Analytical Data
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Gene name
Alkaline Phosphatase/ALPL
- Application
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Alternative Names
BALP; BSAP; HOPS; AP-TNAP; TNSALP; Bone Alkaline Phosphatase; Alkaline Phosphatase,Tissue-Nonspecific Isozyme; Alkaline Phosphatase, Liver/Bone/Kidney
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P08289
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Expression Region
Phe18~Arg335
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Molecular Weight
37kDa
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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 an essential enzyme that plays a critical role in various biological processes, including mineralization, dephosphorylation, and signal transduction. The ALPL gene encodes tissue-nonspecific alkaline phosphatase, which is predominantly expressed in the liver, bone, and kidneys. Deficiency or abnormal activity of ALPL is associated with several metabolic bone disorders such as hypophosphatasia, characterized by defective mineralization and skeletal fragility. Due to its significant implications in both health and disease, ALPL has garnered attention as a biomarker for various conditions. Furthermore, the use of recombinant ALPL has become increasingly important for therapeutic and diagnostic applications, including enzyme replacement therapies. Advances in biotechnology have enabled the production of recombinant ALPL with high purity and specific activity, facilitating its use in research to better understand its biochemical mechanisms and interactions. Additionally, developing assays to measure ALP activity can aid in the diagnosis and monitoring of related diseases. Overall, the study of recombinant ALPL not only enhances our understanding of its physiological roles but also opens avenues for novel therapeutic strategies aimed at managing ALPL-related disorders.
