The Human (PPP1CA) Serine Threonine-protein Phosphatase PP1-alpha Catalytic Subunit ELISA Kit measures Serine/threonine-protein phosphatase PP1-alpha catalytic subunit in samples. The plate has been pre-coated with Human PPP1CA antibody. PPP1CA present in the sample is added and binds to antibodies coated on the wells. And then biotinylated Human PPP1CA Antibody is added and binds to PPP1CA in the sample. Then Streptavidin-HRP is added and binds to the Biotinylated PPP1CA antibody. After incubation unbound Streptavidin-HRP is washed away during a washing step. Substrate solution is then added and color develops in proportion to the amount of Human PPP1CA. The reaction is terminated by addition of acidic stop solution and absorbance is measured at 450 nm.
Research AreasSignal Transduction, Cancer, Metabolism, Enzyme & Kinase
BackgroundProtein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208).
Dephosphorylates CENPA (PubMed:25556658).
Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (PubMed:26083323).
(Microbial infection) Necessary for alphaviruses replication. Source: UniProt Consortium (2025)
