Protein expression underpins both antigen preparation and antibody production: five platforms — mammalian, baculovirus–insect, yeast, E. coli and cell-free — plus stable cell line development and multi-pass transmembrane expertise, matched to each protein's properties and handling 1,000+ projects every month.
We specialise in transmembrane protein expression and purification for target research and drug discovery. As key integral membrane proteins they make up 70–80% of all membrane proteins; combining hydrophilic and hydrophobic regions and embedded in the lipid bilayer through their transmembrane domains, they drive transport, signalling and energy metabolism — and are the targets of more than 60% of known drugs.
They depend on the membrane environment to hold their structure and function, and with many passes and large hydrophobic regions they are extremely hard to express — obtaining structurally intact, stably active protein remains the central challenge of in vitro preparation.
Drawing on E. coli, mammalian and baculovirus–insect systems, we markedly improve soluble expression and correct folding — GLUT1, GLYT1, ActRIIB, ActRIIA, SREBP2, ABCG1 and TET8 among the difficult targets already delivered — in one workflow from gene construction to high-quality protein.
Five expression systems cover everything from non-glycosylated proteins to complex eukaryotic targets; the platform is matched to your protein's properties, modification needs and yield targets before kick-off.
Mammalian expression platformCHO/HEK293 hosts with full folding and post-translational modification give proteins that closely match the native state in structure, physicochemistry and function.
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Baculovirus–insect cell platformInsect cell hosts with baculovirus-mediated expression bring eukaryotic post-translational modification, enabling high-level production of complex proteins and multi-subunit assemblies.
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Yeast expression platformA eukaryotic expression system using yeast as the host, with rapid growth and strong fermentation scale-up capability. It accommodates diverse protein types, including nanobodies and antibody fragments, without mammalian-type glycosylation.
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E. coli expression platformA streamlined prokaryotic system combining short timelines, controlled cost and high yield, supporting rapid scale-up of the target protein.
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Cell-free expression platformAn open in vitro system on cell lysate: synthesis is fast, special requirements like toxic proteins are manageable, and unnatural amino acids can be incorporated with flexible control.
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Mesothelin, long underestimated, has moved from the lab to the clinical frontier across CAR-T, ADCs and bispecifics. With our cellular EC50 and internalisation data.
May 27, 2026
Both formats drop parts of the native immunoglobulin. We compare structure, solubility, stability, size and production cost, then their therapeutic use.
Jul 15, 2026
Heavy-chain-only antibodies, found in camelids and cartilaginous fish in the 1990s, lose the CH1 domain and pair no light chain — leaving a single variable domain of roughly 15 kDa, nanometre-scale.
Jun 10, 2026
The five platforms are not a menu but a toolbox matched to each protein. Before kick-off we assess the sequence and structural features, recommend a system plus fallback routes, and lay out timelines and risks up front.
Share the intended application and what you already have in hand. A scientist — not a sales rep — will scope feasibility, suggest the right route and send a quote, usually within one business day.
