Analytical Data
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Gene name
HGPRT
- Application
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Alternative Names
(HGPRT)(HGPRTase)
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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
P00492
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Expression Region
MHHHHHHLSTAADMQGVVTDGMASGLDKDYLKPDDGGGGSGFLGPAPAPAPAPA+2-218aa
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Molecular Weight
29.8 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
Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is a crucial enzyme in the purine salvage pathway, which recycles purine bases for nucleotide synthesis. Deficiency in HGPRT can lead to the x-linked genetic disorder known as Lesch-Nyhan syndrome, characterized by neurological dysfunction and self-aggressive behaviors. Understanding the structure and function of HGPRT is essential for developing targeted therapies for this condition. Research on recombinant HGPRT proteins has gained traction, as these proteins can be produced in vitro for functional studies and therapeutic applications. Advances in recombinant DNA technology allow researchers to express and purify HGPRT from various host systems, such as bacteria or yeast, facilitating detailed biochemical and structural analyses. These studies aim to elucidate the enzyme's catalytic mechanisms, substrate specificity, and interactions with inhibitors. Furthermore, HGPRT's potential role as a drug target is being explored, as modulating its activity may offer novel therapeutic avenues for treating purine metabolism disorders. Overall, the investigation of recombinant HGPRT not only enhances our understanding of purine metabolism but also opens up possibilities for innovative treatments for related genetic disorders.
