Analytical Data
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Gene name
NT5C3A/NT5C3
- Application
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Alternative Names
UMPH1; PSN1; PN-I; UMPH; P5'N-1; p36; cN-III; Pyrimidine 5'-nucleotidase 1; Uridine 5'-monophosphate hydrolase 1
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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
B2GUX5
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Expression Region
Val8~Val289
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Molecular Weight
38kDa
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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
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Protein Description
NT5C3A (Nucleotidase 5' cytosolic 3A) and its isoform NT5C3 play crucial roles in nucleotide metabolism and signaling pathways. Both proteins are part of the nucleoside triphosphate diphosphate family, involved in the hydrolysis of nucleotide mono- and diphosphates to regulate cellular concentrations of nucleotides, which are essential for various biological processes including DNA and RNA synthesis, energy metabolism, and cell signaling. Alterations in NT5C3A and NT5C3 expression have been linked to several pathological conditions, including cancer and neurological disorders, highlighting their potential as biomarkers and therapeutic targets. Recent studies have focused on characterizing the enzymatic properties, substrate specificity, and structural attributes of these proteins through recombinant expression systems. This research is imperative not only for understanding their functional mechanisms but also for exploring their roles in diseases, offering insights into novel treatment strategies. The successful production of NT5C3A and NT5C3 as recombinant proteins allows for in-depth studies of their biological functions, interactions with other molecules, and the impact of mutations associated with disease. Such investigations pave the way for developing targeted therapies that can modulate their activity, providing a promising avenue for therapeutic intervention in disorders linked to nucleotide dysregulation. Understanding the intricate roles of NT5C3A and NT5C3 in cellular physiology and pathophysiology remains a vital area of biomedical research.
