Strategies for Improving Soluble Protein Production in E. coli
6.5 هزار بار بازدید -
8 سال پیش
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E. coli is a cell-factory
E. coli is a cell-factory for producing large quantities of recombinant protein for basic research studies, industrial bioprocesses, drug discovery, and therapeutics. Although a variety of heterologous proteins from viral to human origin have been successfully overproduced in bacterial systems, each new gene sequence and encoded protein can present well-known expression challenges including low expression levels, protein misfolding, and E. coli cellular toxicity. In this webinar you’ll learn the cellular mechanisms that lead to these impediments and expression strategies for overcoming them. We will introduce enhanced E. coli expression systems with optimized vector properties and unique promoters for tunable induction control and high-level expression. Additionally, we will discuss novel fusion tags that enhance protein expression and solubility, and a 5-second, enzyme-free cloning system that facilitates parallel processing and high-throughput expression screening. You’ll also pick up helpful bench tips for generating soluble and active protein ready for different downstream applications.
Key Learning Objectives
Explore the root causes of common protein expression failures in E.coli.
Learn how stringent growth conditions combined with tunable promoters and novel fusion tags improve protein expression and solubility.
Discover ways to streamline your protein expression screening workflow with a flexible, enzyme-free cloning system.
Key Learning Objectives
Explore the root causes of common protein expression failures in E.coli.
Learn how stringent growth conditions combined with tunable promoters and novel fusion tags improve protein expression and solubility.
Discover ways to streamline your protein expression screening workflow with a flexible, enzyme-free cloning system.
8 سال پیش
در تاریخ 1395/06/26 منتشر شده
است.
6,524
بـار بازدید شده