抄録
We describe herein a new method for covalent labeling of proteins using a complementary recognition pair of peptide tag and synthetic molecular probe. The rapid and specific covalent labeling of a tag-fused protein was achieved by the reaction on the tag site with the probe through their selective molecular recognition. The advantages of this method involve the facile functional modification and the high labeling specificity of the tag-fused protein, which are demonstrated in the labeling experiments in various conditions even inside cells.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 15777-15779 |
| ページ数 | 3 |
| ジャーナル | Journal of the American Chemical Society |
| 巻 | 129 |
| 発行部数 | 51 |
| DOI | |
| 出版物ステータス | 出版済み - 12 26 2007 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry
これを引用
Non-enzymatic covalent protein labeling using a reactive tag. / Nonaka, Hiroshi; Tsukiji, Shinya; Ojida, Akio; Hamachi, Itaru.
：: Journal of the American Chemical Society, 巻 129, 番号 51, 26.12.2007, p. 15777-15779.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Non-enzymatic covalent protein labeling using a reactive tag
AU - Nonaka, Hiroshi
AU - Tsukiji, Shinya
AU - Ojida, Akio
AU - Hamachi, Itaru
PY - 2007/12/26
Y1 - 2007/12/26
N2 - We describe herein a new method for covalent labeling of proteins using a complementary recognition pair of peptide tag and synthetic molecular probe. The rapid and specific covalent labeling of a tag-fused protein was achieved by the reaction on the tag site with the probe through their selective molecular recognition. The advantages of this method involve the facile functional modification and the high labeling specificity of the tag-fused protein, which are demonstrated in the labeling experiments in various conditions even inside cells.
AB - We describe herein a new method for covalent labeling of proteins using a complementary recognition pair of peptide tag and synthetic molecular probe. The rapid and specific covalent labeling of a tag-fused protein was achieved by the reaction on the tag site with the probe through their selective molecular recognition. The advantages of this method involve the facile functional modification and the high labeling specificity of the tag-fused protein, which are demonstrated in the labeling experiments in various conditions even inside cells.
UR - http://www.scopus.com/inward/record.url?scp=37549061836&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=37549061836&partnerID=8YFLogxK
U2 - 10.1021/ja074176d
DO - 10.1021/ja074176d
M3 - Article
C2 - 18052248
AN - SCOPUS:37549061836
VL - 129
SP - 15777
EP - 15779
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 51
ER -