High enzyme cutting efficiency, no RNase residue, suitable for multiple scenarios.
While frequently used in the laboratory, removing contaminating DNA in RNA samples without affecting the accuracy of RNA quantification is still a challenge to many researchers. DNase I (deoxyribonuclease I), as the gold standard for solving this problem, plays a key role in RNA research due to its unique double-stranded/single-stranded DNA digestion ability.
Digestion Conditions | How DNase I works
DNase I is a non-specific endonuclease that can digest single-stranded or double-stranded DNA. It can hydrolyze phosphodiester bonds to produce monodeoxynucleotides and oligodeoxynucleotides containing 5'-phosphate groups and 3'-OH groups. The optimal working pH range of DNase I is 7-8. Its activity depends on Ca2+ and can be activated by divalent metal ions such as Mn2+, Mg2+, and Zn2+.
- In the presence of Mg2+, DNase I randomly cuts any site of double-stranded DNA;
- In the presence of Mn2+, DNase I can cut the DNA double strand at the same site to form a blunt end or a sticky end with 1-2 nucleotides protruding.

Figure 1. Schematic diagram of the cleavage of dsDNA by DNase I in the presence of Mg2+ and Mn2+
Traditional DNase I technology is facing a difficult dilemma: the bovine pancreas extraction method has a complex raw material source and prominent RNase residue problem. The purification process is not only cumbersome, but also difficult to ensure product uniformity; the E. coli expression system is subject to the biosynthesis mechanism and faces the problem of production ceiling.
Recombinant DNase I (RNase-free, Yeast) (Cat#14549/14550)
YeasenBio directly hits the pain points of the industry and launches yeast expression Recombinant DNase I (RNase-free, Yeast) (Cat#14549/14550), relying on the unique advantages of the eukaryotic expression system to achieve two core technology breakthroughs:
- Productivity breakthrough: Using eukaryotic secretion expression technology to effectively avoid the accumulation of intracellular toxins, while combining high-density fermentation technology to improve production capacity in multiple ways to meet large-scale production needs;
- Performance upgrade: Thanks to the natural glycosylation modification of the yeast system, the enzyme is given a more stable spatial structure, and it can still efficiently digest DNA even in a complex sample environment.
Key Product Advantages
- Super strong digestive activity
1 μg of plasmid DNA was digested with different amounts of DNase I from Yeasen and other brands Supplier A. The results showed that the plasmid DNA removal efficiency of Yeasen 14549ES was comparable to that of Supplier A.

Figure 2 Verification of plasmid DNA removal effect
- No RNase residue
10 U of YeasenBio's Recombinant DNase I (RNase-free, Yeast) (Cat#14549) was incubated with the RNA substrate at 37°C for 1 hour. Agarose gel electrophoresis analysis showed that no residual RNase activity was detected in the three batches of the enzyme preparation, completely eliminating the risk of RNA sample degradation and providing reliable protection for RNA analysis scenarios with extremely high purity requirements.

Figure 3 RNase residue results verification
- RNA extraction application verification
To evaluate the application effect of YeasenBio's Recombinant DNase I (RNase-free, Yeast) (Cat#14549) in RNA extraction, 20 U of the enzyme preparation was used to treat 12 mouse liver pre-treatment samples from different sources. Subsequent RNA extraction and agarose gel electrophoresis analysis confirmed that the RNA integrity of the enzyme-treated group was good, indicating that this DNase I effectively digests DNA without affecting the quality of RNA, and fully meets the technical requirements of RNA extraction experiments.

Figure 4 RNA extraction application verification
DNase I Selection Guide
To meet different application requirements, YeasenBio can provide DNase I from three sources: bovine pancreas extraction, large intestine recombinant expression, and yeast recombinant expression, and can also provide GMP grade DNase I.
Description |
Catalog No. |
Application |
Extracted from bovine pancreas, prepared by chromatography, with extremely low RNase A activity. Available as freeze-dried powder. |
1. Remove gDNA when extracting RNA from samples. (If it is a trace sample, recombinant DNase I is required). 2. Protein research: Remove DNA from protein preparations. |
|
Extracted from bovine pancreas, prepared by chromatography, with extremely low RNase A activity (≤0.0005%). Available as freeze-dried powder. |
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DNase I (RNase-free) expressed in E. coli, recombinant expressed in E. coli, RNase-free, liquid form. |
Suitable for various applications:
|
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DNase I (RNase-free) expressed in Pichia pastoris, RNase-free, in liquid form. |
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14550ES |
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DNase I (RNase-free) expressed in E. coli, GMP-grade, available in liquid form. |
GMP pharmaceutical grade. Used in production with pharmaceutical raw materials and excipients. GMP-compliant product production and quality management procedures ensure that the production process and all raw materials are traceable. |
References
1、Ndiaye C, Mena M, Alemany L, et al. HPV DNA, E6/E7 mRNA, and p16INK4a detection in head and neck cancers: a systematic review and meta-analysis[J]. The Lancet Oncology, 2014, 15(12): 1319-1331.
2、Broccolo F, Fusetti L, Rosini S, et al. Comparison of oncogenic HPV type‐specific viral DNA load and E6/E7 mRNA detection in cervical samples: results from a multicenter study[J]. Journal of medical virology, 2013, 85(3): 472-482.
3、Huang Z, Fasco M J, Kaminsky L S. Optimization of Dnase I removal of contaminating DNA from RNA for use in quantitative RNA-PCR[J]. Biotechniques, 1996, 20(6): 1012-1020.
4、Kang D D, Li H, Dong Y. Advancements of in vitro transcribed mRNA (IVT mRNA) to enable translation into the clinics[J]. Advanced Drug Delivery Reviews, 2023, 199: 114961.
5、Wiame I, Remy S, Swennen R, et al. Irreversible heat inactivation of DNase I without RNA degradation[J]. Biotechniques, 2000, 29(2): 252-256.
6、Adolph S, Hameister H. In situ nick translation of metaphase chromosomes with biotin-labeled d-UTP[J]. Human genetics, 1985, 69: 117-121.
7、Song C, Zhang S, Huang H. Choosing a suitable method for the identification of replication origins in microbial genomes. Front Microbiol, 2015, 6: 1049.