Core Viewpoint - The article emphasizes the importance of selecting the appropriate expression host for recombinant protein production, as it significantly impacts yield, post-translational modifications, and functional activity [1]. Group 1: Expression Systems Overview - Recombinant proteins are widely used in life sciences, biopharmaceuticals, vaccine development, and in vitro diagnostics [1]. - Current mainstream expression systems include E. coli, mammalian cells, yeast, and insect cells, each with its own advantages and limitations [1]. - E. coli is favored for its rapid growth, low cost, and high yield, but lacks a complete post-translational modification system and faces challenges with inclusion body refolding [1]. - Mammalian cells (e.g., CHO, HEK293) produce proteins closer to their natural state, essential for therapeutic protein production, but have lower yields and more complex operations [1]. - Yeast and insect cells offer unique advantages in cost control, large-scale production, and complex protein folding, but their post-translational modifications differ from those in mammals [1]. Group 2: Expression Host Selection Strategy - The selection of an expression host should be based on a multidimensional evaluation system considering the target protein's research background, physicochemical properties, biological functions, and downstream applications [1][2]. - The upcoming lecture will focus on strategies for selecting protein expression systems, analyzing the characteristics and application scenarios of various commonly used systems, and discussing real-world cases [2][7]. Group 3: Speaker and Event Details - The lecture will be presented by Dr. Yulu Lu, a senior R&D manager at Beijing Yiqiao Shenzhou Technology Co., Ltd., who has extensive experience in evaluating, designing, and optimizing CRO projects in recombinant protein expression and purification [4][5][6]. - The event is scheduled for May 15 at 19:00, and will address common issues in protein expression and share practical experiences for obtaining high-quality recombinant proteins [3][7].