Human Deoxycytidine Kinase (dCK) WT

Recombinant full length (aa 1-260) wild-type Human Deoxycytidine kinase (dCK) purified by nickel-sepharose chromatography.


  • Highly pure - >99% (SDS-PAGE)
  • Phosphorylates physiological deoxyribonucleosides dC, dA, and dG
  • Phosphorylates nucleoside analogs (e.g., AraC, gemcitabine, clofarabine, 3TC)

Deoxycytidine kinase (dCK, EC: is required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG), and deoxyadenosine (dA). dCK has a broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents.

Also available: Human Deoxycytidine Kinase (dCK) (R104M, D133A)

From the laboratory of Arnon Lavie, PhD, University of Illinois at Chicago.

The Investigator's Annexe Part of The Investigator's Annexe program.

Catalog Number Product Size AVAILABILITY Price Qty
Human Deoxycytidine Kinase (dCK) WT, 100ug
100ug In stock
Regular Price:$323.00
Human Deoxycytidine Kinase (dCK) WT, 1mg
1mg In stock
Regular Price:$2,583.00

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Product Type: Protein
Name: WT human dCK
Accession ID: P27707
Source: Recombinant expression in E. coli
Molecular Weight: ~31 kDa
Fusion Tag(s): N-terminal His tag
Purity: >99% (SDS-PAGE)
Buffer: 25 mM Hepes pH7.5, 200 mM NaCitrate, 10% glycerol, 5 mM DTT, 1 mM EDTA
Concentration: 4.6mg/mL
Activity: 6 IU/mg protein; kcat= 0.05/sec with dC as substrate; One unit of WT human dCK converts 1.0 µmole of dC and ATP to dCMP and ADP per minute at pH 7.5 at 37°C, as measured by a coupled enzyme system with 200 µM dC and 1 mM ATP.
Storage: -80C
Shipped: Dry ice


SDS-PAGE Analysis

From the laboratory of Arnon Lavie, PhD, University of Illinois at Chicago.
  1. Sabini E, Ort S, Monnerjahn C, Konrad M, Lavie A. Structure of human dCK suggests strategies to improve anticancer and antiviral therapy. Nat Struct Biol. 2003 Jul;10(7):513-9.
  2. Sabini E, Hazra S, Konrad M, Lavie A. Nonenantioselectivity property of human deoxycytidine kinase explained by structures of the enzyme in complex with L- and D-nucleosides. J Med Chem. 2007 Jun 28;50(13):3004-14. Epub 2007 May 27.

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