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(E.C.2.7.1.74) * Pricing updated September 23rd, 2011. Prices are subject to change without notice. Shipping charges are not included. ** One unit of deoxycytidine kinase converts 1.0 µmole of deoxyinosine and ATP to dIMP and ADP per minute at pH 8 at 37°C, as measured by a coupled IMPDH enzyme system. Specific Activity: ≥ 0.25 U/mg protein. For other size, please contact us Click to order or to get further information |
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NOVOCIB's human deoxycytidine kinase (dCK) is a recombinant protein of ca. 33kDa cloned by RT-PCR amplification of mRNA extracted from human hepatoma cells and expressed in E.coli.
Human deoxycytidine kinase plays a key role in the salvage pathway of deoxynucleotides synthesis providing resting cells with deoxynucleotides for DNA repair and mitochondrial DNA synthesis. The enzyme has a broad substrate specificity and provides the phosphorylation of both purine and pyrimidine deoxynucleosides (e.g. deoxyadenosine (dA), deoxyguanosine (dG)) and deoxycytidine (dC) and pyrimidine ribonucleoside, cytidine (C)). The enzyme can utilize ATP or UTP as phosphate donor, UTP being a preferred substrate.
Deoxycytidine kinase is responsible for the phosphorylation and activation of numerous nucleoside analogs used to treat cancer (e.g. cytarabine, gemcitabine, cladribine and fludarabine) including nucleoside analogs of non-physiological L-chirality (e.g. 3TC, lamivudine, anti-HIV and anti-hepatitis B agent). Three-dimensional structures of dCK in complex with various pyrimidine(1) and purine(2,3) D- and L-nucleosides have been solved providing structural basis for activation of L- and D-nucleoside analogs.
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Human deoxycytidine kinase plays a key role in the salvage pathway of deoxynucleotides synthesis providing resting cells with deoxynucleotides for DNA repair and mitochondrial DNA synthesis. The enzyme has a broad substrate specificity and provides the phosphorylation of both purine and pyrimidine deoxynucleosides (e.g. deoxyadenosine (dA), deoxyguanosine (dG)) and deoxycytidine (dC) and pyrimidine ribonucleoside, cytidine (C)). The enzyme can utilize ATP or UTP as phosphate donor, UTP being a preferred substrate.
Deoxycytidine kinase is responsible for the phosphorylation and activation of numerous nucleoside analogs used to treat cancer (e.g. cytarabine, gemcitabine, cladribine and fludarabine) including nucleoside analogs of non-physiological L-chirality (e.g. 3TC, lamivudine, anti-HIV and anti-hepatitis B agent). Three-dimensional structures of dCK in complex with various pyrimidine(1) and purine(2,3) D- and L-nucleosides have been solved providing structural basis for activation of L- and D-nucleoside analogs.
 Unit Definition: One unit of deoxycytidine kinase converts 1.0 µmole of deoxyinosine and ATP to dIMP and ADP per minute at pH 8 at 37°C, as measured by a coupled IMPDH enzyme system. (see dCK Assay Kit for further details) Specific Activity: ≥ 0.25 unit/mg protein. Purity: controlled by 12%AA SDS-PAGE. |
The enzymatic activity of human recombinant dCK was confirmed by ion-pair HPLC analysis (Agilent 1100 series, Zorbax C18plus) as shown by formation of dCMP and ADP (red) from deoxycytidine and ATP (blue).
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| Assay condition: Enzymatic activity of dCK is measured by spectrophotometric assays in a coupled lactate dehydrogenase/pyruvate kinase system. Assays were carried out at 37°C, at 50mM Tris-HCl pH7,6; 50mM KCl, 10mM MgCl2, 5mM ATP, 0,1mM NADH, 1mM phosphoenolpyruvate, 1mM DTT, PK 10U/ml, LDH 15U/ml, 0,9µM dCK. Reaction was followed in an iEMS Reader MF (Labsystems) microtiter plate reader at 340nm. Nucleosides, nucleotides, LDH and PK were purchased from Sigma-Aldrich. |
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