Analytical Data
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Gene name
PPP1R3D
- Application
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Alternative Names
PPP1R6; Protein phosphatase 1-binding subunit R6; Protein phosphatase 1 regulatory subunit 6
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Species
Mouse
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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
A2AJW4
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Expression Region
Met1~Ile279
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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
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Protein Description
PPP1R3D, or Protein Phosphatase 1 Regulatory Subunit 3D, is a member of the protein phosphatase 1 (PP1) regulatory subunits, which play a crucial role in modulating the activity of PP1, a major serine/threonine phosphatase involved in various cellular processes, including cell division, glycogen metabolism, and signal transduction. The regulation of PP1 is essential for maintaining cellular homeostasis, and its dysregulation is implicated in numerous diseases, including cancer and diabetes. Recent studies have highlighted the importance of PPP1R3D in the regulation of glycogen metabolism and its potential role in metabolic disorders. Researchers have focused on the recombinant production of PPP1R3D to better understand its biochemical properties, interactions with PP1, and its regulatory mechanisms. The recombinant protein facilitates detailed studies on its structure-function relationship and has been instrumental in elucidating its role in various signaling pathways. Furthermore, the development of antibodies against PPP1R3D enables the investigation of its expression patterns and functionality in different tissues and disease states. Overall, the study of PPP1R3D as a recombinant protein is not only essential for understanding the fundamental biology of protein phosphatases but also holds promise for potential therapeutic applications in conditions where PP1 activity is disrupted. This research underscores the significance of protein-protein interactions and post-translational modifications in regulating cellular functions, paving the way for future studies aimed at developing targeted therapies based on the modulation of PPP1R3D and related pathways.
