Construction, expression and functional characterization of an engineered antibody against tumor antigen MUC-1C

Mona Pourjafar, Michaela Miehe, Rezvan Najafi, Meysam Soleimani*, Edzard Spillner

*Corresponding author af dette arbejde

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Abstract

Minibodies (single-chain Fv-CH3) are fusion proteins of a single-chain variable fragment (scFv) to the human IgG1 CH3 domain. They exhibit superior properties as compared to whole antibodies due to their smaller size and less complex composition, and also as compared to scFvs due to the two antigen-binding domains, for immunotherapy and imaging of various carcinomas including breast cancer. In the current study, efficient production of the recombinant anti-MUC-1 minibody for its dominant format (VH-VL) was obtained in the periplasmic space of the Escherichia coli BL21 (DE3) expression system. The active recombinant protein was successfully purified from soluble fraction. Functional assays presented the in vitro targeting properties and specificity of the expressed anti-MUC-1 HL minibody in the MUC-1 positive cell lines compared to normal cell.

OriginalsprogEngelsk
Artikelnummer106148
TidsskriftProtein Expression and Purification
Vol/bind199
ISSN1046-5928
DOI
StatusUdgivet - nov. 2022

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