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The protein encoded by PPM1B is a member of the PP2C family of Ser/Thr protein phosphatases. De plus, nous expédions Protein Phosphatase, Mg2+/Mn2+ Dependent, 1B Anticorps (101) et Protein Phosphatase, Mg2+/Mn2+ Dependent, 1B Protéines (9) et beaucoup plus de produits pour cette protéine.
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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 (Montrer PPP1R1A Kits ELISA) (RhoGDI1 (Montrer ARHGDIA Kits ELISA)).
PPM1B plays a negative role in the activation of the p38 (Montrer CRK Kits ELISA)-RB1 (Montrer RB1 Kits ELISA)-E2F1 (Montrer E2F1 Kits ELISA) 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 (Montrer MAPK14 Kits ELISA)-dependent and independent senescence pathways during normal cellular aging process.
Cadmium reversed PPM1A (Montrer PPM1A Kits ELISA)-induced cell cycle arrest and cadmium insensitive PPM1A (Montrer PPM1A Kits ELISA) mutant rescued cadmium induced cell death.
Protein kinase A activates NF-kappaB (Montrer NFKB1 Kits ELISA)-mediated transcription by destabilization of PP2Cbeta.
the phosphatase PPM1B as a novel selective modulator of PPARgamma (Montrer PPARG Kits ELISA) activity.
PPM1B functions as a TBK1 (Montrer TBK1 Kits ELISA) phosphatase dephosphorylates TBK1 (Montrer TBK1 Kits ELISA) at serine 172 and terminates TBK1 (Montrer TBK1 Kits ELISA)-mediated IRF3 (Montrer IRF3 Kits ELISA) activation and IFNbeta gene expression.
Studies show that Ppm1b plays a multilayered role in regulating the availability and optimal activity of the EKLF (Montrer KLF1 Kits ELISA) protein in erythroid cells.
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