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An anti-peptide monoclonal antibody recognizing the tobacco etch virus protease-cleavage sequence and its application to a tandem tagging system.

Abstract：

:Peptide-based affinity tags are commonly used in recombinant production/purification of proteins, and are often preceded or followed by a protease recognition sequence to allow tag removal. We describe a rat monoclonal antibody 2H5 recognizing an undecapeptide tag called "eTev", which contains a recognition sequence for Tobacco Etch Virus (TEV) protease. In the crystal structure of 2H5-eTev complex, the long eTev peptide assumes compact α-helical conformation in the binding groove, exposing both ends to the solution. This architecture allowed us to connect eTev with another peptide tag called PA tag via linker sequence, ensuring the simultaneous access of two anti-tag antibodies. When this tandem double tag was attached at one end of various proteins, it enabled highly sensitive and protein-independent detection by sandwich ELISA. Utilizing this system during a rapid cell line screening, we succeeded in isolating stable cell clones expressing high level of mouse Wise protein.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Tabata S,Kitago Y,Fujii Y,Mihara E,Tamura-Kawakami K,Norioka N,Takahashi K,Kaneko MK,Kato Y,Takagi J

doi

10.1016/j.pep.2018.03.004

subject

Has Abstract

pub_date

2018-07-01 00:00:00

pages

94-99

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(18)30143-8

journal_volume

147

pub_type

杂志文章

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