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anti-Mouse (Murine) MAPKAP Kinase 5 Antibodies:
anti-Human MAPKAP Kinase 5 Antibodies:
anti-Rat (Rattus) MAPKAP Kinase 5 Antibodies:
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Human Monoclonal MAPKAP Kinase 5 Primary Antibody for IHC, ELISA - ABIN969362
Paliga, Natale, Watson: p38 mitogen-activated protein kinase (MAPK) first regulates filamentous actin at the 8-16-cell stage during preimplantation development. in Biology of the cell / under the auspices of the European Cell Biology Organization 2005
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Human Monoclonal MAPKAP Kinase 5 Primary Antibody for ELISA, WB - ABIN532682
Sun, Yoshizuka, New, Moser, Li, Liao, Xie, Chen, Deng, Yamout, Dong, Frangou, Yates, Wright, Han: PRAK is essential for ras-induced senescence and tumor suppression. in Cell 2007
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Human Polyclonal MAPKAP Kinase 5 Primary Antibody for ELISA, WB - ABIN543741
Ni, Wang, Diener, Yao: MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase. in Biochemical and biophysical research communications 1998
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Human Polyclonal MAPKAP Kinase 5 Primary Antibody for ICC, IF - ABIN4347179
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. in Nature methods 2013
MK5 is being discussed as a putative novel regulator of cardiac fibroblast function. (Review)
MK5 haplodeficiency attenuated the progression of hypertrophy, reduced collagen type 1 mRNA, and protected diastolic function in response to chronic pressure overload.
An alternative targeting strategy of MK5/PRAK (termed MK5/PRAK-Deltaex6) increased neither tumor incidence in the one step skin carcinogenesis model, nor Ras-induced transformation in primary cells.
MK5 positively regulates Rag transcription via phosphorylation of Foxo1 in developing B cells.
observations have demonstrated that PRAK is not required for either the rottlerin-mediated anti-chlamydial activity or rottlerin inhibition of sphingolipid trafficking, suggesting rottlerin may achieve its inhibitory role by targeting other host factors
Results suggest that PRAK may function as a tumor suppressor in multiple types of cancers.
the regulation of neuronal morphogenesis is proposed as the first physiological function of the ERK3/MK5 signaling module
It was shown that the tumor-suppressing and tumor-promoting functions of the p38-PRAK pathway are temporally and spatially separated during cancer development in vivo, relying on the stimulus, and the tissue type and the stage of cancer development.
Rheb inactivation by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1
MK5 co-immunoprecipitated ERK3, but not ERK4 or p38 alpha, in control and hypertrophying hearts (MK5).
Both binding and activation of p38 mitogen-activated protein kinase (MAPK) play essential roles in regulation of the nucleocytoplasmic distribution of MAPK-activated protein kinase 5 by cellular stress.
Data suggest that the differences between the phenotypes of MK5- and MK2-deficient mice result from clearly different functional properties of both enzymes.
Data show that extracellular-regulated kinase 3 (ERK3) specifically interacts with the MAPK-activated protein kinase 5 (MK5 or PRAK) in vitro and in vivo.
Results demonstrate a specific interaction between extracellular signal-regulated kinase 3 (ERK3) and mitogen-activated protein kinase-activated protein kinase-5 (MK5).
We propose that phosphorylation of p53 by PRAK following activation of p38 MAPK by ras plays an important role in ras-induced senescence and tumor suppression.
multiple determinants control the distinct subcellular localization of p38alpha-PRAK and p38beta-PRAK complexes, and the location of PRAK plays a role in its function
Several binding motifs for heat shock factor are dispersed in the mouse and rat promoter, and temperature shock transiently enhanced the MAP-kinase-activated kinase 5 transcript levels.
PRAK might be a potential therapeutic target of Alzheimer's disease involved in receptor for advanced glycation end products-mediated cell signaling induced by Abeta
Plasma MAPKAPK5 protein was found to positively associate with the 10-year change in paired associates learning assessment in asymptomatic older twins.
Data highlight that DJ-1 is the downstream interacting target for PRAK, and in response to oxidative stress PRAK may exert a cytoprotective effect by facilitating DJ-1 to sequester Daxx in the nucleus, thus preventing cell death.
Data indicate that the structurally most flexible regions during molecular dynamics (MD) simulations of the native mitogen-activated protein kinase-activated protein kinase MK5 model were the loop regions.
Studies with specific phosphoantibodies indicate that MK5 phosphorylates Hsp40/DnaJB1 in vivo at Ser-149 or/and Ser-151 and Ser-171 in the C-terminal domain of Hsp40/DnaJB1.
study shows Tip60 plays an essential role in oncogenic ras-induced senescence; revealed a cascade of posttranslational modifications involving p38, Tip60 and PRAK, 3 proteins essential for ras-induced senescence; these modifications are critical for prosenescent function of Tip60 and PRAK
these results firstly demonstrate that MK5 is degraded in response to doxorubicin and negatively regulates doxorubicin-induced apoptosis, providing novel insights into the molecular mechanism of doxorubicin resistance in hepatoma cells.
IGF2BP1 promotes the velocity and directionality of tumor-derived cell migration by determining the cytoplasmic fate of two novel target mRNAs: MAPK4 and PTEN
Activation loop phosphorylation of ERK3/ERK4 by group I p21-activated kinases (PAKs) defines a novel PAK-ERK3/4-MAPK-activated protein kinase 5 signaling pathway.
This review discusses the different characteristics of regulating the activity and subcellular localization of MK5 and RSK1 by PKA and the functional implications of these interactions.
results imply that MK5 is involved in Hsp27-controlled F-actin dynamics in response to activation of the cAMP-dependent protein kinase pathway.
Data defined a novel MK5 interaction motif (FRIEDE) within both ERK4 and ERK3 that is essential for binding to the C-terminal region of MK5.
The protein encoded by this gene is a tumor suppressor and member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. The encoded protein is found in the nucleus but translocates to the cytoplasm upon phosphorylation and activation. This kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites. Two alternately spliced transcript variants of this gene encoding distinct isoforms have been reported.
mitogen-activated protein kinase-activated protein kinase 5
, MAP kinase-activated protein kinase 5
, MAP kinase-activated protein kinase 5-like
, MAPK-activated protein kinase 5
, MAPKAP kinase 5
, p38-regulated/activated protein kinase