|Application ||WB, IHC-P, E|
|Other Accession||P49187, Q61831, P53779, Q8QHK8, P49185, Q91Y86, NP_620637|
|Predicted||Mouse, Rat, Xenopus|
|Calculated MW||48296 Da|
|Antigen Region||159-195 aa|
|Other Names||Mitogen-activated protein kinase 8, MAP kinase 8, MAPK 8, JNK-46, Stress-activated protein kinase 1c, SAPK1c, Stress-activated protein kinase JNK1, c-Jun N-terminal kinase 1, MAPK8, JNK1, PRKM8, SAPK1, SAPK1C|
|Target/Specificity||This MAPK8 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 159-195 amino acids from human MAPK8.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MAPK8 Antibody (T183/Y185) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||JNK1, PRKM8, SAPK1, SAPK1C|
|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 (PubMed:22441692).|
|Cellular Location||Cytoplasm. Nucleus|
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Provided below are standard protocols that you may find useful for product applications.
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.
Dasgupta, J., et al. J. Cell. Physiol. 225(1):52-62(2010)
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Gao, D., et al. J. Biol. Chem. 285(39):29965-29973(2010)
Han, J.S., et al. Anticancer Res. 30(9):3407-3412(2010)
Yang, X.H., et al. World J. Gastroenterol. 16(27):3385-3393(2010)
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