|? Over 10 years' experience for 6000+ recombinant proteins production.
? One-stop service from gene to protein.
? Multiple protein expression systems: bacterial, yeast, baculovirus-insect and mammalian expression system.
? Multiple purification systems (30+) to choose.
? Abundant R & D ability with over 1000 new proteins per year and quick troubleshooting.
? Close to 100 bioreactors with various volumes ranging from 2 to 1000 L to meet high-throughput and large-scale production.
NOTE: This video displays in Chinese.
|E.coli protein expression service||? Over 10 years' experience of protein expression|
|? Multiple protein purification and refolding technologies|
|? High-throughput and large-scale protein expression and production|
|? One-stop service from gene to purified protein|
|? Multiple expression vectors and E.coli cells to meet various expression needs|
|Mammalian transient protein expression service||? High-efficiency expression vectors|
|? Optimized mammalian expression systems|
|? High-throughput and large-scale production|
|? High yield expression with post-translational modification and correct folding|
|? One-stop service from gene sequence to purified protein|
|Baculovirus-Insect Cell Protein Expression Service||? High-efficiency expression of intracellular and extracellular proteins|
|? Multiple insect cells: Sf9，Sf21，Hi-5|
|? High-throughput and large-scale protein production|
|? Optimized expression vectors and higher-titre virus packaging|
|Advantages||? low cost
? rapid expression
? easy scale-up
? most widely used system for recombinant protein production
|? low cost
? rapid expression
? high yield
? diverse post-translational modifications
|? high capacity genes
? soluble proteins
? suitable for toxic proteins
? post-translational modifications similar to mammalian systems
|? soluble protein
? lower endotoxin
? better bioactivity
? comprehensive post-translational modifications
? transient & stable expression
|Challenges||? inclusion bodies
? lack of eukaryotic post-translational modifications
? difficult to express higher MW proteins
|? improper glycosylation
? high mannose modification
|? more demanding culture conditions
? lack of partial glycosylation
|? more demanding culture conditions|
|Most common applications||? bacterial proteins
? antigen proteins
? lower MW proteins
|? cytoplasmic proteins
? toxic proteins
? transmembrane proteins
? secretory proteins
|? secretory proteins
? extracellular domain of transmembrane proteins
? recombinant antibodies
? antibody fragments