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Reconstituted by adding 0.5 mL sterile distilled water, spun down to remove insoluble particles, divided into small aliquots, frozen and stored at or below -20°C.
Cross-reactivities against enzymes of other sources may occur but have not been determined.
Prior to use, an aliquot is thawed slowly at ambient temperature, spun down again and used to prepare working dilutions by adding sterile phosphate buffered saline (PBS, pH 7.2). Repeated thawing and freezing should be avoided. Working dilutions should be stored at 4°C, not refrozen, and preferably used t he same day. If a slight precipitation occurs upon storage, this should be removed by centrifugation. It will not affect the performance of the product.
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.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: deoxyribonuclease; Deoxyribonuclease 1; Deoxyribonuclease I; Deoxyribonuclease-1; Deoxyribonuclease1; DeoxyribonucleaseI; DNASE 1; DNase I; DNase I lysosomal; DNL 1; FLJ38093
基因别名: DNASE1; DNL1
UniProt ID: (Bovine) P00639
Entrez Gene ID: (Bovine) 282217