ArticleBiochemistry and biophysics reports2020
RIEDL tag: A novel pentapeptide tagging system for transmembrane protein purification.
Article in Biochemistry and biophysics reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 23 citations in OpenAlex.
- A novel epitope tag from rabies virus has versatile in vitro applications.Applied microbiology and biotechnology · 2023Article
- Defucosylated mouse‑dog chimeric anti‑HER2 monoclonal antibody exerts antitumor activities in mouse xenograft models of canine tumors.Oncology reports · 2022Article
- Isolation and characterization of human anti-CD20 single-chain variable fragment (scFv) from a Naive human scFv library.Medical oncology (Northwood, London, England) · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Affinity tag systems are an essential tool in biochemistry, biophysics, and molecular biology. Although several different tag systems have been developed, the epitope tag system, composed of a polypeptide "tag" and an anti-tag antibody, is especially useful for protein purification. However, almost all tag sequences, such as the FLAG tag, are added to the N- or C-termini of target proteins, as tags inserted in loops tend to disrupt the functional structure of multi-pass transmembrane proteins. In this study, we developed a novel "RIEDL tag system," which is composed of a peptide with only five amino acids (RIEDL) and an anti-RIEDL monoclonal antibody (mAb), LpMab-7. To investigate whether the RIEDL tag system is applicable for protein purification, we conducted the purification of two kinds of RIEDL-tagged proteins using affinity column chromatography: whale podoplanin (wPDPN) with an N-terminal RIEDL tag (RIEDL-wPDPN) and human CD20 with an internal RIEDL tag insertion (CD20-
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