Analytical Data
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Gene name
PPP1Ca
- Application
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Alternative Names
PPP1C-A; PPP1-CA; PP-1A; PPP1A; Serine/Threonine-Protein Phosphatase PP1-Alpha Catalytic Subunit
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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
P62136
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Expression Region
Ser2~Lys330
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Molecular Weight
41kDa
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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
PPP1Ca, or Protein Phosphatase 1 Catalytic Subunit Alpha, is a critical enzyme in the regulation of various cellular processes, including cell division, metabolism, and signal transduction. Dysregulation of PPP1Ca has been implicated in numerous diseases, particularly cancer, making it a significant target for therapeutic intervention. Research into PPP1Ca's structure and function has illuminated its role in modulating protein phosphorylation, a key mechanism in cellular signaling pathways. The development of recombinant PPP1Ca proteins is vital for elucidating the detailed mechanisms of its action, allowing researchers to explore its interactions with substrates and regulatory proteins. By producing these proteins in heterologous systems, scientists can overcome challenges related to the purification and functional analysis of native PPP1Ca, which is often complicated by post-translational modifications. Moreover, recombinant PPP1Ca can be used to screen for small molecules that could inhibit or activate its activity, paving the way for novel therapeutic strategies. As the understanding of PPP1Ca continues to evolve, its potential as a biomarker for disease and a target for drug development is becoming increasingly recognized, underscoring the importance of ongoing research in this field.
