphorylation, although they both could promote the proliferation of 293T cells. PMID: 21110917
these data demonstrates for the first time that JNK2a can regulate the transcriptional activity of STAT3 by phosphorylating the Ser727 residue, thereby regulating the expression of oncogenic genes, such as c-Myc. PMID: 20871632
The role of JNK2 in the mechanism of osmotic stress-induced tight junction disruption in the intestinal epithelium in 3 species is described. PMID: 20595622
JNK2 collaborates with other oncogenes, such as Ras, at multiple molecular levels to promote tumorigenesis PMID: 20354187
Our results indicate that the activation of phosphorylated c-Jun NH2-terminal kinase may play a role in the carcinogenesis of basal-like and triple-negative breast carcinoma. PMID: 19913278
Protein kinase D complexes with C-Jun N-terminal kinase via activation loop phosphorylation and phosphorylates the C-Jun N-terminus. PMID: 11948398
involves TRAF4 in oxidative activation PMID: 12023963
biochemical pathway exists wherein fluid shear activates cyclooxygenase-2, via a c-Jun N-terminal kinase2/c-Jun-dependent pathway, which in turn elicits downstream prostaglandin EP2 and EP3a1 receptor mRNA synthesis PMID: 12743126
JNK2 functions in maintaining the genomic stability of mammalian cells by signaling that is independent of cyclin-dependent kinase 1/cyclin B1 down-regulation. PMID: 15262983
analysis of the regions required for JNK2alpha2 autophosphorylation PMID: 15637069
JIP1 and JIP3, have a cross-talk that leads to the regulation of the ASK1-SEK1-JNK signal during glucose deprivation; cross-talk between JIP3 and JIP1 is mediated through SEK1-JNK2 and Akt1. PMID: 15911620
results indicate that the aberrant p-JNK1/2 expression and the co-expressed p-JNK1/2 and p-p38 in breast tissues may play a role in the carcinogenesis of breast IDC PMID: 16381010
Results showed that certain regulation involved in c-myc, c-fos, and c-jun was present in the apoptosis, and the c-Myc dependent-on and Jun N-terminal kinase (JNK) pathway also play roles. PMID: 16552729
we defined the kinetic mechanism for the active form of JNK2alpha2. PMID: 17397142
Results indicate that purified JNK2 from transfected nonstressed 293T cells is a mixture of the mono-sites pThr183 and pTyr185 of its activation loop and of pThr386 along its unique C-terminal region. PMID: 17637567
Neutrophils from transgenic JNK2 knockout mice (which are devoid of all JNK isoforms) demonstrate a requirement for JNK2 in Toxoplasma gondii infection-induced interleukin-12p40 and CCL2/MCP-1 production. PMID: 17785791
These findings are consistent with JNK2 signaling playing a protective role in acetaminophen-induced liver injury. PMID: 18586006
Player in triglyceride (TG) homeostasis and lipid droplet metabolism and, more specifically, in the regulation of lipolysis. PMID: 18612143
Results suggest that the MAP kinase insert of JNK2 plays a role in the regulation of JNK2 activation, possibly by interacting with intracellular binding partners. PMID: 18801372
JNK2 is linked, directly or indirectly, with SIRT1 protein stability and that this function is coupled with SIRT1 phosphorylation at serine 27. PMID: 18838864
JNK2 alpha2 activity is dependent on a unique mechanism of MAPK activation PMID: 18940813
detection of the mutation could characterize a subset of ET patients with distinct phenotype, despite its clinical significance being still undetermined PMID: 19093167
Knock-down of JNK2 unexpectedly increased the intensity of differentiation intensity in human myeloid leukemia cells. PMID: 19339050
Both cell protective (cell cycle progression) and destructive mechanisms (apoptosis) are simultaneously controlled by a single JNK isoform in the same cell system even under the influence of one stimulus. PMID: 19385049
NAG7 plays a potential role in promoting nasopharyngeal carcinoma invasion by regulation of ERalpha and the H-ras/p-c-Raf and JNK2/AP-1/MMP1 signaling pathways. PMID: 19591174

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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