DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. It acts on single-stranded DNA, double-stranded DNA, and chromatin.

DNase I, (RNase-free) is an endonuclease that nonspecifically cleaves DNA to release di-, tri- and oligonucleotide products with 5´-phosphorylated and 3´-hydroxylated ends. DNase I acts on single- and double-stranded DNA, chromatin and RNA:DNA hybrids.

Thermo Scientific DNase I, RNase-free is an endonuclease that digests single- and double-stranded DNA. It hydrolyzes phosphodiester bonds producing mono- and oligodeoxyribonucleotides with 5'-phosphate and 3'-OH groups. The enzyme activity is strictly dependent on Ca2+ and is activated by Mg2+ or Mn2+ ions.

DNase I is suitable for removing DNA from protein preparations, nick translating DNA, and generating random fragments for dideoxy sequencing. NOTE: for removing DNA from RNA preparations, use Amplification Grade DNase I (Cat. No. 18068-015).

A powerful research tool for DNA manipulations, DNase I is used in a range of molecular biology applications. Some of its uses include: 1. Degradation of contaminating DNA after RNA isolation, 2. "Clean-up" of RNA prior to RT-PCR and after in vitro transcription, 3. Identification of protein binding sequences on DNA (DNase I footprinting), 4.

2001年6月1日 · In this review, available structural data of deoxyribonucleases I (DNases I) from several mammalian species, hen, snake and frog are summarized. Comparative studies on enzymatic and immunological properties and glycosylation are discussed, and several evolutionary conclusions are presented.

Deoxyribonuclease I (DNase I, EC 3.1.21.1) is an endonuclease that preferentially attacks double-stranded DNA in a Ca 2 +-dependent manner to produce oligonucleotides with 5′-phospho and 3′-hydroxy termini. This review deals with the biochemical properties and …

DNase I is a ubiquitous endonuclease that cleaves the phosphodiester backbone of the DNA double helix in the presence of divalent cations, introducing single-stranded nicks through hydrolysis of the P-O3′-bond and yielding 5′-phosphorylated fragments [1], [2].

DNase I is one of the most well characterized endonucleases of mammalian origin. It is a double-strand-specific endonuclease that requires bivalent cations for maximal activity. Application. Isolation procedures for proteins (e.g., membrane proteins).

Recombinant DNase I (rDNase I) is a recombinant form of bovine DNase I purified from an overexpressing host. rDNase I is bovine-free. In addition, the host expressing rDNase I contains 107-fold less endogenous RNase activity than pancreatic tissues, the source for bovine DNase I.