Analytical Data
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Gene name
Alkaline Phosphatase/ALPI
- Application
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Alternative Names
/
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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
P09923
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Expression Region
20-503aa
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Molecular Weight
58.4 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
Alkaline phosphatase (ALP) is a crucial enzyme involved in various physiological processes, such as bone mineralization, cellular signaling, and detoxification. The recombinant form of alkaline phosphatase (recombinant ALPI) has gained significant attention in biomedical research and therapeutic applications due to its stability, high purity, and the ability to modify its properties through genetic engineering. ALPI is expressed in multiple tissues, primarily in the liver, intestines, and bones, making it a useful biomarker for various diseases, including liver dysfunction and bone disorders. Moreover, the enzyme's role in hydrolyzing phosphate groups from molecules has implications in cancer research, as alterations in ALP levels can be indicators of tumor progression and metastasis. Recent advancements in recombinant DNA technology have facilitated the production of ALPI in microbial and eukaryotic systems, allowing for the exploration of its structure-function relationship and the development of novel therapeutic agents. Overall, the study of recombinant alkaline phosphatase not only enhances our understanding of its biological functions but also opens new avenues for clinical applications, including the development of enzyme-based diagnostics and therapeutic strategies.
