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Novel short peptide tag from a bacterial toxin for versatile applications
- Novel short peptide tag from a bacterial toxin for versatile applications
- Lee, Tae Hee; Kim, Kwang Soo; Kim, Jin Hee; Jeong, Jae-Ho; Woo, Hye Ryun; Park, So Ra; Sohn, Myung-Ho; Lee, Hyeon Ju; Rhee, Joon Haeng; Cha, Sun-Shin; Hwang, Joo-Hee; Chung, Kyung Min
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- JOURNAL OF IMMUNOLOGICAL METHODS
- JOURNAL OF IMMUNOLOGICAL METHODS vol. 479
- Epitope tag; Monoclonal antibody; Immunodetection; Affinity purification
- SCIE; SCOPUS
- Document Type
- The specific recognition between a monoclonal antibody (mAb) and its epitope can be used in a tag system that has proved valuable in a wide range of biological applications. Herein, we describe a novel tag called RA-tag that is composed of a seven amino acid sequence (DIDLSRI) and recognized by a highly specific mAb, 47RA, against the bacterial toxin Vibrio vulnificus RtxA1/MARTX(Vv). By using recombinant proteins with the RA-tag at the N-terminal, C-terminal, or an internal site, we demonstrated that the tag system could be an excellent biological system for both protein purification and protein detection in enzyme-linked immunosorbent, Western blot, flow cytometry, and immunofluorescence staining analyses in Escherichia coll., mammalian cell lines, yeast, and plant. In addition, our RA-tag/47RA mAb combination showed high sensitivity and reliable affinity (K-D = 5.90 x 10(-8) M) when compared with conventional tags. Overall, our results suggest that the RA-tag system could facilitate the development of a broadly applicable tag system for biological research.
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