Recombinant human PPP1A/PPP1CA protein is a Human Full Length protein, in the 1 to 330 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE, MS, FuncS.
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Key facts
- Purity
- >80% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE, MS, FuncS
- Biologically active
- Yes
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Target data
Function
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 (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). Together with PPP1CC (PP1-gamma subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response (PubMed:23499489). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:36175670). (Microbial infection) Necessary for alphaviruses replication.
Alternative names
PPP1A, PPP1CA, Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, PP-1A
Recommended products
Recombinant human PPP1A/PPP1CA protein is a Human Full Length protein, in the 1 to 330 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE, MS, FuncS.
Key facts
- Purity
- >80% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE, MS, FuncS
- Biologically active
- Yes
- Biological activity
- >3,000 units/mg. Enzymatic activity was confirmed by measuring the amount of enzyme hydrolyzing 1 nmole of p-nitrophenyl phosphate (pNPP) per minute at 37 °C, pH 7.5, using 10 mM of substrate.
- Accession
- P62136-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8.5
Constituents: 50% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.79% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.01% Manganese chloride, 0.002% PMSF
Sequence info
Amino acid sequence
- Accession
- P62136
- Protein length
- Full Length
- Predicted molecular weight
- 39.7 kDa
- Amino acids
- 1 to 330
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Liquid
- Additional notes
ab113150 was purified using conventional chromatography techniques.
General info
- Function
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 (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). Together with PPP1CC (PP1-gamma subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response (PubMed:23499489). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:35768504, PubMed:35830882, PubMed:35831509, PubMed:36175670). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:36175670).
- Sequence similarities
Belongs to the PPP phosphatase family. PP-1 subfamily.
- Post-translational modifications
Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation.
- Subcellular localisation
- Nucleus, Nucleoplasm, Nucleolus
Storage
- Shipped at conditions
- Blue Ice
- Appropriate short-term storage duration
- 1-2 weeks
- Appropriate short-term storage conditions
- +4°C
- Appropriate long-term storage conditions
- -20°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Notes
This product was previously labelled as PPP1A
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Protein phosphatase 1 alpha also known as PPP1A or PPP1CA is a catalytic subunit of protein phosphatase 1 with a molecular weight of approximately 37 kDa. PPP1A plays a role in the dephosphorylation of serine/threonine residues in various proteins. It is expressed widely in human tissues with significant presence in the brain heart and skeletal muscle. PPP1A is essential for many cellular processes due to its widespread distribution and ability to interact with different substrate proteins.
- Biological function summary
Protein phosphatase 1 alpha controls key aspects of cellular function. It often exists as part of complexes with other regulatory proteins which modulate its specificity and activity. These complexes participate in cell cycle regulation muscle contraction protein synthesis and glycogen metabolism. PPP1A's role in forming reversible phosphorylation networks highlights its importance in maintaining cellular homeostasis and responding to various signals.
- Pathways
The role of PPP1A is vital in pathways such as the cell cycle and glycogen metabolism. It interacts with proteins like cyclin-dependent kinases to manage the cell division process and collaborates with glycogen synthase to regulate glycogen synthesis and breakdown. The involvement of PPP1A in these pathways showcases its versatility in influencing cellular metabolism and division processes.
- Associated diseases and disorders
Protein phosphatase 1 alpha is linked to cardiac diseases and cancer. Its dysregulation can influence heart muscle contractility contributing to cardiac hypertrophy and heart failure. Additionally abnormal PPP1A activity can impact tumorigenesis through interactions with cancer-related proteins like Akt. Understanding PPP1A's role in these diseases provides insights into potential therapeutic targets for treatment.
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1 product image
SDS-PAGE - Recombinant human PPP1A/PPP1CA protein (ab113150)
SDS-PAGE showing ab113150 (3 μg) under reducing conditions with coomassie blue protein stain
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