Recombinant Human PP1C gamma Protein

Name: Recombinant Human PP1C gamma Protein
Brand: Beta LifeScience
SKU: BLA-7205P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P36873
Synonym	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
Description	Recombinant Human PP1C gamma Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MGSSHHHHHH SSGLVPRGSH MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE KKKPNATRPV TPPRGMITKQ AKK
Molecular Weight	39 kDa including tags
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target 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. 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.
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 References	HGNC: 9283 OMIM: 176914 KEGG: hsa:5501 STRING: 9606.ENSP00000335084 UniGene: Hs.79081

Gene Functions References

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
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
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
knock-down of PP1gamma alleviates glioma proliferation by reducing p65 transportation into the nucleus. PMID: 26936744
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
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
the lipin-1 N-terminal domain is important for its catalytic activity, nuclear localization, and binding to PP-1cgamma PMID: 24558042
Protein phosphatase 1gamma promotes the alternative splicing of CaMKIIdelta through its interaction with alternative splice factor. PMID: 24196533
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
Depletion of PP1gamma enhances the localization of the SMN complex and snRNPs to Cajal bodies. PMID: 22454514
NUAK1 and PPP1CC are identified as positional candidate loci for skeletal muscle strength phenotypes. PMID: 21750233
The counteracting Nek2A and PP1gamma activities on the centrosome linker are controlled by Plk1. PMID: 21723128
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
gamma isoform of the human protein phosphatase-1 catalytic subunit (PP1c gamma) as a high affinity in vitro target of phosphatidic acid PMID: 11856740
Nek2.PP1C complex is regulated by Inh2 via inhibition of phosphatase activity to initiate centrosome separation PMID: 12221103
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
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
crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c PMID: 16343532
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
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
Results describe a specific intracellular pathway involving the activation of PP1cgamma to mediate the effects of confluence-induced beta-catenin dephosphorylation. PMID: 17996206
PP1cgamma1 overexpression promotes VSMC survival by interfering with JNK1 and p53 phosphorylation cascades involved in apoptosis PMID: 18540044

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.