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The protein encoded by PPM1B is a member of the PP2C family of Ser/Thr protein phosphatases. Zusätzlich bieten wir Ihnen Protein Phosphatase, Mg2+/Mn2+ Dependent, 1B Antikörper (92) und Protein Phosphatase, Mg2+/Mn2+ Dependent, 1B Kits (4) und viele weitere Produktgruppen zu diesem Protein an.
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Results indicate that protein phosphatase 1B (PPM1B) negatively regulates cancer cell motility and invasiveness through dephosphorylating Rho guanine nucleotide dissociation inhibitor 1 (RhoGDI1).
PPM1B plays a negative role in the activation of the p38-RB1-E2F1 pathway and that targeting PPM1B could be useful in certain types of cancer by stimulating chemotherapy-induced cell death.
This study has identified PPM1B and miR-186 as potential diagnostic markers in bladder cancer. Promotion of PPM1B and suppression of miR-186 may offer effective therapeutic strategies in the treatment of bladder cancer.
PPM1B interacts with Groucho 4 and is localized to DNA in a Groucho-dependent manner, and phosphatase activity is required for transcriptional silencing.
Results identify PPM1B as a critical regulator of both p38 MAPK-dependent and independent senescence pathways during normal cellular aging process.
Cadmium reversed PPM1A-induced cell cycle arrest and cadmium insensitive PPM1A mutant rescued cadmium induced cell death.
Protein kinase A activates NF-kappaB-mediated transcription by destabilization of PP2Cbeta.
the phosphatase PPM1B as a novel selective modulator of PPARgamma activity.
PPM1B functions as a TBK1 phosphatase dephosphorylates TBK1 at serine 172 and terminates TBK1-mediated IRF3 activation and IFNbeta gene expression.
Studies show that Ppm1b plays a multilayered role in regulating the availability and optimal activity of the EKLF protein in erythroid cells.
results implicate a novel and important role for PP2Cbetal in regulating hPXR activity and CYP3A4 expression by inhibiting or desensitizing signaling pathways that negatively regulate the function of pregnane X receptor in liver cells
PP2Cbeta down-regulates cytokine-induced NF-kappaB activation by altering IKK activity.
Overexpression of PPM1A and the related PPM1B greatly reduced Cdk9 T-loop phosphorylation
Protein phosphatase 1B is mediated dephosphorylation and inactivation of I-kappa B kinase as well as the termination of the Tumor Necrosis Factor-alpha-induced NF-kappaappaB activation.
Ppm1b negatively regulates necroptosis through dephosphorylating Rip3 in vitro and in vivo.
Although a non-myristoylated mutation (G2A) of PPM1A and PPM1B prevented membrane association, this relocalization did not likely cause the decreased activity towards AMPKalpha.
These observations suggest that relatively high PP2Cbeta expression is specifically required during the early stages of pre-implantation development.
The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase has been shown to dephosphorylate cyclin-dependent kinases (CDKs), and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to cause cell-growth arrest or cell death. Alternative splicing results in multiple transcript variants encoding different isoforms. Additional transcript variants have been described, but currently do not represent full-length sequences.
, protein phosphatase 1B
, protein phosphatase 1B (formerly 2C), magnesium-dependent, beta isoform
, protein phosphatase 2C isoform beta
, protein phosphatase 2C-like protein
, Protein phosphatase type 1B (formely 2C) Mg-dependent beta isoform
, Protein phosphatase type 1B (formely 2C), Mg-dependent, beta isoform
, protein phosphatase 1B, magnesium dependent, beta isoform
, protein phosphatase type 2C beta