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Human ERK2 Protein expressed in Baculovirus infected Insect Cells - ABIN2001936
Slack, Seternes, Gabrielsen, Keyse: Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1. in The Journal of biological chemistry 2001
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Human ERK2 Protein expressed in Wheat germ - ABIN1310256
Abeydeera, Egli, Cox, Mercier, Conde, Pallan, Mizurini, Sierant, Hibti, Hassell, Wang, Liu, Liu, Martinez, Sood, Lybrand, Frydman, Monteiro, Gomer, Nawrot, Yang: Evoking picomolar binding in RNA by a single phosphorodithioate linkage. in Nucleic acids research 2016
Down-regulation of PRDX1 in colorectal cancer SW480 cells could inhibit the cell proliferation, migration, invasion, and induce cell apoptosis.
The anti-apoptotic extracellular signal-regulated kinase 1/2 (ERK1/2) also contributed to infectious bronchitis virus-induced autophagy.
RNF25 plays an essential role in gefitinib resistance of Non-small cell lung cancer by mediating cross-talk between NF-kappaB and ERK pathways.
We have identified mutations in ERK1/2, amplification and overexpression of ERK2, and overexpression of EGFR/ERBB2 as mechanisms of acquired resistance. Structural analysis of ERK showed that specific compounds that induced on-target ERK mutations were impaired in their ability to bind mutant ERK.
ERK/NF- kappa B signaling pathway has a role in the inhibition of tumor growth by amentoflavone in glioblastoma.
multiple GPCR agonists utilize non-canonical TAB1-TAB2 and TAB1-TAB3-dependent p38 activation to promote endothelial inflammatory responses.
Silencing of TAB1, but not TAK1, prevented p38MAPK activation, which is indicative of TAB1-mediated autophosphorylation of p38MAPK
miR-22 is found to suppress cell proliferation/apoptosis by directly targeting MAPK1 (mitogen-activated protein kinase 1, ERK2) and inhibit cell motility by targeting both MAPK1 and Snail.
CSNK2A1 plays a role in the nuclear translocation of ERK1/2. Ser246 phosphorylation by CK2 is sufficient for full ERK translocation, while Ser244 phosphorylation accelerates it.
mismatch repair-deficient (dMMR)-competent stage III tumours harbouring BRAF mutations have an improved prognosis when strong nuclear phosphorylation of both ERK and p38MAPK is present.
The computer prediction was confirmed with pulldown and in vitro kinase assays, in which IBC directly bound with ERK1/2 and RSK2, and dosedependently blocked RSK2 kinase activity in liver cancer cells
Shear stress loading for 6h promotes liver cancer stem cells (LCSCs) migration and activation of the focal adhesion kinase (FAK) and extracellular signal regulated kinase1/2 (ERK1/2) signalling pathways.
both HSP60 knockdown and oxidative phosphorylation (OXPHOS) inhibition by metformin decreased Erk1/2 phosphorylation and induced apoptosis and cell cycle arrest.
Ebastine-mediated human follicle dermal papilla cells(HFDPC) growth was completely reversed by blocking ERK kinase. The results from our present study suggest that the regulation of HFDPC proliferation by ebastine might be directly involved in hair regrowth through the ERK signaling pathway.
GPS2 enhances BK channel activity and its protein expression by reducing ERK1/2 signaling-mediated degradation of the channel.
It is a serine/threonine-specific protein kinase that transduces intracellular signals in critical cellular phenomena.
our results indicate that TLR4-dependent upregulation of glycolysis in human MoDCs involves a p38-MAPK-dependent HIF-1alpha accumulation, leading to an increased HK activity supported by enhanced HK2 expression.
High MAPK1 expression is associated with drug resistance in ovarian cancer.
reveals a new role of mitochondrial Stat3 in preventing ASK1/p38(MAPK)-mediated apoptosis.
High ERK2 expression is associated with glioma cell growth and invasiveness.
These data show that connexin43-dependent gap junctional communication among osteoblast cells permits efficient ERK1/2 activation. ERK1/2 signaling promotes the recruitment of the potent transcriptional activator, Sp1, to the osteoprotegerin proximal promoter, resulting in robust transcription of anti-osteoclastogenic factor, osteoprotegerin.
Overexpression of Gm2199 restored the reduced proliferation of damaged hepatocyte lines and increased the expression of ERK1/2.
cisplatin activates TAK1, which phosphorylates p38 and ERK, leading to excessive autophagy of tubular epithelial cells that exacerbates kidney damage.
these resultssuggested that kavain inhibits osteoclast formation and function bymodulating intracellular calcium-mediated NFATc1 and MAPK deactivation, while not affecting osteoblasts
spinophilin fulfills an essential role in cocaine-induced behavioral sensitization, likely via ERK1/2 phosphorylation and induction of c-Fos and FosB in the striatum.
Combined treatment of PA and LPS in RAW264.7 cells mimics the situation of diabetes with obesity that has higher level of PA and LPS, MAPK/TLR4/ MCP-1 might be potential therapeutic targets for diabetes with obesity.
DUSP5 functions in the feedback inhibition of ERK1/2 signaling in response to TNFalpha, which resulted in increased inflammatory gene expression.
Data suggest diabetes is accompanied by increases in arterial miR-221 and -222 expression that promotes intimal thickening via extracellular signal-regulated kinases 1/2 signaling.
IL-17A aggravates inflammatory response during Acute myocardial infarction by inducing macrophages infiltration and activating NLRP3 inflammasome through AMPKalpha/p38MAPK/ERK1/2 pathway.
Mutation of the ERK phosphorylation site in KLF4 (S132) blocks KLF4 nuclear export, the decline in Nanog, Klf4, and Sox2 mRNA, and differentiation.
temporal regulation of AMPK is required for proper control of S phase in NIH3T3 cells
SIRT6 attenuates cisplatin-induced acute kidney injury by binding to the promoters of ERK1 and ERK2 and deacetylated histone 3 at Lys9 (H3K9) thereby inhibiting ERK1/2 expression.
results demonstrate the mechanism for the maintenance of the undifferentiated state of embryonic stem cells via the inhibition of the FGF4-PKCzeta-MEK-ERK1/2 pathway by O-GlcNAcylation on PKCzeta.
Selective inhibition or knockdown of Rac1 decreased IL-6 and IL-8 release in 16HBE cells induced by cigarette smoke extract (CSE), which correlated with CSE-induced Rac1-regulated Erk1/2 mitogen-activated protein kinase (MAPK) and signal transducer and activator of transcription-3 (STAT3) signaling.
M-CSF-evoked ERK1/2 activation was decreased, whereas AKT activation was enhanced in SHP2-deficient BMMs. ERK1/2, via its downstream target RSK2, mediates this negative feedback by negatively regulating phosphorylation of M-CSF receptor at Tyr721 and, consequently, its binding to p85 subunit of PI3K and PI3K activation.
ERK5 provides a common bypass route in intestinal epithelial cells, which rescues cell proliferation upon abrogation of ERK1/2 signalling, with therapeutic implications in colorectal cancer.
MAPKs play a critical role in the control of cellular responses to cytokines and stressors and involved in the LPS-induced signaling pathway by which iNOS is expressed.
The Macrophage Activation Induced by Bacillus thuringiensis Cry1Ac Protoxin Involves ERK1/2 and p38 Pathways and the Interaction with Cell-Surface-HSP70
persistent distention/stretch on colonic smooth muscle cells could suppress SCF production probably through Ca(2+) -ERK-AP-1-miR-34c deregulation.
This indicates that TcpC may promote MIP2 production in kidney cells through the p38 MAPK signaling pathway. Taken together, the data of the present study demonstrated that TcpC can induce MIP2 production, which may contribute to the characteristic histological change associated with pyelonephritis.
both granulosa and theca cells of ERK1/2-inhibited follicles had higher expression of SLC16A1, a monocarboxylate transporter, transporting substances including beta-hydroxybutyrate across the plasma membrane. Taken together, ERK1/2 plays a significant role in mediating LH surge-induced gene expression in granulosa and theca cells of the ovulating follicle in cattle.
The present results suggest that demecolcine might contribute to the activation of the Mos/MAPK pathway and affect spindle structure
MAPK1 upregulated milk protein synthesis through the Stat5 and mTOR pathways.
Chronic hypoxia induces Egr-1 via activation of ERK1/2 and contributes to pulmonary vascular remodeling.
ER Ca(2+) release enhances eNOS Ser-635 phosphorylation and function via ERK1/2 activation.
Cyclin-dependent kinase inhibition did not affect the expression (mRNA and protein levels) and localization of maturation promoting factor(MPF) and MAPK, and had nearly no effect on kinase activities during maturation.
Thrombospondin 1, fibronectin, and vitronectin are differentially dependent upon RAS, ERK1/2, and p38 for induction of vascular smooth muscle cell chemotaxis.
results suggest that Nav1.7-Ca2+ influx-protein kinase C-alpha pathway activated ERK1/ERK2 and p38, which increased phosphorylation of glycogen synthase kinase-3beta, decreasing tau phosphorylation
These data suggest that Gab1-ERK1/2 binding and their nuclear translocation play a crucial role in Egr-1 nuclear accumulation.
Role of CaMKII in hydrogen peroxide activation of p38 MAPK/heat shock protein 27 pathway and ERK1/2
data demonstrate that hypoxia-induced adventitial fibroblast proliferation requires activation and interaction of PI3K, Akt, mTOR, p70S6K, and ERK1/2.
This study demonstrates for the first time that cyclic mechanical stretch induces the proliferation of bovine satellite cells and suppresses their myogenic differentiation through the activation of ERK.
findings indicate that exposure to DHEA, at concentrations found in human blood, causes vascular endothelial proliferation by a plasma membrane-initiated activity that is Gi/o and ERK1/2 dependent.
These results suggest that bGPR40 mediates LCFA signaling in mammary epithelial cells and thereby plays an important role in cell proliferation and survival.
Results suggest that estrogen receptors and the ERK1/2 signaling pathway are involved in the anti-apoptotic action of LY117018 in vascular endothelial cells.
The intracellular mechanism of action of CART in regulation of FSH-induced MAPK signaling.
IFN-alpha mediated activation of ERK1/2 appeared to be responsible for the increased phosphorylation of tyrosine hydroxylase.
MAPK1 role in the oocyte maturation
Excess PLAC8 promotes an unconventional ERK2-dependent EMT in colon cancer.
ERK1/2-Akt1 crosstalk regulates arteriogenesis in mice and zebrafish.
eena plays an important role in the development of the myeloid cell through activation of the ERK1/ERK2 pathway
ERK1 and ERK2 target common and distinct gene sets, confirming diverse roles for these kinases during embryogenesis; for ERK2 genes involved in cell-migration, mesendoderm differentiation and patterning were identified.
These results demonstrate that induction of Hsp70 in response to heat stress is dependent on ERK activation in Pac2 cells.
Data define distinct roles for ERK1 and ERK2 in developmental cell migration processes during zebrafish embryogenesis.
Here the authors show that CPEB4 activity is regulated by ERK2- and Cdk1-mediated hyperphosphorylation. These phosphorylation events additively activate CPEB4 in M-phase by maintaining it in its monomeric state.
The reciprocal feedback observed between MPF and ERK2 in meiosis is not observed during mitotic M-phase in cell-free Xenopus embryo extracts.
The data suggest a MKK3 * MPK1 * RBK1 phosphorylation cascade that may provide a dynamic module for altering cell expansion.
MKP1 is a negative regulator of signaling pathways required for some, but not all, early and late pathogen-associated molecular pattern responses.
MKP1 and PTP1 act redundantly to suppress salicylic acid and camalexin biosynthesis, and regulate growth homeostasis and PR gene expression in an MPK3- and MPK6-dependent manner.
Regulation of AtMPK1/2 kinase activity in Arabidopsis might be under the control of signals involved in different kinds of stress.
Early activation of MAPK p44/42 is involved in deoxynivalenol -induced disruption of intestinal barrier function and tight junction network signaling.
Agonist stimulation of vascular smooth muscle increases PKC activity, which, in turn, increases MKP-1 activity and maintains MAPK1 activity at submaximal values.
sub-vasomotor concentration of ET-1 leads to vascular dysfunction by impairing endothelium-dependent NO-mediated dilation via p38 kinase-mediated production of superoxide from NADPH oxidase following ETA receptor activation
Treatment with ERK inhibitors or ERK1/2 knockdown significantly suppressed porcine epidemic diarrhea virus progeny production.
This study reveals a new function of the gE glycoprotein of pseudorabies virus and suggests that pseudorabies virus, through activation of ERK1/2 signaling, has a substantial impact on T cell behavior.
CSF2 stimulates proliferation of trophectoderm cells by activation of the PI3K-and ERK1/2 MAPK-dependent MTOR signal transduction cascades.
PGRN inhibits adipogenesis in porcine preadipocytes partially through ERK activation mediated PPARgamma phosphorylation.
Data show that proinflammatory cytokines induction was ERK1/2 and JNK1/2 dependent.
The authors show that porcine circovirus type 2 (PCV2) activates ERK1/2 in PCV2-infected PK15 cells dependent on viral replication.
20-HETE activates the Raf/MEK/ERK pathway in renal epithelial cells through an EGFR- and c-Src-dependent mechanism.
Data show that treatment with GH or IGF-I reduced leptin receptor expression, and increased Phosphorylation of ERK1/2 in response to acute leptin.
Cyclosporine A/sirolimus alter claudin-1 expression in renal proximal tubular cells via ERK1/2 signaling pathway to alter barrier function.
role of ERK1 and 2 in mediating IGF-I-stimulated vascular smooth muscle cell proliferation and chemotaxis [ERK1, ERK2]
endogenous ceramides are important second messengers in IL-1beta-induced apoptosis in pig thyroid cells through inhibition of adenylyl cyclase and ERK1/2 activities
Phorbol 12-myristate 13-acetate activation of ERK and JNK signaling is relevant in the regulation of gene expression during follicular development, ovulation, and luteinization.
There was no correlation of infarct size with expression or phosphorylation of ERK2 in ischemic postconditioning.
Retinal ischemia-reperfusion alters expression of mitogen-activated protein kinases, particularly ERK1/2, in the neuroretina and retinal arteries.
Saccharomyces cerevisiae inhibits the Enterotoxigenic Escherichia coli-induced expression of pro-inflammatory transcripts and this inhibition was associated to a decrease of ERK1/2 and p38 MAPK phosphorylation
ERK2 phosphorylation in response to Insulin-like Growth Factor-1 does not require activation of the Insulin-like Growth Factor-1 receptor tyrosine kinase
The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), 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. The activation of this kinase requires its phosphorylation by upstream kinases. Upon activation, this kinase translocates to the nucleus of the stimulated cells, where it phosphorylates nuclear targets. Two alternatively spliced transcript variants encoding the same protein, but differing in the UTRs, have been reported for this gene.
, MAP kinase 1
, MAP kinase 2
, MAP kinase isoform p42
, MAPK 2
, extracellular signal-regulated kinase 2
, mitogen-activated protein kinase 2
, protein tyrosine kinase ERK2
, MAPK 1
, mitogen activated protein kinase 1
, extracellular-signal-regulated kinase 2
, mitogen-activated protein kinase 1
, MAP kinase
, mitogen-activated protein kinase 1b
, myelin basic protein kinase-like protein
, mitogen-activated protein kinase 1a
, extracellular signal-regulated kinase-2
, extracellular regulated protein 2