DNaseI Gene-free RNase that nonspecifically cleaves vaccine mRNA with 5-phosphorylated and 3-hydroxylated ends of DNA

DNaseI (RNase-free) is an endonuclease that cleaves DNA nonspecifically to release di-, tri-, and oligonucleotide products with 5'-phosphorylated and 3'-hydroxylated ends (1,2). DNase I acts on single- and double-stranded DNA, chromatin, and RNA:DNA hybrids. Its activity depends on calcium ions and can be activated by magnesium ions or divalent manganese ions. In the presence of magnesium ions, DNase I can randomly cleave double-stranded DNA at any site. In the presence of divalent manganese ions, DNase I can simultaneously cut double-stranded DNA and fragment DNA.

Carbomenu has a protein expression platform in prokaryotic cells (E.coil) and eukaryotic cells (Yeast/CHO-k1/293). Carbomenu is able to handle custom protein production orders at the kilogram scale. Carbomenu's product line can be optimized according to customer orders to meet individual needs.

information

feature

• DNA specific endonuclease

• Degrades double-stranded and single-stranded DNA

• Products are short oligonucleotides with 5'-phosphate and 3'-OH

application

• Prepare DNA from cell-free RNA.

• Removal of contaminating genomic DNA from RNA samples.

• Degradation of the DNA template in the transcription reaction after T7, T3, SP6 RNA polymerase catalyzed transcription in vitro.

• Footprint analysis for DNA-protein interactions.

• Used with DNA polymerase I for nick translation.

• In the presence of divalent manganese ions, DNA fragments can be fragmented to generate random DNA fragment pools.

• Partial genomic DNA clipping was used as a positive control for TUNEL detection of apoptosis.

storage

Store at -20°C.

heat inactivation

To inactivate DNaseI, add EDTA with a final concentration of 2.5mM and heat at 65°C for 10 minutes.

notes

1) Operate on ice and store at -20°C after use.

2) Enzyme activity can be inhibited by metal ion chelating agents, 0.1% SDS, DTT, mercaptoethanol, etc.

For Research Use Only.

refer to

1. IL-1β promotes the novel function of DNase I as a transcription factor of the Fas receptor gene. Dhivya Thiyagarajan1, Hege L. Pedersen1, Natalya Seredkina1, Kjersti D. Horvei1, Lorena Arranz, Ramon Sonneveld, Tom Nijenhuis, Johan van der Vlag, and Ole P. Rekvig1. Original research article. Front. Cell Developmental Biology, 6 February 2018.

2. Cisplatin nephrotoxicity is mediated by deoxyribonuclease I. Basnakian, AG, Apostolov, EO, Yin, X., Napirei, M., Mannherz, HG, and Shah, SV (2005). J. Am. society. Adrenaline. 16, 697–702.

3. How cations assist DNase I in DNA binding and hydrolysis. Mark Gairul, Daniel Picot, Josephine Abbey-Ghanem, Brigitte Hartman, Mark Barden. PLOS Computational Biology. November 18, 2010.