Deoxyribonuclease I (DNase I) is a nuclease found in a wide variety of cells and tissues. It targets and cleaves the phosphodiester bond adjacent to the pyrimidine to produce polynucleotides with a phosphate group at the 5' end and a hydroxyl group at the 3' end. The average digestion product is about the size of a polynucleotide. DNase can catalyse different forms of DNA such as single-stranded DNA, double-stranded DNA and even chromatin (its cutting rate is affected by histones). The optimum operating range is pH 7-8. The activity of DNase is Ca²⁺ dependent and can be activated by divalent metal ions such as Co²⁺, Mn²⁺ and Zn²⁺. 5 mM Ca²⁺ can protect the enzyme from hydrolysis. In the presence of Mg²⁺, the enzyme can randomly recognise and cut any site on either DNA chain; in the presence of Mn²⁺, it can recognise both DNA chains simultaneously and cut at almost the same site. DNase I was first isolated from pancreas, and mammalian pancreas is still a major source of the enzyme.

This product is derived from bovine pancreas and consists of four chromatographically distinct components A, B, C and D in a molar ratio of 4:1:1, with component D being very small. It is often used in molecular biology experiments to remove DNA from proteins or to create gaps in DNA to allow the insertion of labelled bases into DNA. This product is supplied as a lyophilised powder containing calcium chloride with an enzyme activity of ≥2000 Kunitz units/mg protein.

Features

High activity

Low residual RNase

Stable Quality: No variations between batches

Applications

DNA removal in RNA extraction; DNA removal in in vitro transcription; DNase I blotting; nick translation; RNA purification;

Specification

Components