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Updated: Dec 18, 2025

High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
Published on: July 30, 2014
A Single Common Protocol for the Expression and Purification of Soluble Mammalian DSPs from Escherichia coli
Natalia Stepanyants1, Patrick J Macdonald1, Pooja Madan Mohan2
1Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH, USA.
Abstract:
Mammalian DSPs have been historically isolated either from native tissue sources or from transfected insect cell cultures via time-consuming and cumbersome protocols often yielding protein of variable quality and quantity. A facile and highly reproducible alternative methodology involving the heterologous expression and purification of soluble mammalian DSPs from E. coli, which yields highly active and functional protein of a uniform quality and quantity, free of spurious posttranslational modifications inherent to mammalian and insect cell expression systems, is described in this chapter.

