Protein Expression Services
It pairs the efficiency and low cost of prokaryotic systems with eukaryotic modification: proteins fold correctly and carry yeast-type glycosylation, suiting soluble proteins, secreted antigens and multimeric proteins such as trimers.
A mature eukaryotic expression system combining moderate culture timelines, stable yields and correct folding with simple glycosylation — suited to secreted proteins, soluble antigens, multimeric proteins (including trimers), enzymes and selected antibody fragments.
The platform uses S. cerevisiae as the expression host in a mature, controllable process supporting either intracellular or secretory expression. Preparation routes for multimeric conformational antigens are available, backed by standardised purification and QC for consistent, qualified protein samples.
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Built on S. cerevisiae hosts, with strain and tag design plus induction and fermentation optimisation, supporting either intracellular or secretory expression.
It pairs the efficiency and low cost of prokaryotic systems with eukaryotic modification: proteins fold correctly and carry yeast-type glycosylation.
Rapid growth and strong fermentation scale-up give moderate timelines, stable yields and a clear cost advantage.
Suited to secreted proteins, soluble antigens, multimeric proteins (including trimers), enzymes and selected antibody fragments.
Eight stages, with a choice of S. cerevisiae strains and tag designs plus induction and fermentation optimisation; outputs and acceptance criteria are in the specifications below.
Codons optimised for the S. cerevisiae host and the gene synthesised
Cloned into a high-efficiency yeast expression vector, sequenced and prepared
Plasmid transformed into competent yeast for small-volume induction trials
Pilot-sample components are analyzed by SDS-PAGE and an expression verification report is delivered
Scale-up expression at 1–2 L
1–2 affinity steps to 85–90% purity at >1 mg/mL
Certificate of analysis (CoA) delivered
Purified protein shipped under cold chain throughout
Vector construction takes 1–2 weeks, pilot expression and verification 1–2 weeks, and scale-up fermentation and purification (1 L) 3–4 weeks — approximately 5–8 weeks in total.
Built on S. cerevisiae hosts, with strain and tag design plus induction and fermentation optimisation for either intracellular or secretory expression. It pairs prokaryotic efficiency and cost with eukaryotic modification — correct folding and yeast-type glycosylation. Preparation routes for multimeric conformational antigens are available, backed by standardised purification and QC for consistent, qualified samples.
Deliverables, acceptance criteria and timelines by experimental stage. The staging differs from the process above: the process shows how a project runs, while this table is the acceptance basis written into the contract.
| Stage | Scope | Deliverables | Standards | Timeline |
|---|---|---|---|---|
| Expression vector construction | Codon optimisation and gene synthesis, cloning into a high-efficiency expression vector, plasmid sequencing and preparation | Sequencing report (on request) and the recombinant expression plasmid | Sequence verified | 1-2 weeks |
| Pilot expression & verification | Shake-flask pilot expression using the recombinant strain, induction conditions optimised, small-scale purification and basic QC analysis | Expression verification report; expression plasmid or strain on request | / | 1-2 weeks |
| Scale-up fermentation & purification (1 L) | Scale-up fermentation (1 L and above) on the validated process, with large-scale purification and full QC analysis | Purified protein sample with certificate of analysis (CoA) | Protein yield 0.1–1 mg, purity 85–90%, concentration >1 mg/mL | 3-4 weeks |
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.
