Mammalian DNA polymerase κ, a member of the UmuC/DinB nucleotidyl transferase superfamily, has been implicated in spontaneous mutagenesis (1). Human DNA polymerase κ copies undamaged DNA with average single-base subsitution and deletion error rates of 7 x 10-3 and 2 x 10-3, respectively. These error rates are high when compared to those of most other DNA polymerases (2). DNA polymerase κ has important role in the mutagenic bypass of certain types of DNA lesions (3). This product was over-expressed as a recombinant protein in E. coli with a plasmid carrying a C-terminal histidine-tagged human DNA polymerase κ (1-560 aa), and highly purified by several steps of chromatography (2). The product is catalytically active and its molecular weight is 65 kD (Fig 1). Activity of this product has been confirmed by a user researcher even if it was diluted 8,000-fold.
1) Analysis of mutagenesis
Fig.1 Polyacrylamide gel electrophoresis of DNA polymerase κ protein.
DNA Polymerase (KAPPA)
1) Friedberg EC et al “The many faces of DNA polymerases: strategies for mutagenesis and for mutational
avoidance.” Proc Natl Acad Sci USA 97: 5681-5683 (2000) PMID: 10811923
2) Ohashi E et al “Fidelity and processivity of DNA synthesis by DNA polymerase kappa, the product of the
human DINB1 gene.” J Biol Chem 275: 39678-39684 (2000) PMID: 11006276
3) Ohashi E et al “Error-prone bypass of certain DNA lesions by the human DNA polymerase kappa.” Genes
Dev 14: 1589-1594 (2000) PMID: 10887153
To be used for research only. DO NOT use for human gene therapy or clinical diagnosis.