Protein Sciences

A: The choice between a mammalian or E. coli expression system for producing fusion proteins hinges on several factors, including the fusion protein’s unique characteristics, its intended use, and the required post-translational modifications. If the fusion protein requires advanced post-translational modifications, precise folding, and is intended for therapeutic purposes, a mammalian system is the preferred choice. In contrast, for research purposes where these considerations are less crucial, E. coli may offer a faster and more cost-effective alternative. Conducting preliminary experiments in both systems can help determine the most suitable expression system for a specific fusion protein.

A: In the initial phases of developing a therapeutic protein, it’s important to pay careful attention to several critical factors. These factors include: assessing protein expression and stability, evaluating protein solubility and proper folding, ensuring optimal protein bioactivity and functionality, addressing potential immunogenicity concerns, assessing suitability for scale-up and manufacturing, planning for formulation and delivery methods, and prioritizing safety. By integrating these considerations into the early stages of therapeutic protein development, you establish a strong foundation for later phases of pre-clinical and clinical development.

A: We typically use buffers like HEPES buffer with 150 mM NaCl at neutral pH. This approach ensures a stable environment for a wide range of proteins, without extensive efforts in buffer optimization.