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anti-Human MKNK2 Antibodies:
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Human Polyclonal MKNK2 Primary Antibody for ELISA - ABIN543672
Scheper, Morrice, Kleijn, Proud: The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells. in Molecular and cellular biology 2001
Show all 3 Pubmed References
We conclude that MNK2 overexpression in NSCLC is associated with proliferation, migration, invasion, and lower survival rates in patients via the phosphorylated eIF4E-mediated signaling pathway.
Data show that galeterone (gal) and VNPT55 inhibit migration and invasion of prostate cancer cells, possibly by down-regulating protein expression via antagonizing the Mnk1/2-eIF4E axis.
Data suggest MNK1/MNK2 stimulate mRNA translation but only of mRNA containing both 5-prime-terminal cap and hairpin duplex; this stimulation involves up-regulation of phosphorylation/mRNA un-winding activity of eIF4E (via decreased binding to eIF4G).
MNK1 and MNK2 inhibition ablates eIF4E1 phosphorylation and concurrently enhances eIF4E3 expression in diffuse large B-cell lymphoma.
Data show that interferon-gamma regulated the metabolism and mRNA translation of macrophages by targeting the kinases mTORC1 and MNK1/2, both of which converge on the selective regulator of translation initiation eukaryotic initiation factor-4E (eIF4E).
Provide evidence for the existence of a Mnk2/eIF4E-controlled feedback loop in medulloblastoma cells that accounts for resistance to mTORC1 inhibitors.
Data suggest that a combined pharmacologic inhibition of mTORC1 and Mnk1/2 kinases offers a therapeutic opportunity in blast crisis-chronic myeloid leukemia (BC-CML).
These findings provide evidence for key and essential roles of the Mnk kinase pathway in the generation of the antineoplastic effects of type I IFNs in Jak2V617F-dependent myeloproliferative neoplasms.
eIF4E phosphorylation is enhanced by Rapamycin, which activates Mnk2a
MNK2-dependent phosphorylation of eIF4E represents a novel drug resistance, pro-survival pathway in pancreatic ductal carcinoma.
siRNA-mediated Mnk1/2 knockdown results in partial reversal of the suppressive effects of IFNgamma on human CD34+-derived myeloid (CFU-GM) and erythroid (BFU-E) progenitors.
The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization
Mnk2 can interact with CBC(VHL) complex, and is probably one of the new substrates of the CBC(VHL) complex.
MNK2 plays a role in adipogenesis and/or lipogenesis and in macrophage biology
Data suggest that Mnk1 and Mnk2 regulate cell migration/wound healing, expression of vimentin, stability of vimentin protein, and binding of eIF4E (eukaryotic translation initiation factor 4E) and Cyfip1 (cytoplasmic FMR1 interacting protein 1).
Mnk2a directly interacts with and translocates p38alpha-MAPK into the nucleus. Alternatively, Mnk2b does not activate p38-MAPK.
Mnk1/2 has a minimal role in T cell development and activation but may regulate non-T cell lineages to control Th1 and Th17 differentiation in vivo.
Data indicate that MNK2 plays a unique role, not shared by its closest paralog MNK1, in limiting protein translation through its negative effect on eIF4G Ser1108 phosphorylation and p70S6K activation.
MAP kinase-interacting kinase 1 and 2 activity enhances formation of the EIF-4F complex in pachytene spermatocytes but not in round spermatids.
oncogenic role for Mnk1/2 in tumor development
Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development
The roles of features in the catalytic domains and C termini in determining the regulatory properties and basal activities of Mnk1 AND Mnk2 are reported.
Roles of mitogen-activated protein kinase signal-integrating kinases 1 and 2 in oxidant-mediated eIF4E phosphorylation.
MNK1 and MNK2 are kinases involved in anti-apoptotic signaling in response to serum withdrawal
This gene encodes a member of the calcium/calmodulin-dependent protein kinases (CAMK) Ser/Thr protein kinase family, which belongs to the protein kinase superfamily. This protein contains conserved DLG (asp-leu-gly) and ENIL (glu-asn-ile-leu) motifs, and an N-terminal polybasic region which binds importin A and the translation factor scaffold protein eukaryotic initiation factor 4G (eIF4G). This protein is one of the downstream kinases activated by mitogen-activated protein (MAP) kinases. It phosphorylates the eukaryotic initiation factor 4E (eIF4E), thus playing important roles in the initiation of mRNA translation, oncogenic transformation and malignant cell proliferation. In addition to eIF4E, this protein also interacts with von Hippel-Lindau tumor suppressor (VHL), ring-box 1 (Rbx1) and Cullin2 (Cul2), which are all components of the CBC(VHL) ubiquitin ligase E3 complex. Multiple alternatively spliced transcript variants have been found, but the full-length nature and biological activity of only two variants are determined. These two variants encode distinct isoforms which differ in activity and regulation, and in subcellular localization.
G protein-coupled receptor kinase 7
, MAP kinase signal-integrating kinase 2
, MAP kinase-interacting serine/threonine-protein kinase 2
, MAPK signal-integrating kinase 2
, MAP kinase interacting serine/threonine kinase 2
, MAP kinase-interacting serine/threonine kinase 2
, MAP kinase interacting serine/threonine kinase 2a