Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PPP1CB), human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 2-327aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-tagged. Target Protein Sequence: ADGELNVDSL ITRLLEVRGC RPGKIVQMTE AEVRGLCIKS REIFLSQPIL LELEAPLKIC GDIHGQYTDL LRLFEYGGFP PEANYLFLGD YVDRGKQSLE TICLLLAYKI KYPENFFLLR GNHECASINR IYGFYDECKR RFNIKLWKTF TDCFNCLPIA AIVDEKIFCC HGGLSPDLQS MEQIRRIMRP TDVPDTGLLC DLLWSDPDKD VQGWGENDRG VSFTFGADVV SKFLNRHDLD LICRAHQVVE DGYEFFAKRQ LVTLFSAPNY CGEFDNAGGM MSVDETLMCS FQILKPSEKK AKYQYGGLNS GRPVTPPRTA NPPKKR. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is 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 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: 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. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. 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 (PubMed:23396208). Reference: "Characterization of the protein phosphatase 1 catalytic subunit in endothelium: involvement in contractile responses."Verin A.D., Csortos C., Durbin S.D., Aydanyan A., Wang P., Patterson C.E., Garcia J.G.J. Cell. Biochem. 79:113-125(2000). Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. 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