GMP DNase I: The Purest and Most Reliable DNase for Your Research Needs
GMP DNase I is the purest and most reliable DNase available, making it the ideal choice for a wide range of research applications. With its high efficiency and specificity, GMP DNase I can completely degrade DNA in minutes, without damaging other biomolecules.
Deoxyribonuclease I (DNase I), also known as Deoxyribonuclease I, is a nucleic acid enzyme present in various cells and tissues. It is an endonuclease that cleaves phosphodiester bonds adjacent to pyrimidines, generating polynucleotides with a 5' phosphate group and a 3' hydroxyl group. The average digestion product size is a minimum of tetranucleotides. DNase I can catalyze various forms of DNA, including single-stranded DNA, double-stranded DNA, and even chromatin (its cutting rate is influenced by histones). The optimal working range is pH 7-8. DNase activity depends on Ca2+ 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 recognize and cleave at any site on either strand of DNA, while in the presence of Mn2+, it can simultaneously recognize both strands of DNA and cleave at almost the same sites. DNase I was originally isolated from the pancreas and remains one of the major sources of this enzyme in mammals.
|1||Deoxyribonuclease I / DNase I (GMP-grade)||200 U, 1 KU, 2 KU|
|Product Name||Deoxyribonuclease I / DNase I (GMP-grade)|
|Enzyme Activity||2 U/μL|
|Storage Buffer||20 mM sodium acetate (pH 6.5), 5 mM CaCl2, 0.1 mM PMSF, 50% glycerol|
|Activity Definition||At 25°C, pH 5.0, when acting on highly polymerized DNA, the amount of enzyme required to increase the absorbance at 260 nm by 0.001 per minute per milliliter is defined as one unit.|
|Shelf Life||24 months|
DNase I, a versatile nuclease, exhibits the capability to digest both single-stranded and double-stranded DNA, yielding monodeoxynucleotides or single/double-stranded oligodeoxynucleotides. It efficiently hydrolyzes phosphodiester bonds, generating monodeoxynucleotides and oligodeoxynucleotides with 5'-phosphate groups and 3'-OH groups, with the average digestion product size being the smallest tetranucleotide. Catalyzing various forms of DNA, including single-stranded DNA, double-stranded DNA, and chromatin (its cutting rate influenced by histones), DNase I operates optimally within a pH range of 7-8. Its activity is contingent on Ca2+ and can be activated by divalent metal ions like Co2+, Mn2+, Zn2+, etc. The presence of 5mm Ca2+ shields the enzyme from hydrolysis. In the presence of Mg2+, the enzyme can randomly recognize and cut at any site on any DNA strand; in the presence of Mn2+, it can simultaneously recognize both DNA strands and cut at nearly the same position, forming blunt ends or sticky ends with 1-2 nucleotides protruding.
- DNase I can typically be inactivated using heat-based methods. In scenarios necessitating the removal of residual denatured proteins, phenol-chloroform extraction is employed to precipitate RNA samples post-digestion at 37°C (without heating operation).
- GMP-compliant production system.
- DNase I finds widespread utility in RNA preparation devoid of DNA; removal of template DNA post in vitro transcription; preparation of DNA-free RNA before RT-PCR and RT-qPCR reactions; coupled with DNA polymerase I for DNA labeling via nick translation; and DNA fragment library construction.
This product is formulated for protein extraction experiments and serves as a reference guide.
- Reaction System: Incorporate the DNase I storage solution into the protein extraction solution at a 1/100 volume ratio (resulting in a final concentration of 20 U/mL). Supplement with 1 M MgCl2 at a 1/100 volume ratio.
- Reaction Conditions: Maintain a temperature of 37°C for a duration of 30-60 minutes. Subsequently, proceed with the planned protein extraction experiments.
Note: Eliminate EDTA from the initial protein lysate, as it chelates the Ca2+ and Mg2+ ions essential for enzyme activity, potentially reducing the digestion capacity of DNase I.