Analytical Data
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Gene name
ITPase
- Application
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Alternative Names
Non-canonical purine NTP pyrophosphatase Non-standard purine NTP pyrophosphatase Nucleoside-triphosphate diphosphatase Nucleoside-triphosphate pyrophosphatase
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BY32
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Expression Region
2-194aa
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Molecular Weight
48.3 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
ITPase (inosine triphosphate pyrophosphatase) is an essential enzyme that catalyzes the hydrolysis of inosine triphosphate (ITP) to inosine monophosphate (IMP) and inorganic pyrophosphate (PPi), playing a crucial role in nucleotide metabolism. The accumulation of ITP, which can arise from disruptions in purine metabolism, is implicated in various cellular dysfunctions and diseases, including cancer and neurodegenerative disorders. The importance of ITPase in maintaining nucleotide pool integrity, coupled with its regulatory functions in nucleotide biosynthesis and signaling pathways, has spurred extensive research into its structural and functional properties. Recombinant ITPase proteins have been produced to elucidate the enzyme's mechanistic aspects, enabling detailed studies on substrate specificity, kinetic parameters, and inhibition mechanisms. Understanding ITPase's structure-function relationship is vital for potential therapeutic interventions, particularly as its dysfunction may correlate with pathophysiological conditions. The development of high-throughput assays for screening ITPase inhibitors has also gained attention in drug discovery, highlighting the enzyme's significance in biomedical research. Overall, the study of recombinant ITPase proteins encapsulates a multidisciplinary approach, intertwining biochemistry, molecular biology, and pharmacology, aiming to reveal new insights into nucleotide metabolism and its implications for human health.
