Human PPP1CC protein (Recombinant) (N-His) (STJP008033)

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STJP008033
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Host: E. coli
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description : Recombinant-Human PPP1CC-N-His protein was developed from e. coli and has a target region of N-His. For use in research applications.
Formulation: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Storage Instruction: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt.
Gene Symbol: PPP1CC
Gene ID: 5501
Uniprot ID: PP1G_HUMAN
Immunogen Region: Met1-Lys323
Immunogen: Homo sapiens (Human)
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. Dephosphorylates RPS6KB1. 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. 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. Regulates the recruitment of the SKA complex to kinetochores. 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. Together with PPP1CA (PP1-alpha subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response. Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation. 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. The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c.
Protein Name Serine/Threonine-Protein Phosphatase Pp1-Gamma Catalytic Subunit
Pp-1g
Protein Phosphatase 1c Catalytic Subunit
Database Links Reactome: R-HSA-141444
Reactome: R-HSA-163560
Reactome: R-HSA-2173788
Reactome: R-HSA-2467813
Reactome: R-HSA-2500257
Reactome: R-HSA-400253
Reactome: R-HSA-5663220
Reactome: R-HSA-5673000
Reactome: R-HSA-68877
Reactome: R-HSA-9648025
Reactome: R-HSA-9726840
Reactome: R-HSA-9726842
Reactome: R-HSA-9828806
Cellular Localisation Cytoplasm
Nucleus
Nucleolus
Nucleoplasm
Nucleus Speckle
Chromosome
Centromere
Kinetochore
Cleavage Furrow
Midbody
Mitochondrion
Cytoskeleton
Microtubule Organizing Center
Colocalizes With Spz1 In The Nucleus
Colocalizes With Uri1 At Mitochondrion
Rapidly Exchanges Between The Nucleolar
Nucleoplasmic And Cytoplasmic Compartments
Highly Mobile In Cells And Can Be Relocalized Through Interaction With Targeting Subunits
In The Presence Of Ppp1r8 Relocalizes From The Nucleolus To Nuclear Speckles
Shows A Dynamic Targeting To Specific Sites Throughout The Cell Cycle
Highly Concentrated In Nucleoli Of Interphase Cells And Localizes At Kinetochores Early In Mitosis
Relocalization To Chromosome-Containing Regions Occurs At The Transition From Early To Late Anaphase
Also Accumulates At The Cleavage Furrow And Midbody By Telophase
Colocalizes With Dynlt4 In The Microtubule Organizing Center (Mtoc)
Alternative Protein Names Serine/Threonine-Protein Phosphatase Pp1-Gamma Catalytic Subunit protein
Pp-1g protein
Protein Phosphatase 1c Catalytic Subunit protein
PPP1CC protein

Information sourced from Uniprot.org