Recombinant Human DNASE1 protein

**Background of Recomcombinant DNASE1 Protein**

Deoxyribonuclease I (DNASE1), also known as bovine pancreatic DNase, is a glycoprotein endonuclease that cleaves double-stranded DNA into oligonucleotides by hydrolyzing phosphodiester bonds. Naturally produced in vertebrates, DNASE1 plays a critical role in degrading extracellular DNA during apoptosis, preventing autoimmunity triggered by self-DNA accumulation. Its ability to digest chromatin and extracellular DNA also makes it essential in maintaining tissue homeostasis and reducing inflammation.

Recombinant DNASE1 is engineered using genetic cloning techniques, where the human *DNASE1* gene is expressed in host systems like *E. coli*, yeast, or mammalian cell lines. This recombinant form retains the enzymatic activity of native DNASE1 but offers advantages such as high purity, scalability, and reduced immunogenicity. It is widely utilized in biomedical research, including studies on chromatin remodeling, cell death mechanisms, and neutrophil extracellular trap (NET) degradation.

Therapeutically, recombinant DNASE1 (e.g., dornase alfa) is FDA-approved for treating cystic fibrosis (CF). In CF patients, viscous mucus in airways contains high levels of DNA released by neutrophils, contributing to respiratory obstruction. DNASE1 inhalation therapy hydrolyzes this DNA, reducing mucus viscosity and improving lung function. Beyond CF, its potential applications extend to chronic obstructive pulmonary disease (COPD), systemic lupus erythematosus (SLE), and other conditions involving pathogenic DNA accumulation.

Structurally, recombinant DNASE1 typically includes a signal peptide for secretion and may undergo post-translational modifications (e.g., glycosylation) depending on the expression system. Researchers continue to explore engineered variants with enhanced stability or targeting capabilities, underscoring its versatility as both a therapeutic agent and a molecular biology tool.