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The protein encoded by PPM1B is a member of the PP2C family of Ser/Thr protein phosphatases. Additionally we are shipping Protein Phosphatase, Mg2+/Mn2+ Dependent, 1B Antibodies (103) and Protein Phosphatase, Mg2+/Mn2+ Dependent, 1B Kits (4) and many more products for this protein.
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This study has identified PPM1B and miR (show MLXIP Proteins)-186 as potential diagnostic markers in bladder cancer. Promotion of PPM1B and suppression of miR (show MLXIP Proteins)-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 (show MAPK14 Proteins)-dependent and independent senescence pathways during normal cellular aging process.
Cadmium reversed PPM1A (show PPM1A Proteins)-induced cell cycle arrest and cadmium insensitive PPM1A (show PPM1A Proteins) mutant rescued cadmium induced cell death.
Protein kinase A activates NF-kappaB (show NFKB1 Proteins)-mediated transcription by destabilization of PP2Cbeta.
the phosphatase PPM1B as a novel selective modulator of PPARgamma (show PPARG Proteins) activity.
PPM1B functions as a TBK1 (show TBK1 Proteins) phosphatase dephosphorylates TBK1 (show TBK1 Proteins) at serine 172 and terminates TBK1 (show TBK1 Proteins)-mediated IRF3 (show IRF3 Proteins) activation and IFNbeta gene expression.
Studies show that Ppm1b plays a multilayered role in regulating the availability and optimal activity of the EKLF (show KLF1 Proteins) protein in erythroid cells.
results implicate a novel and important role for PP2Cbetal in regulating hPXR activity and CYP3A4 (show CYP3A4 Proteins) expression by inhibiting or desensitizing signaling pathways that negatively regulate the function of pregnane X receptor (show NR1I2 Proteins) in liver cells
PP2Cbeta down-regulates cytokine-induced NF-kappaB (show NFKB1 Proteins) activation by altering IKK (show CHUK Proteins) activity.
Ppm1b negatively regulates necroptosis through dephosphorylating Rip3 in vitro and in vivo.
Although a non-myristoylated mutation (G2A (show GPR132 Proteins)) of PPM1A (show PPM1A Proteins) and PPM1B prevented membrane association, this relocalization did not likely cause the decreased activity towards AMPKalpha (show GRK4 Proteins).
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