Analytical Data
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Gene name
PSP
- Application
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Alternative Names
L-3-phosphoserine phosphatase O-phosphoserine phosphohydrolase
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P78330
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Expression Region
1-225aa
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Molecular Weight
52 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
Related Products
Protein Description
The study of PSP (plasma secretory protein) recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including biotechnology and medicine. PSPs are a class of proteins involved in the regulation of immune responses, tissue repair, and inflammation. Their unique structural properties and functionalities make them ideal candidates for therapeutic interventions and as biomarkers for disease diagnostics. Researchers have focused on the recombinant expression of PSPs in various host systems, such as bacteria, yeast, and mammalian cells, to produce large quantities of these proteins for functional characterization and practical applications. Advances in genetic engineering techniques and protein purification methods have facilitated the successful production and refinement of PSPs, enabling scientists to explore their roles in cell signaling pathways and their therapeutic potential against various diseases, including cancer and autoimmune disorders. The growing understanding of PSP structural biology has also opened avenues for the design of optimized proteins with enhanced stability and activity. As the demand for novel therapeutic agents rises, the exploration of PSP recombinant proteins represents a promising avenue for developing innovative solutions to address health challenges.
