Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10753649 | Biochemical and Biophysical Research Communications | 2015 | 5 Pages |
Abstract
The redox states of proteins in cells are key factors in many cellular processes. To determine the redox status of cysteinyl thiol groups in proteins in vivo, we developed a new maleimide reagent, a photocleavable maleimide-conjugated single stranded DNA (DNA-PCMal). The DNA moiety of DNA-PCMal is easily removed by UV-irradiation, allowing DNA-PCMal to be used in Western blotting applications. Thereby the state of thiol groups in intracellular proteins can be directly evaluated. This new maleimide compound can provide information concerning redox proteins in vivo, which is important for our understanding of redox networks in the cell.
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Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Satoshi Hara, Yuki Tatenaka, Yuya Ohuchi, Toru Hisabori,