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AB128559

Recombinant human PPP1A/PPP1CA protein

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Recombinant human PPP1A/PPP1CA protein is a Human Full Length protein, in the 1 to 330 aa range, expressed in Baculovirus infected Sf9 cells, with >75%, suitable for WB, Phosphatase Activity.

View Alternative Names

PPP1A, PPP1CA, Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, PP-1A

4 Images
Functional Studies - Recombinant human PPP1A/PPP1CA protein (AB128559)
  • FuncS

Unknown

Functional Studies - Recombinant human PPP1A/PPP1CA protein (AB128559)

The specific activity of PPP1A/PPP1CA (ab128559) was determined to be 250 nmol/min/mg as per activity assay protocol

SDS-PAGE - Recombinant human PPP1A/PPP1CA protein (AB128559)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PPP1A/PPP1CA protein (AB128559)

SDS PAGE analysis of ab128559

Phosphatase Activity - Recombinant human PPP1A/PPP1CA protein (AB128559)
  • Phosphatase Activity

Unknown

Phosphatase Activity - Recombinant human PPP1A/PPP1CA protein (AB128559)

The specific activity of ab128559 was determined to be 228 nmol/min/mg.

SDS-PAGE - Recombinant human PPP1A/PPP1CA protein (AB128559)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PPP1A/PPP1CA protein (AB128559)

SDS-PAGE showing ab128559 at approximately 62 kDa.

Key facts

Purity

>75% Densitometry

Expression system

Baculovirus infected Sf9 cells

Tags

Tag free

Applications

WB, Phosphatase Activity

applications

Biologically active

Yes

Biological activity

The specific activity of ab128559 was determined to be 228 nmol/min/mg.

Accession

P62136

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 0.88% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.005% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Phosphatase Activity": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

This product was previously labelled as PPP1A

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"62 kDa","actualMolecularWeight":null,"aminoAcidEnd":330,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P62136","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.

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.

Specifications

Form

Liquid

Additional notes

Affinity purified.

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).. (Microbial infection) Necessary for alphaviruses replication.

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

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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.
See full target information PPP1CA

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Associated Products

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Recombinant human PPP1A/PPP1CA protein

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