As an expert in enzyme assays, Creative Enzymes shares our advanced techniques with you. We offer the most comprehensive and the latest optimized version of activity testing for hydrolases. The results for micrococcal nuclease are guaranteed with high accuracy and reproducibility.

Micrococcal nuclease (nuclease T, EC 3.1.31.1) can act on both double-stranded or single-stranded substrates. More specifically, its endonucleolytic activity allows it to cleave the double-stranded DNA or RNA and single-stranded nucleic acid to nucleoside 3'-phosphates and 3'-phosphooligonucleotide. The rate of cleavage is 30 times greater at the 5’ side of A or T than at G or C. Through the hydrolysis of the enzyme, all sequences will be ultimately cleaved. The enzyme activity strictly depends on Ca²⁺, and its activity is easily inactivated by EGTA.

Among various sources, Staphylococcal micrococcal nuclease is used as a model protein to study protein folding and enzymatic catalysis. The structure of Staphylococcal nuclease T has been fully identified. It contains only 149 residues, carries no disulfide bonds or free sulfhydryl groups, and can be unfolded and refolded reversibly. Many applications have been developed on this enzyme. For example, the enzyme is a useful tool for mapping chromatin structure in eukaryotes, and for determining the positions of nucleosomes within a region of DNA to identify dynamic changes induced during gene regulation. In molecular biology, the purified enzyme can be used as an exogenous reagent to clear cellular extracts and facilitate protein purification. In clinical treatment, this enzyme is an attractive and potential target for the development of anti-malarial drugs. Owing to the significances in research and therapy, a large number of variants have been constructed to expand the biochemical and biophysical data. To facilitate such effort, Creative Enzymes provides high-quality assay services for micrococcal nuclease.

Figure: The crystal structure of the ternary complex of Staphylococcal micrococcal nuclease, Ca²⁺, and the inhibitor deoxythymidine 3',5'-bisphosphate (pdTp).
Reference: Loll, P.J. et al. Proteins 1989 5: 183-201.

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