Analytical Data
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Gene name
PPP1R10
- Application
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Alternative Names
CAT53; FB19; PNUTS; p99; Phosphatase 1 nuclear targeting subunit; MHC class I region proline-rich protein CAT53; PP1-binding protein of 114 kDa
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96QC0
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Expression Region
Met1~Glu275
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Molecular Weight
36kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
PPP1R10, also known as Protein Phosphatase 1 Regulatory Subunit 10, is a critical component in the regulation of protein phosphatase 1 (PP1), an essential enzyme involved in various cellular processes such as cell cycle regulation, signal transduction, and gene expression. The study of PPP1R10 has gained attention due to its role in modulating the activity of PP1, thereby influencing numerous cellular functions. Dysregulation of the PP1 signaling pathway has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Investigating the structure and function of recombinant PPP1R10 provides valuable insights into its regulatory mechanisms and potential therapeutic targets. Recent advancements in structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, have facilitated the detailed characterization of PPP1R10 and its interactions with PP1 and other binding partners. Furthermore, the development of recombinant PPP1R10 proteins offers opportunities for functional assays, enabling researchers to explore its biological roles in a controlled environment. Understanding the intricate workings of PPP1R10 can lead to the identification of novel interventions for diseases associated with its dysregulation, ultimately contributing to the advancement of precision medicine. As a result, research on PPP1R10 not only deepens our understanding of PP1 regulation but also opens new avenues for therapeutic exploration in the context of various pathologies.
