Analytical Data
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Gene name
ALP
- Application
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Alternative Names
ALP；ALP；KIAA1709；RNA cytidine acetyltransferase
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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
Q53GG5
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Expression Region
1-316aa
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AA Sequence
MPQTVILPGPAPWGFRLSGGIDFNQPLVITRITPGSKAAAANLCPGDVIL AIDGFGTESMTHADAQDRIKAAAHQLCLKIDRGETHLWSPQVSEDGKAHP FKINLESEPQEFKPIGTAHNRRAQPFVAAANIDDKRQVVSASYNSPIGLY STSNIQDALHGQLRGLIPSSPQNEPTASVPPESDVYRMLHDNRNEPTQPR QSGSFRVLQGMVDDGSDDRPAGTRSVRAPVTKVHGGSGGAQRMPLCDKCG SGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFIEGELYCETHARAR TKPPEGYDTVTLYPKA
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Molecular Weight
61 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 ALP (alkaline phosphatase) recombinant proteins has gained significant attention due to their crucial roles in various biological processes and potential applications in biotechnology and medicine. ALP is an important enzyme that catalyzes the hydrolysis of phosphate esters in an alkaline environment, playing vital roles in processes such as dephosphorylation, bone mineralization, and liver function. Recombinant technology allows for the production of ALP with specific properties and modifications, facilitating detailed studies of its function, regulation, and interactions. Furthermore, recombinant ALP is increasingly used in diagnostic assays, therapeutic applications, and as a reporter enzyme in molecular biology. The ability to produce ALP in heterologous systems, such as bacteria or yeast, not only enhances yield and purity but also allows for the incorporation of post-translational modifications that can affect enzyme activity and stability. Current research focuses on optimizing the expression systems, refining purification methods, and engineering ALP variants with enhanced properties for specific applications. Additionally, understanding the structural and functional dynamics of this enzyme at the molecular level holds promise for developing novel therapeutic strategies for diseases associated with dysregulated phosphatase activity. As a result, the exploration of ALP recombinant proteins stands at the intersection of fundamental biochemical research and practical biotechnological applications, reflecting their importance in both scientific and commercial realms.
