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anti-Mouse (Murine) MAPKAP Kinase 2 Antibodies:
anti-Human MAPKAP Kinase 2 Antibodies:
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Human Monoclonal MAPKAP Kinase 2 Primary Antibody for ICS - ABIN1177087
Ben-Levy, Leighton, Doza, Attwood, Morrice, Marshall, Cohen: Identification of novel phosphorylation sites required for activation of MAPKAP kinase-2. in The EMBO journal 1996
Show all 8 Pubmed References
Human Monoclonal MAPKAP Kinase 2 Primary Antibody for ICS - ABIN1177089
Clifton, Young, Cohen: A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress. in FEBS letters 1996
Show all 8 Pubmed References
Human Monoclonal MAPKAP Kinase 2 Primary Antibody for ICS - ABIN1177088
Engel, Kotlyarov, Gaestel: Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation. in The EMBO journal 1998
Show all 7 Pubmed References
Chicken Polyclonal MAPKAP Kinase 2 Primary Antibody for ELISA, WB - ABIN538401
Kotlyarov, Neininger, Schubert, Eckert, Birchmeier, Volk, Gaestel: MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis. in Nature cell biology 1999
Show all 3 Pubmed References
Cow (Bovine) Polyclonal MAPKAP Kinase 2 Primary Antibody for IF (p), IHC (p) - ABIN681523
Rosenzweig, Djap, Ou, Quinn: Mechanical injury of bovine cartilage explants induces depth-dependent, transient changes in MAP kinase activity associated with apoptosis. in Osteoarthritis and cartilage / OARS, Osteoarthritis Research Society 2012
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Human Polyclonal MAPKAP Kinase 2 Primary Antibody for DB, IHC (p) - ABIN389585
Xu, Zhou, Xiong, Zou, Deng, Ganaie, Kleiboeker, Peng, Liu, Wang, Ye, Qiu: Parvovirus B19 NS1 protein induces cell cycle arrest at G2-phase by activating the ATR-CDC25C-CDK1 pathway. in PLoS pathogens 2017
Human Polyclonal MAPKAP Kinase 2 Primary Antibody for IHC, WB - ABIN6713457
Hu, Zhang, Gao, Gao, Xu, Lv, Zhang, Zhu, Zhang, Li, Wong, Cui, Zhang, Ma, Wang: Roles of Kruppel-associated Box (KRAB)-associated Co-repressor KAP1 Ser-473 Phosphorylation in DNA Damage Response. in The Journal of biological chemistry 2012
Human Polyclonal MAPKAP Kinase 2 Primary Antibody for IHC, WB - ABIN6712277
Zhang, Tan, Wang, Chen, Quan, Xian, Zhang, He, Zhang: Musashi2 modulates K562 leukemic cell proliferation and apoptosis involving the MAPK pathway. in Experimental cell research 2013
a p38 MAPKAPK2 kinase cascade modulates the activity of F-actin at the yolk cell margin circumference allowing the gradual closure of the blastopore as epiboly progresses
results suggested that MK2 boosts LPS-induced macrophage activation and ALI via increasing activation of CREB and consequently, the expression of Lin28 and downregulation of let-7e.
MK2 deletion in CD11c(+) cells led to an expansion of stimulatory CD103(+) DCs, mounting a potent CD8(+) T cell response that resulted in elimination of highly aggressive B16-F10 tumours upon toll-like receptor (TLR) activation in the presence of tumour antigen.
A novel role of Hsp70 in regulating myoblast differentiation by interacting with MK2 to stabilize p38MAPK.
The importance of MK2 in driving proinflammatory cytokine production, its relevance to in vivo tumor proliferation and invasion.
MK2 promotes polarization of tumor-associated macrophages into protumorigenic, proangiogenic M2-like macrophages.
Phosphorylation of inhibitory PAS domain protein (IPAS) at Ser184 by MAPK-activated protein kinase 2 (MK2 or MAPKAPK2) enhances the proapoptotic function of IPAS.
MK2-mediated RIPK1 phosphorylation is an important molecular mechanism limiting the sensitivity of the cells to the cytotoxic effects of TNF.
p38MAPK/MK2 phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.
MK2-mediated phosphorylation of RIPK1 serves as a checkpoint within the TNF signaling pathway that integrates cell survival and cytokine production.
this study shows that the loss of MK2 in mast cells decreases the IL-33-induced leukocyte recruitment and the resulting skin inflammation
MK2 signaling differentially regulated CCL3 and CCL4.
In silico analyses and experimental validation demonstrated that the kinase activity of p38(MAPK) determines signal amplitude, whereas phosphatase activity affects both signal amplitude and duration. p38(MAPK) and MK2 concentrations and responsiveness toward IL-1beta were quantitatively compared between hepatocytes and macrophages
MK2-activating peptide (MK2-AP) blocks the effects of anthrax lethal toxin on endothelial barriers in cultured cells and reduces pulmonary vascular leak in rats.
MK2 regulates postnatal arteriogenesis by controlling vascular recruitment of monocytes/macrophages in dual manner: regulation of endothelial MCP-1 expression in response to hemodynamic and inflammatory forces as well as MCP-1 dependent monocyte migration
these data suggest there is a sexual dimorphism in MK2 signaling of osteoclast progenitor cell subpopulations.
Loss of MK2 effectively blocks bone resorption and prevents the development of postmenopausal bone loss.
This study showed that cmpd28, a Mapkapk2/3 inhibitor, represents a potentially new approach to type 2 diabetes therapy.
Deficiency of MK2 prevents adverse remodelling and promotes endothelial healing of the arterial wall after injury.
high-fat diet-fed MK2-/- mice display decreased glucose tolerance and increased insulin resistance compared to controls. Decreased adipose tissue expression of GLUT4 might contribute to this phenotype.
Show a low dose of tumor necrosis factor (TNF) causes hyperacute mortality via an oxidative stress driven mechanism in MK2-deficient mice. In addition, MK2-deficient mice were found to be more sensitive to cecal ligation and puncture-induced sepsis.
In this review, we have highlighted in detail the importance of MK2(MAPKAPK2) as the master regulator of RBPs and its role in the regulation of transcript stability, tumor progression, as well as the possibility of use of MK2 as a therapeutic target in tumor management
These results reveal a novel mechanism by which miR-296-3p negatively regulated by nicotine directly targets MK2-induced Ras/Braf/Erk/Mek/c-Myc or PI3K/AKT/c-Myc signaling to stimulate its own expression and suppress NPC cell proliferation and metastasis.
Platelets drive a p38-MK2-RTN4-Bcl-xl pathway associated with the regulation of the endoplasmic reticulum and platelet phosphatidylserine exposure, modulating procoagulant phenotype.
Study found an elevated expression level of MK2 in serum specimens of patients with spinal cord injury. MiR-137 targets MK2 and inhibits its mediated inflammatory response and apoptosis after spinal cord injury.
The novel MK2 substrates have emerged in the DNA damage response, autophagy, and obesity, making MK2 a multifunctional kinase at the crossroads of stress response and cell death.
According to the information mentioned above, we now report the design and synthesis of some series of new urea derivatives that were then evaluated for their inhibitory activities against MAPKAPK2, TNF-a, and p38a
MK2 post-transcriptionally regulates TNF-alpha-induced ICAM-1 expression by altering the cytoplasmic localization of HuR in human lung microvascular endothelial cells.
MK2 overexpression is associated with primary liver tumors.
CEP131 is the key regulatory target of MK2 and 14-3-3 in centriolar satellite remodeling.
mTOR controls the senescence-associated secretory phenotype by differentially regulating the translation of the MK2 (also known as MAPKAPK2).
analysis of signaling cooperation between p38-MAPK/MAPKAP-2/Hsp27 and intracellular calcium release in AA-induced HBEC apoptosis
findings reveal MK2/MK3 as crucial stress-responsive kinases that promote autophagy through Beclin 1 S90 phosphorylation
Low pMK2 expression was found to correlate significantly with overall survival after induction plus chemoradiation therapy in head and neck squamous cell carcinoma patients.
The protein expression of both HMGB1 and MAPKAPK2 were increased in KLM1-R cells.
Data indicate the binding mode and molecular mechanism of action of MAPK-activated protein kinase-2 (MK2) and inhibitors.
Treatment with MK2 or p38 inhibitors blocked human papillomavirus genome amplification, identifying the p38/MK2 pathway as a key regulator of the human papillomavirus life cycle.
a key role of MK2 and FasR in the regulation and limitation of the immune response in the CNS
IscU is a new substrate of MK2 both in Drosophila cells and in human cells
MK2 mediates gemcitabine efficacy in pancreatic cancer cells that respond to the drug, suggesting that the p38/MK2 pathway represents a determinant of the efficacy by that gemcitabine counteracts pancreatic cancer.
MK2 plays a critical role in the development of apoptosis.
This gene encodes a member of the Ser/Thr protein kinase family. This kinase is regulated through direct phosphorylation by p38 MAP kinase. In conjunction with p38 MAP kinase, this kinase is known to be involved in many cellular processes including stress and inflammatory responses, nuclear export, gene expression regulation and cell proliferation. Heat shock protein HSP27 was shown to be one of the substrates of this kinase in vivo. Two transcript variants encoding two different isoforms have been found for this gene.
MAP kinase-activated protein kinase 2
, betty boop
, mitogen-activated protein kinase-activated protein kinase 2
, MAPK-activated protein kinase 2
, MAPKAP kinase 2
, map kinase activated protein kinase-2