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Product Info

ELISA 1:10000, WB 1:500-1:2000
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Monoclonal [AFB1952]
PPP1CA antibody detects endogenous levels of total PPP1CA.
Cite Format: Affinity Biosciences Cat# BF0683, RRID:AB_2833975.
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


Alpha isoform serine threonine protein phosphatase PP1alpha 1 catalytic subunit; Catalytic subunit; EC; MGC15877; MGC1674; PP 1A; PP-1A; PP1A; PP1A_HUMAN; PP1alpha; PP2C ALPHA; PP2CA; Ppp1ca; Protein Phosphatase 2C Alpha Isoform; Serine threonine protein phosphatase PP1 alpha catalytic subunit; Serine threonine protein phosphatase PP1 alpha catalytic subunit protein phosphatase 1; Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;



Purified recombinant fragment of human PPP1CA expressed in E. Coli.

The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Mouse studies also suggest that PP1 functions as a suppressor of learning and memory. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene.

PTMs - P62136 As Substrate

Site PTM Type Enzyme
S2 Acetylation
S2 Phosphorylation
K6 Ubiquitination
S11 Phosphorylation
S22 Phosphorylation
K26 Ubiquitination
R36 Methylation
K41 Ubiquitination
S48 Phosphorylation
K60 Ubiquitination
Y93 Phosphorylation
K98 Ubiquitination
K113 Ubiquitination
R122 Methylation
S129 Phosphorylation
R132 Methylation
Y134 Phosphorylation
Y137 Phosphorylation
K141 Acetylation
K141 Ubiquitination
K147 Acetylation
K147 Ubiquitination
K150 Ubiquitination
S177 Phosphorylation
K238 Acetylation
K238 Ubiquitination
Y255 Phosphorylation
K260 Acetylation
K260 Ubiquitination
K305 Acetylation
K305 Ubiquitination
Y306 Phosphorylation
S310 Phosphorylation
T320 Phosphorylation P24941 (CDK2) , P31749 (AKT1) , Q8IWU2 (LMTK2) , Q00535 (CDK5) , P06493 (CDK1)
S325 Phosphorylation
K329 Methylation

Research Backgrounds


Protein 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 Ca(2+)/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. Dephosphorylates CENPA. Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy.

(Microbial infection) Necessary for alphaviruses replication.


Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation.

Subcellular Location:

Cytoplasm. Nucleus. Nucleus>Nucleoplasm. Nucleus>Nucleolus.
Note: Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. Shuttles toward the cytosol during infection with VEEV (PubMed:29769351).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with PPP1R39 (By similarity). Interacts with BTBD10 (By similarity). Interacts with KCTD20 (By similarity). Interacts with PPP1R9A and PPP1R9B. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with PHACTR4; which acts as an activator of PP1 activity (By similarity). Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1. Interacts with PPP1R7. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with PPP1R16B. Interacts with RPSA only in the presence of PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of PPP1R10/PNUTS. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site. Interacts with isoform 1 and isoform 4 of NEK2. Interacts with FER; this promotes phosphorylation at Thr-320. Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction. Interacts with FOXP3. Interacts with CENPA. Interacts with ATG16L1. Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1.

(Microbial infection) Interacts with HHV-1 ICP34.5.

(Microbial infection) Interacts with Venezuelan equine encephalitis virus (VEEV) capsid protein; this interaction dephosphorylates the capsid protein, which increases its ability to bind to the viral genome.


Belongs to the PPP phosphatase family. PP-1 subfamily.

Research Fields

· Cellular Processes > Cell growth and death > Oocyte meiosis.   (View pathway)

· Cellular Processes > Cell growth and death > Cellular senescence.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Environmental Information Processing > Signal transduction > cGMP-PKG signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > cAMP signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Hippo signaling pathway.   (View pathway)

· Genetic Information Processing > Translation > mRNA surveillance pathway.

· Human Diseases > Endocrine and metabolic diseases > Insulin resistance.

· Human Diseases > Substance dependence > Amphetamine addiction.

· Human Diseases > Substance dependence > Alcoholism.

· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Organismal Systems > Circulatory system > Adrenergic signaling in cardiomyocytes.   (View pathway)

· Organismal Systems > Circulatory system > Vascular smooth muscle contraction.   (View pathway)

· Organismal Systems > Immune system > Platelet activation.   (View pathway)

· Organismal Systems > Nervous system > Long-term potentiation.

· Organismal Systems > Nervous system > Dopaminergic synapse.

· Organismal Systems > Sensory system > Inflammatory mediator regulation of TRP channels.   (View pathway)

· Organismal Systems > Endocrine system > Insulin signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Oxytocin signaling pathway.

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