

| Catalog No. | HX142014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Species reactivity | Human, Mouse, Rat | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Clonality | Polyclonal | ||||||||
| Isotype | IgG | ||||||||
| Immunogen | E. coli - derived recombinant Human PPP1CB (Met1-Arg327). | ||||||||
| Target | Serine/threonine-protein phosphatase PP1-beta catalytic subunit, PPP1CD, PP-1B, PPP1CB | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | P62140 | ||||||||
| Form | Liquid | ||||||||
| Storage buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
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| Product Usage Information |
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| Stability and Storage | 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. | ||||||||
| Background | Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PPP1CB) is a ~37 kDa protein. 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. 1. Nie, H. et al. (2013) Nature medicine 19, 322-8. PMID: 23396208 2. Liau, NPD. et al. (2022) Nature 609, 400-407. PMID: 35768504 3. Kwon, JJ. et al. (2022) Nature 609, 408-415. PMID: 35831509 4. Bonsor, DA. et al. (2022) Nature structural & molecular biology 29, 966-977. PMID: 36175670 | ||||||||
| Note | For research use only. |
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