Analytical Data
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Gene name
NT5C
- Application
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Alternative Names
NT5C；DNT1；UMPH2；5'(3')-deoxyribonucleotidase. cytosolic type
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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
Q8TCD5
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Expression Region
1-201aa
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AA Sequence
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADKVASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRLLSWSDNWREILDSKRGAAQRE
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Molecular Weight
28.4 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
NT5C, or nucleotidase 5' cytosolic, is an enzyme that plays a crucial role in nucleotide metabolism by hydrolyzing nucleotides to their respective nucleosides. Research on NT5C has gained significant attention due to its involvement in various physiological and pathological processes, including cellular energy regulation, immune responses, and tumor progression. Abnormal expression or activity of NT5C has been implicated in several diseases, particularly cancer, where it is associated with resistance to chemotherapy and poor patient prognosis. The enzyme's ability to modulate nucleotide pools can influence cell viability and proliferation, making it a potential therapeutic target. Recent advances in recombinant protein technology have facilitated the purification and characterization of NT5C, enabling detailed studies of its enzymatic properties and biological functions. These studies have the potential to reveal novel insights into the mechanisms by which NT5C contributes to disease states, paving the way for the development of targeted therapies aimed at restoring normal nucleotide metabolism. Understanding the structure-function relationship of NT5C, as well as its interactions with other biomolecules, is essential for elucidating its role in health and disease. Overall, the investigation of NT5C as a recombinant protein not only enhances our fundamental understanding of nucleotide metabolism but also opens up opportunities for innovative approaches in the treatment of diseases where NT5C dysfunction is a contributing factor.
