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anti-Human PPP1R3C Antibodies:
anti-Mouse (Murine) PPP1R3C Antibodies:
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PPP1R3C, a novel hypermethylated gene in colorectal cancer, may play a critical role in cancer cell growth in association with glucose levels.
detection of methylation of PPP1R3C alone or in combination with EFHD1 in plasma DNA showed high sensitivity and specificity in CRC detection, and may be useful detection method for CRC, especially for early-stage CRCs.
Findings suggest that variations in PTG may condition the course of Lafora disease and establish PTG as a potential target for pharmacogenetic and therapeutic approaches.
Results demonstrated that HIF1 promotes glycogen accumulation through regulating PPP1R3C expression under hypoxia, which revealed a novel metabolic adaptation of cells to hypoxia.
phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity.
metabolic crosstalk is due to decreased mTORC1 and SREBP activity in PTG knockout mice or knockdown cells, suggesting a positive feedback loop in which once accumulated, glycogen stimulates the mTORC1/SREBP1 pathway to shift energy storage to lipogenesis.
removing PTG, a glycogen synthesis activator protein, nearly completely eliminates Lafora bodies and rescues the neurodegeneration, myoclonus,seizure susceptibility, and behavioral abnormality.
Laforin-deficient mice lacking PTG have greatly decreased Lafora bodies and normal glycogen levels.
These data suggest that PTG plays a critical role in glycogen synthesis and is necessary to maintain the appropriate metabolic balance for the partitioning of fuel substrates between glycogen and lipid.
PTG overexpression in 3T3-L1 adipocytes discretely stimulates PP1 activity against glycogen synthase and phosphorylase, resulting in a marked and specific increase in glucose uptake and storage as glycogen.
These data indicate that disruption of PTG expression resulted in the uncoupling of PP1 activity from glycogen metabolizing enzymes, the enhancement of glycogenolysis, and a dramatic decrease in cellular glycogen levels.
mouse protein targeting to glycogen (PTG) promoter is regulated by the FoxA2 forkhead protein and by 3',5'-cyclic adenosine 5'-monophosphate in H4IIE hepatoma cells
This gene encodes a regulatory subunit of protein phosphatase-1 (PP1). PP1 catalyzes reversible protein phosphorylation, which is important in a wide range of cellular activities: neuronal, muscular, RNA splicing, protein synthesis, cell death, and glycogen metabolism, to name just a few. By interacting with different regulatory subunits, PP1 is directed to different parts of the cell, to different substrates, or to respond to extracellular signals.
PP1 subunit R5
, Phosphatase 1, regulatory inhibitor subunit 5
, protein phosphatase 1 regulatory subunit 3C
, protein phosphatase 1 regulatory subunit 5
, protein phosphatase 1, regulatory (inhibitor) subunit 3C
, protein targeting to glycogen
, protein phosphatase 1 binding protein PTG
, protein phosphatase 1, regulatory (inhibitor) subunit 5
, protein targeting to glicogen
, protein phosphatase 1 regulatory subunit 3C-B