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Rolf Wenderoth

Researcher at Leibniz Association

Publications -  10
Citations -  520

Rolf Wenderoth is an academic researcher from Leibniz Association. The author has contributed to research in topics: Recombinant DNA & Escherichia coli. The author has an hindex of 7, co-authored 10 publications receiving 515 citations. Previous affiliations of Rolf Wenderoth include Merck & Co..

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Journal ArticleDOI

Improved bivalent miniantibodies, with identical avidity as whole antibodies, produced by high cell density fermentation of Escherichia coli.

TL;DR: A high-cell density fermentation of E. coli producing these miniantibodies is reported and a work-up procedure suitable for large scale production is reported, without any need of subsequent chemical coupling in vitro.
Journal ArticleDOI

High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions.

TL;DR: Functional bivalent miniantibodies, directed against the epidermal growth factor receptor, accumulated to more than 3 gl−1 in high-cell-density cultures of Escherichia coli RV308(pHKK) on a pilot scale.
Patent

Process for the preparation of recombinant proteins in e.coli by high cell density fermentation

TL;DR: In this article, a fed-batch fermentation process using special E. coli host/vector systems for the purpose of efficiently forming recombinant proteins, in particular recombinant antibody molecules, preferably antibody fragments such as miniantibodies.
Journal ArticleDOI

An online monitoring system based on a synthetic sigma32-dependent tandem promoter for visualization of insoluble proteins in the cytoplasm of Escherichia coli.

TL;DR: Data of misfolding studies showed that the ibpfxs::lucA reporter unit provides an adequate tool for in vivo folding studies in E. coli from microtiter up to fermentation scales.
Journal ArticleDOI

A dual expression platform to optimize the soluble production of heterologous proteins in the periplasm of Escherichia coli.

TL;DR: A dual expression system, containing a degP-promoter-based reporter system and a highly versatile plasmid set, is developed that demonstrates that the amount of functional protein is inversely proportional to the on-line luciferase signal.