Analytical Data
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Gene name
APRT
- Application
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Alternative Names
APRT；Adenine phosphoribosyltransferase
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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
P07741
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Expression Region
1-180aa
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AA Sequence
MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE
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Molecular Weight
46.5kDa
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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
APRT (adenine phosphoribosyltransferase) is an important enzyme involved in purine metabolism, specifically in the salvage pathway that recycles adenine nucleotides. Deficiencies in APRT can lead to accumulation of toxic metabolites, resulting in various health issues, including kidney stones and nephropathy. Research on recombinant APRT has gained momentum due to its potential applications in understanding metabolic disorders and developing therapeutic interventions. The study of APRT not only provides insights into the molecular mechanisms of nucleotide metabolism but also offers a platform for enzyme engineering and drug design. Recombinant forms of APRT can be utilized in functional assays, drug screening, and as a reference for studying enzyme kinetics and regulatory mechanisms. Furthermore, understanding the structure-function relationship of APRT can aid in the development of small molecule inhibitors or modulators, which have therapeutic potential in treating diseases associated with purine metabolism dysregulation. As the exploration of APRT progresses, it holds promise for unraveling the complexities of metabolic pathways and addressing related health complications.
