Summary
High-quality, high-yield protein production is a fundamental requirement for structural biology, functional analysis, and drug discovery research. Although significant progress in expression and purification technologies has enabled the handling of a wide variety of biomolecules, sample preparation―including expression optimization, solubilization, and stabilization―has long been a critical factor determining research success. This remains a major challenge, particularly for membrane proteins, large macromolecular complexes, and targets containing intrinsically disordered regions.
Protein Production Support Unit provides multiple expression platforms, including an E. coli cell-free synthesis system, expression system in E. coli, yeast, insect cells, and mammalian cells. We systematically evaluate and select the most suitable system according to the biochemical and biophysical properties of each target protein. From the design of purification strategies utilizing fast liquid chromatography systems to quality assessment and seamless integration into functional and structural analyses, our research scientists and technical staffs provide comprehensive, end-to-end support.
Protein Production Support Unit provides multiple expression platforms, including an E. coli cell-free synthesis system, expression system in E. coli, yeast, insect cells, and mammalian cells. We systematically evaluate and select the most suitable system according to the biochemical and biophysical properties of each target protein. From the design of purification strategies utilizing fast liquid chromatography systems to quality assessment and seamless integration into functional and structural analyses, our research scientists and technical staffs provide comprehensive, end-to-end support.
Mikako Shirouzu Ph.D.
Activity
- We maintain an extensive collection of expression vectors and expression cell strains, enabling systematic evaluation across multiple expression platforms./li>
- - E. coli-based cell-free expression systems: Applicable not only to soluble proteins but also to membrane proteins, secreted proteins,
- and antibody fragments. Site-specific incorporation of nonnatural amino acids is also available.
- - Expression screening in diverse E. coli strains and under varied culture conditions to optimize yield and solubility
- - Baculovirus-mediated protein expression in insect cells
- - Protein expression in mammalian suspension cell cultures
- - Purification of recombinant proteins using a broad range of chromatographic techniques
- - Biophysical characterization of proteins and macromolecular complexes, including analyses of stability, assembly state,
- and interactions with diverse molecular partners
Resources and Facilitie
(mammalian cells)
AKTA system for purification
Cell culture equipment (insect cells)
Facility for protein purification
Support for external users
・Research support is provided through the BINDS program.
https://www.binds.jp/supports/A13-1