Analytical Data
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Gene name
NT5C3
- Application
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Alternative Names
NT5C3；NT5C3；P5N1；UMPH1；Cytosolic 5'-nucleotidase 3A
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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
Q9H0P0
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Expression Region
1-336aa
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AA Sequence
MRAPSMDRAA VARVGAVASA SVCALVAGVV LAQYIFTLKR KTGRKTKIIE MMPEFQKSSV RIKNPTRVEE IICGLIKGGA AKLQIITDFD MTLSRFSYKG KRCPTCHNII DNCKLVTDEC RKKLLQLKEK YYAIEVDPVL TVEEKYPYMV EWYTKSHGLL VQQALPKAKL KEIVAESDVM LKEGYENFFD KLQQHSIPVF IFSAGIGDVL EEVIRQAGVY HPNVKVVSNF MDFDETGVLK GFKGELIHVF NKHDGALRNT EYFNQLKDNS NIILLGDSQG DLRMADGVAN VEHILKIGYL NDRVDELLEK YMDSYDIVLV QDESLEVANS ILQKIL
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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
NT5C3, or 5'-nucleotidase, cytosolic, type III, is an important enzyme involved in nucleotide metabolism, specifically in the hydrolysis of nucleotide monophosphates to their respective nucleosides and inorganic phosphate. This enzyme is crucial for maintaining cellular nucleotide pools and regulating purine and pyrimidine metabolism. Research into NT5C3 has gained momentum due to its potential role in various diseases, including cancer and metabolic disorders. Elevated levels of NT5C3 have been associated with tumor progression and resistance to chemotherapy, making it a promising target for therapeutic interventions. Additionally, the study of NT5C3 recombinant protein has significant implications for understanding its enzymatic mechanisms and developing inhibitors. Recent advances in molecular cloning and protein expression techniques have facilitated the production of recombinant NT5C3, enabling detailed biochemical assays and structural analyses. These studies aim to elucidate the enzyme's function in health and disease, providing insights that could lead to novel strategies for disease management and treatment. As a result, NT5C3 is emerging as a critical focus area in biochemical research, with the potential to unveil new therapeutic pathways in oncology and beyond.
