Recombinant Human Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA)

Code CSB-YP018503HU
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Source Yeast
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Code CSB-EP018503HU
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Source E.coli
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Code CSB-EP018503HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP018503HU
MSDS
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Source Baculovirus
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Code CSB-MP018503HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PPP1CA
Uniprot No.
Alternative Names
Alpha isoform serine threonine protein phosphatase PP1alpha 1 catalytic subunit; Catalytic subunit; EC 3.1.3.16; 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
Species
Homo sapiens (Human)
Expression Region
2-330
Target Protein Sequence
SDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting 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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

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. 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.
Gene References into Functions
  1. Study reports a S6K/PP1alpha/B-Raf pathway that activates MAPK signaling in PI3K/AKT-driven cancers and is opposed by the promyelocytic leukemia (PML) tumor suppressor. Its importance in regulating prostate cancer cell migration and invasion and in metastatic human prostate cancer is demonstrated. PMID: 29335436
  2. Downregulation of the expression of DUSP1 or protein phosphatase 1 led to a decline in the beta2adrenergic receptormediated dephosphorylation of ERK1/2 PMID: 29257221
  3. human plasma protects against endothelial cell apoptosis through sustained BAD phosphorylation, which is achieved by, at least in part, a novel interaction between PP1 with PAI1. PMID: 28296156
  4. Data show that protein phosphatase-1 alpha (PP1alpha) is required to maintain checkpoint kinase 1 (CHK1) in a dephosphorylated state and for the accelerated replication fork progression in Spi1/PU.1 transcription factor-overexpressing cells. PMID: 28415748
  5. Data suggest that protein phosphatase 1, catalytic subunit, alpha isoform (PPP1CA) is a candidate sero-diagnostic and prognostic marker for badder cancer (BC). PMID: 29187447
  6. Rif1 can mediate MCM dephosphorylation at replication forks and that the stability of dephosphorylated replisomes strongly depends on Chk1 activity. PMID: 28273463
  7. Data, including data from studies using cells from knockout mice, suggest that gasotransmitter H(2)S up-regulates eIF2a phosphorylation by inhibiting PPP1CA via persulfidation, which in turn leads to transient suppression of global translation and activation of Atf4 expression. (eIF2a = eukaryotic initiation factor-2alpha; PPP1CA = protein phosphatase 1 catalytic subunit alpha; Atf4 = activating transcription factor 4) PMID: 28637872
  8. Protein phosphatase 1 (PP1) forms stable complexes with PP1-interacting proteins (PIPs) that guide the phosphatase throughout its life cycle and control its fate and function. PMID: 28202662
  9. The authors found that RNA recognition motif 1 (RRM1) in SRSF1 binds PP1 and represses its catalytic function through an allosteric mechanism. PMID: 28576472
  10. this study shows a pivotal role for PP1 in impeding IRF7-mediated IFN-alpha production in host immune responses PMID: 27469204
  11. The data support a model where Cdc7 (de)phosphorylation is the molecular switch for the activation and inactivation of DNA replication in mitosis, directly connecting Cdc7 and PP1a/Cdk1 to the regulation of once-per-cell cycle DNA replication in mammalian cells. PMID: 27105124
  12. These results indicate that PP1 is recruited to the extracellular calcium-dependent E-cadherin-catenin-PIP5K1a complex in the plasma membrane to activate PIP5K1a, which is required for PLC-g1 activation leading to keratinocyte differentiation. PMID: 27340655
  13. Data suggest that targeting protein phosphatase 1 catalytic subunit (PP1alpha) or the androgen receptor AR-PP1alpha interaction may be effective in castration-resistant prostate cancer (CRPC). PMID: 26636645
  14. Both PP-1 and PP-2A are directly involved in regulating eye development, and are aberrantly expressed in cataract and glaucoma patients. (Review) PMID: 26592247
  15. Data suggest that activation of TAZ (tafazzin) inhibits adipogenesis in mesenchymal stem cells; interaction of TAZ and protein phosphatases (PP1A, PP2A) up-regulates dephosphorylation and transport of TAZ to cell nucleus. PMID: 25979969
  16. ATG16L1 as a bona fide physiological CSNK2 and PPP1 substrate, which reveals a novel molecular link from CSNK2 to activation of the autophagy-specific ATG12-ATG5-ATG16L1 complex and autophagy induction PMID: 26083323
  17. PARD3 promotes interaction between PP1A and LATS1 to induce LATS1 dephosphorylation and inactivation,leading to dephosphorylation and activation of TAZ PMID: 26116754
  18. activation of the Nherf1-PP1alpha-TAZ pathway in osteoblasts is targeted by histone deacetylase inhibitors PMID: 26491017
  19. Protein phosphatase 1 (PP1) activity is critical for radiosensitization in non-small cell lung cancer cells and PP1 activators can serve as promising radiosensitizers to improve therapeutic efficacy. PMID: 26033480
  20. PP1alpha is an important proximal effector of Manumycin-A mediated lymphoma cell apoptosis. PMID: 25556058
  21. PP1alpha and class I histone deacetylase (HDAC1/2/3) signaling pathways are essential for the stress-induced BRD4 release from chromatin. PMID: 24939842
  22. 14-3-3zeta regulates nuclear trafficking of PP1alpha in mammalian cells PMID: 24956593
  23. Data indicate that the protein phosphatase 1 (PP1) binding domain in nuclear membrane protein lamina associated polypeptide 1B (LAP1B) was here identified as the REVRF motif at amino acids 55-59. PMID: 24116158
  24. Data show that tumor necrosis factor (TNF) tolerance in monocytic cells differentially inhibits NF-kappaB/transcription factor AP-1 and protein phosphatase 1 (PP1)-associated signaling. PMID: 24574500
  25. The protein phosphatase 1 directly interacts with Mdmx and specifically dephosphorylates Mdmx at Ser367. PMID: 23277204
  26. PP-1alpha and PP-1gamma not only antagonize each other in lung cancer cells, but also display differential functions in tumorigenicity. PMID: 23176181
  27. PPP1C isoforms have distinct contribution to the outside-in alphaIIbbeta3 signalling-dependent functions in HEK293 alphaIIbbeta3 cells. PMID: 23197154
  28. Findings indicate that phosphatases PP1alpha and PP1gamma are key regulators of RIG-I and MDA5 antiviral signaling. PMID: 23499489
  29. Studies suggest that any change in substrate specificity of the spinophilin : PP1 holoenzyme complex was probably due to direct modification of a PP1 substrate binding surface. PMID: 22284538
  30. Studies indicate that the diversity of the PP1 interactome and the properties of the PP1 binding code account for the exquisite specificity of PP1 in vivo. PMID: 22360570
  31. Studies indicate that the Ser/Thr phosphatases PP1 and PP2A are responsible for the dephosphorylation and activation of Rb proteins. PMID: 22299668
  32. PP1/NIPP1 is a novel molecular compass that controls directed cell migration. PMID: 22815811
  33. The molecular basis by which NIPP1 directs PP1 substrate specificity in the nucleus. PMID: 22940584
  34. Cell surface expression of the major amyloid-beta peptide (Abeta)-degrading enzyme, neprilysin, depends on phosphorylation by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK) and dephosphorylation by protein phosphatase 1a. PMID: 22767595
  35. analysis of selective regulation of NR2B by protein phosphatase-1 for the control of the NMDA receptor in neuroprotection PMID: 22479519
  36. Data show that knockdown of the catalytic subunit of PP1 (PP1Calpha), but not PP2A (PP2ACalpha), increased pS137-PFN1 levels. PMID: 22479341
  37. Results identify specific protein phosphatase 1alpha-interacting proteins in human brain. PMID: 22321011
  38. We have identified a novel mechanism for direct activation of P-Rex1 through PP1alpha-dependent dephosphorylation. PMID: 22242915
  39. a novel, acute mechanism of ERM regulation dependent on PP1alpha and plasma membrane ceramide. PMID: 22311981
  40. Changes in cell polarity proteins Par-3 and PP-1 are associated with altered expression and assembly of tight junction proteins claudin-2, -3, -5 and -7 and ZO-1, causing paracellular leakage in active coeliac disease. PMID: 21865402
  41. These findings define a novel molecular mechanism that YAP2 is positively regulated by PP1-mediated dephosphorylation in the cell survival. PMID: 21909427
  42. Results demonstrate that PP1-mediated inhibition of the key anti-apoptotic protein, Akt, plays an important role in SPH-mediated apoptosis in Jurkat cells. PMID: 21308747
  43. Results identify a molecular pathway by which leptin confers inhibitory action on insulin secretion, and impaired PP-1 inhibition by leptin may be involved in dysfunction of the adipoinsular axis during the development of hyperinsulinemia and NIDDM. PMID: 21427225
  44. PP1A and ASPP2 play a critical role in promoting TAZ function by antagonizing the LATS kinase through TAZ dephosphorylation. PMID: 21189257
  45. The deregulation of cellular NIPP1/PP1 holoenzyme affects RNAPII phosphorylation and pointing to NIPP1 as a potential regulatory factor in RNAPII-mediated transcription. PMID: 20941529
  46. Could use the urinary hTERT, SENP1, PPP1CA, and MCM5 mRNA to detect bladder cancer recurrence. PMID: 21106093
  47. PP-1 ( PP-1alpha or PP-1beta ) acts as a major phosphatase to dephosphorylate AKT1 at Thr-450 and thus modulate its functions in regulating gene expression, cell survival and differentiation. PMID: 20186153
  48. CSK21 and PP1A, whose functions are intimately associated with cell cycle regulation, might play key role in gliomagenesis. PMID: 20663907
  49. mammalian Wdr82 functions in a variety of cellular processes; PTW/PP1 phosphatase complex (PNUTS, Tox4, Wdr82, PP1) has a role in the regulation of chromatin structure during the transition from mitosis into interphase PMID: 20516061
  50. conclusion: protein phosphatase 1alpha associates with the non-catalytic domain of protein tyrosine phosphatase-PEST (PTP-PEST)and regulates PTP activity via dephosphorylation of phospho-Ser39 PMID: 19919952

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Subcellular Location
Cytoplasm. Nucleus. Nucleus, nucleoplasm. Nucleus, nucleolus.
Protein Families
PPP phosphatase family, PP-1 subfamily
Database Links

HGNC: 9281

OMIM: 176875

KEGG: hsa:5499

STRING: 9606.ENSP00000326031

UniGene: Hs.183994

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