Recombinant Human Serine/threonine-protein phosphatase PP1-gamma catalytic subunit(PPP1CC)

In Stock
Code CSB-EP018505HU
Size US$306
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 85% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
PP 1G; PP-1G; PP1C; PP1G; PP1G_HUMAN; PP1gamma; PPP 1G; PPP1CC; PPP1G; Protein phosphatase 1; catalytic subunit; gamma isozyme; Protein phosphatase 1C catalytic subunit; Serine/threonine phosphatase 1 gamma; Serine/threonine protein phosphatase PP1 gamma catalytic subunit; Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Homo sapiens (Human)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
44.3 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Tris-based buffer,50% glycerol
and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

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. 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.
Gene References into Functions
  1. Here the authors show how Ki-67 and RepoMan form mitotic exit phosphatases by recruiting PP1, how they distinguish between distinct PP1 isoforms and how the assembly of these two holoenzymes are dynamically regulated by Aurora B kinase during mitosis. PMID: 27572260
  2. Data suggest that PPP1CC catalyzes hydrolysis of an assortment of substrates (aryl methylphosphonates, fluorophosphate esters, phosphorothioate esters, phosphodiesters); conservative mutation of R221 to K results in a mutant that is more effective catalyst toward monoanionic substrates; PPP1CC does not catalyze the hydrolysis of a sulfate ester, which is unexpected. PMID: 28678475
  3. PP1gamma is upregulated in hepatocellular carcinoma (HCC) cell lines and HCC specimens and promotes cancer cell proliferation through regulation of p53. High expression of PP1gamma in HCC cells contributed to doxorubicin resistance. PMID: 27921263
  4. knock-down of PP1gamma alleviates glioma proliferation by reducing p65 transportation into the nucleus. PMID: 26936744
  5. PP1gamma may be a novel target of the HPV-16 oncoproteins and indicate that it might be a potential novel biomarker for HPV-16 induced malignancy. PMID: 25886518
  6. Although no obvious defects in the progression of mitosis were observed, the timing of dephosphorylation of the mutant Ki67 in anaphase was delayed, indicating that Ki67 itself is one of the substrates of PP1gamma-Ki67. PMID: 25012651
  7. the lipin-1 N-terminal domain is important for its catalytic activity, nuclear localization, and binding to PP-1cgamma PMID: 24558042
  8. Protein phosphatase 1gamma promotes the alternative splicing of CaMKIIdelta through its interaction with alternative splice factor. PMID: 24196533
  9. When the Px(T)PxR motif is deleted or mutated via insertion of a phosphorylation site mimic (T311D), PP-1c fails to bind to all three ASPP proteins, ASPP1, ASPP2 and iASPP. PMID: 23088536
  10. Depletion of PP1gamma enhances the localization of the SMN complex and snRNPs to Cajal bodies. PMID: 22454514
  11. NUAK1 and PPP1CC are identified as positional candidate loci for skeletal muscle strength phenotypes. PMID: 21750233
  12. The counteracting Nek2A and PP1gamma activities on the centrosome linker are controlled by Plk1. PMID: 21723128
  13. The ataxia telangiectasia, mutated and Rad3-related-Chk1 axis regulates H3-pThr 11 dephosphorylation on DNA damage, at least in part by the activation of PP1gamma through Chk1-dependent inhibition of cyclin dependent kinases. PMID: 20948546
  14. gamma isoform of the human protein phosphatase-1 catalytic subunit (PP1c gamma) as a high affinity in vitro target of phosphatidic acid PMID: 11856740
  15. Nek2.PP1C complex is regulated by Inh2 via inhibition of phosphatase activity to initiate centrosome separation PMID: 12221103
  16. Tat might function as a nuclear regulator of PP1 and interaction of Tat with PP1 is critical for activation of HIV-1 transcription by Tat PMID: 16131488
  17. analysis of novel phosphatidic acid (PA) binding region on PP1c gamma that contains a unique loop-strand structural fold responsible for the interaction with PA PMID: 16201749
  18. crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c PMID: 16343532
  19. We demonstrate that interaction with NIPP1 mediates decreased PP1gamma activity in hypoxia, an event which may constitute an inherent part of the cellular oxygen-sensing machinery and may play a role in physiologic adaptation to hypoxia. PMID: 16826568
  20. Data show that URI and PP1gamma are components of an S6K1-regulated mitochondrial pathway dedicated to oppose sustained S6K1 survival signaling and to ensure that the threshold for apoptosis is set based on nutrient and growth factor availability. PMID: 17936702
  21. Results describe a specific intracellular pathway involving the activation of PP1cgamma to mediate the effects of confluence-induced beta-catenin dephosphorylation. PMID: 17996206
  22. PP1cgamma1 overexpression promotes VSMC survival by interfering with JNK1 and p53 phosphorylation cascades involved in apoptosis PMID: 18540044

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Subcellular Location
Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus, nucleoplasm. Nucleus speckle. Chromosome, centromere, kinetochore. Cleavage furrow. Midbody. Mitochondrion. Cytoplasm, cytoskeleton, microtubule organizing center.
Protein Families
PPP phosphatase family, PP-1 subfamily
Database Links

HGNC: 9283

OMIM: 176914

KEGG: hsa:5501

STRING: 9606.ENSP00000335084

UniGene: Hs.79081

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