ArticleResearch in pharmaceutical sciences2026
Development of a recombinant biosimilar single-chain variable fragment antibody targeting human estrogen receptor α36.
Article in Research in pharmaceutical sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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8 authors.
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Abstract
Background and purpose: The estrogen receptor alpha-36 (ER-α36) is an alternative splice variant of classical ER-α66 and is abundantly present in both ER-α66-positive and ER-α66-negative breast tumor cells. Given its clinical relevance, developing targeted strategies against this isoform is of particular significance to breast cancer research. This study aimed to develop an ER-α36-specific recombinant biosimilar single-chain variable fragment (scFv) antibody. Experimental approach: The primary amino acid sequence of the anti-ER-α36 scFv was retrieved from patent Findings/Results: Characterization using sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blotting experiments revealed a molecular weight of 29 kDa for the expressed scFv antibody. Relative quantification revealed the highest scFv protein expression level 16 h after induction with 1 mM isopropyl β-D-1-thiogalactopyranoside at 25 °C. Flow cytometry and ELISA assays demonstrated specific binding of the scFv to ER-α36 protein on MDA-MB-231 breast cancer cells, while no interaction was detected with ER-α36-negative MCF-10A normal mammary epithelial cell line. Conclusion/implications: The anti-ER-α36 scFv antibody fragment was successfully expressed using the
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