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The degree of protein phosphorylation is regulated by a balance of protein kinase and phosphatase activities. Additionally we are shipping PPP1R14C Antibodies (20) and PPP1R14C Proteins (4) and many more products for this protein.
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analysis of antibodies generated against the protein phosphatase 1 inhibitor KEPI and characterization of the epitope
PPP1R14C gene encodes a PKC-potentiated inhibitory protein, KEPI, for type-1 Ser/Thr protein phosphatase (PP1 (show PPA1 ELISA Kits)). KEPI mRNA and protein were enriched in brain, heart and skeletal muscle.
the data presented in this manuscript demonstrate a critical function of VPS35 in regulating PTH1R (show PTH1R ELISA Kits) trafficking. This event and VPS35-interaction with PPP1R14C appear to be essential for turning off PTH1R's endosomal signaling, and promoting PTH1R (show PTH1R ELISA Kits)-mediated catabolic response and bone remodeling.
PPP1R14C gene encodes a PKC (show PKC ELISA Kits)-potentiated inhibitory protein, KEPI, for type-1 Ser/Thr protein phosphatase (PP1). KEPI mRNA and protein are enriched in brain, heart and skeletal muscle.
The expression patterns point to possible roles for KEPI in regulating protein dephosphorylation by inhibiting PP1 activities in a number of brain pathways.
The degree of protein phosphorylation is regulated by a balance of protein kinase and phosphatase activities. Protein phosphatase-1 (PP1\; see MIM 176875) is a signal-transducing phosphatase that influences neuronal activity, protein synthesis, metabolism, muscle contraction, and cell division. PPP1R14C is an inhibitor of PP1 (Liu et al., 2002
PKC-potentiated PP1 inhibitory protein
, kinase C-enhanced PP1 inhibitor
, kinase-enhanced PP1 inhibitor
, protein phosphatase 1 regulatory subunit 14C
, serologically defined breast cancer antigen NY-BR-81