DNASE1 polyclonal antibody

Internucleosomal DNA fragmentation following the activation of endonucleases is the common end point of apoptosis. DNase I, a Ca2+/Mg2+-dependent endonuclease ubiquitously expressed in mammalian tissues, has been implicated to mediate internucleosomal DNA degradation in human cells undergoing apoptosis. DNase I is highly polymorphic, and at least six alleles of DNase I are known. DNase II, the ubiquitously expressed acidic deoxyribonuclease, acts downstream of caspase activation and may also induce DNA digestion during apoptosis. DNase I cleaves DNA to 5'-phosphodinucleotide and 5'-phospho- oligonucleotide end-products, whereas DNase II cleaves DNA to 3'-phosphomononucleotide and 3'-phosphooligonucleotide end-products. The mechanism by which DNase II cuts DNA is similar to DNase I, which produces nicks rather than double-strand cuts. DNase II is usually present in cytoplasm of epithelial cells, but it appears concentrated in the nuclei of lens fibers. In contrast, DNase I is always concentrated in nuclei of epithelial and fiber cells.