Analytical Data
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Gene name
PSPH
- Application
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Alternative Names
PSPH；Phosphoserine phosphatase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE
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Molecular Weight
52.0kDa
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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
Phosphoserine phosphatase (PSPH) is an enzyme that plays a crucial role in the metabolic pathways involving serine and phosphoserine, which are key amino acids in cellular biochemistry. Its primary function is to dephosphorylate phosphoserine to serine, thereby regulating the levels of these amino acids and influencing various physiological processes, including cell growth, differentiation, and signaling. Research into PSPH has gained significant attention due to its implications in several diseases, including cancer and neurological disorders. Abnormal regulation of PSPH has been linked to tumorigenesis, making it a potential target for therapeutic intervention. Furthermore, understanding the structure and function of PSPH through recombinant protein studies can provide insights into its catalytic mechanisms and regulatory roles, offering avenues for drug discovery. Recent advances in recombinant DNA technology have enabled the efficient production of PSPH in model organisms, facilitating detailed biochemical and structural analyses. This research not only elucidates the enzyme's biological significance but also paves the way for the development of PSPH inhibitors that could be used in clinical settings, potentially leading to novel treatments for disorders linked to its dysregulation. The field continues to evolve, with ongoing studies aiming to map out the intricate network of PSPH's interactions within the cellular landscape.
