Analytical Data
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Gene name
phosphatase
- Application
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Alternative Names
PiALP
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Species
Prevotella intermedia
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Source
E. coli
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Tag
N- His-GST & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P81800
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Expression Region
1-20aa
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Molecular Weight
32.1 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
Phosphatases are a class of enzymes that play a crucial role in various cellular processes by catalyzing the removal of phosphate groups from proteins and other molecules. These enzymes are essential for regulating signaling pathways, cell growth, and metabolism, making them vital for maintaining cellular homeostasis. Dysregulation of phosphatase activity is often associated with various diseases, including cancer, diabetes, and neurodegenerative disorders, highlighting their importance as therapeutic targets. In recent years, the production of recombinant phosphatases has gained momentum due to advancements in biotechnology, enabling researchers to generate these enzymes in a controlled manner for detailed biochemical studies. The ability to produce large quantities of functional phosphatases in a recombinant form allows for a better understanding of their structure-function relationships, substrate specificity, and kinetic properties. Moreover, recombinant phosphatases can be engineered for enhanced activity, stability, or altered substrate specificity, opening new avenues for potential drug development and therapeutic applications. Overall, research on recombinant phosphatases is pivotal for unraveling complex biological systems and developing innovative strategies for disease intervention.
