Analytical Data
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Gene name
X155S;X158S
- Application
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Alternative Names
PPP1CA; Serine/threonine-protein phosphatase PP1-alpha catalytic subunit; PP-1A; EC 3.1.3.16
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Species
Dog
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WMS6
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Expression Region
2-330aa(X155S;X158S)
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Molecular Weight
42.3 kDa
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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
The X155S and X158S recombinant proteins have garnered significant attention in the field of protein engineering and biotechnology due to their potential applications in therapeutics and diagnostics. These proteins are derivatives of the original X protein, modified to enhance their stability, functionality, and interaction with biological systems. Research has indicated that these specific mutations, X155S and X158S, may improve the proteins' binding affinity and specificity towards target molecules, making them valuable candidates for drug development and enzyme catalysis. Additionally, the study of these recombinant proteins provides critical insights into the structure-function relationships of proteins, shedding light on how slight alterations can influence biochemical properties and interactions. The investigation into X155S and X158S thus represents a pivotal step towards optimizing protein engineering strategies for various applications, including targeted drug delivery systems and biosensors. The advancements made in understanding these modified proteins contribute not only to the broader field of protein science but also hold the promise for innovative therapeutic interventions and improved diagnostic tools in clinical settings.
