Human Deoxycytidine Kinase (dCK) (R104M, D133A)

Recombinant full length (aa 1-260) Human Deoxycytidine kinase (dCK) variant (R104M, D133A) purified by nickel-sepharose chromatography.


  • Highly pure - >99% (SDS-PAGE)
  • Phosphorylates ALL four physiological deoxyribonucleosides dC, dA, dG, T
  • Posesses thymidine kinase activity

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: Wild-type Human Deoxycytidine Kinase (dCK)

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) (R104M, D133A), 100ug
100ug In stock
Regular Price:$376.00
Human Deoxycytidine Kinase (dCK) (R104M, D133A), 1mg
1mg In stock
Regular Price:$3,121.00

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Product Type: Protein
Name: Human dCK (R104M, D133A) (dCK-DM)
Accession ID: P27707 mutated at positions 104 and 133
Source: Recombinant expression in E. coli
Molecular Weight: ~31 kDa
Fusion Tag(s): N-terminal His tag
Purity: >99% (SDS-PAGE)
Buffer: 25 mM Tris pH7.5, 500 mM NaCl, 20 % glycerol, 10 mM DTT, 1 mM EDTA
Concentration: 4.8mg/mL
Activity: ? 145 IU/mg protein; kcat 1.22/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. Hazra S, Sabini E, Ort S, Konrad M, Lavie A. Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase. Biochemistry. 2009 Feb 17;48(6):1256-63. doi: 10.1021/bi802062w.
  3. Neschadim A, Wang JC, Sato T, Fowler DH, Lavie A, Medin JA. Cell fate control gene therapy based on engineered variants of human deoxycytidine kinase. Mol Ther. 2012 May;20(5):1002-13. doi: 10.1038/mt.2011.298. Epub 2012 Jan 24.

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