AtaGenix Laboratories
AtaGenix Laboratories
AtaGenix offers yeast recombinant protein expression using Pichia pastoris and Saccharomyces cerevisiae systems. Yeast combines eukaryotic processing (glycosylation, disulfide bonds, proper folding) with the ease of microbial culture — enabling high-density fermentation and efficient secreted expression at a fraction of mammalian cell costs.
The Pichia system is particularly well-suited for secreted proteins, as the host secretes very few native proteins — simplifying downstream purification and reducing processing time. Multiple strains of both P. pastoris and S. cerevisiae are available to maximize yield, solubility, and biological activity for your specific target.
Our integrated gene-to-protein service covers codon optimization, vector construction, clone screening, fermentation scale-up, chromatography purification, and comprehensive QC. For targets requiring mammalian-type complex glycosylation, explore our Mammalian Expression Services. For non-glycosylated targets where speed is the priority, consider E. coli Expression.
AtaGenix provides multiple strains of Pichia pastoris and Saccharomyces cerevisiae with both methanol-induced (AOX1) and constitutive (GAP) promoter options. Yeast expression delivers eukaryotic post-translational modifications at microbial speed and cost — ideal for secreted proteins, industrial enzymes, and targets where mammalian-level glycosylation is not required.
Service Scope
| ✓ Gene synthesis & codon optimization for yeast | ✓ Yeast expression vector construction |
| ✓ Pichia pastoris & S. cerevisiae hosts | ✓ AOX1 (methanol-induced) & GAP (constitutive) promoters |
| ✓ Secreted & intracellular expression | ✓ Clone screening & expression optimization |
| ✓ Flask to fermenter scale-up | ✓ Chromatography-based purification |
| ✓ Full QC: SDS-PAGE, Western Blot, SEC, HPLC, endotoxin testing | |
Yeast expression is the best choice when your protein needs eukaryotic folding and simple glycosylation, but mammalian-level costs and timelines are not justified. The Pichia secretion system is especially efficient because the host secretes very few native proteins, making purification straightforward.
| Target Type | Why Yeast |
| Secreted proteins | Low host protein background simplifies purification — fewer contaminants, fewer steps |
| Industrial enzymes | High-density fermentation enables gram-level production at low cost |
| Glycoproteins (simple glycans) | Eukaryotic glycosylation and disulfide bond formation without mammalian cost |
| Food-grade & diagnostic proteins | GRAS-status organism (S. cerevisiae) suitable for regulatory-friendly applications |
Pichia
Primary Host
Secreted
Expression Mode
g/L
Yield Potential
Scalable
Flask to Fermenter
Every yeast expression project follows a 4-step pipeline from gene design through fermentation to purified protein. Clone screening is the critical optimization step — identifying top-expressing clones before committing to scale-up.
01
Gene & Vector
Optional
Codon optimization
Gene synthesis
Yeast vector subcloning
02
Pilot Expression
4–5 weeks
Transformation & clone screening
Expression optimization
Pilot purification test
03
Scale-up & Purify
~2 weeks
Fermentation under optimized conditions
Chromatography purification
Concentration & buffer exchange
04
QC & Delivery
Included
SDS-PAGE, WB, SEC
HPLC, endotoxin
Detailed QC report
Step 1 — Gene & Vector (optional): Codon optimization for yeast expression, gene synthesis, and subcloning into a yeast expression vector with appropriate signal peptide for secretion. Skipped if client provides a ready-to-use construct.
Step 2 — Pilot Expression (4–5 weeks): Transformation into Pichia or S. cerevisiae strains, clone screening by SDS-PAGE and Western Blot to identify top expressers, and expression optimization (induction conditions, temperature, time). Pilot purification confirms feasibility before scale-up.
Step 3 — Scale-up & Purification (~2 weeks): Large-scale fermentation under optimized conditions (flask or bioreactor). Chromatography-based purification workflow tailored to your protein. Concentration and buffer exchange to your specifications.
Step 4 — QC & Delivery: Comprehensive quality control including SDS-PAGE, Western Blot, analytical SEC, HPLC, and endotoxin testing. Protein delivered with a detailed QC report including purity, concentration, and identity confirmation.
Yeast sits between E. coli and insect cells in terms of capability and cost. It offers eukaryotic folding and simple glycosylation with microbial speed and scalability. Choose yeast when your protein needs more than E. coli can provide, but mammalian or insect cell costs are not justified.
| Feature | E. coli | Yeast | Insect | Mammalian |
|---|---|---|---|---|
| Glycosylation | None | High-mannose | Paucimannose | Complex / human |
| Secretion | Limited | Excellent | Good | Good |
| Scalability | High | Very high | Moderate | Moderate |
| Relative Cost | $ | $–$$ | $$ | $$$ |
Pichia pastoris is the preferred choice for secreted protein production — it grows to very high cell densities and secretes very few native proteins, making purification straightforward. Saccharomyces cerevisiae is a GRAS (Generally Recognized As Safe) organism with well-established genetics, making it suitable for food-grade and regulatory-friendly applications. AtaGenix offers both and will recommend the best host for your specific target.
The pilot expression phase (transformation, clone screening, optimization) takes approximately 4 to 5 weeks. Scale-up expression and purification adds approximately 2 weeks. If gene synthesis and vector construction are needed, add additional time at the start of the project.
Choose yeast when your protein needs eukaryotic folding, disulfide bonds, or simple glycosylation, but insect cell or mammalian costs are not justified. Yeast is especially strong for secreted proteins (simplified purification), industrial enzymes (high-density fermentation at low cost), and GRAS-requirement applications. For non-glycosylated targets, E. coli is faster and cheaper. For complex or human-type glycosylation, choose insect cell or mammalian.
Every project includes SDS-PAGE (purity), Western Blot (identity), analytical SEC (aggregation), HPLC, and endotoxin testing. A detailed QC report is delivered with your purified protein. Additional characterization such as mass spectrometry, activity assays, and stability testing are available upon request.
Yeast glycosylation produces high-mannose type glycans which differ from mammalian complex glycans. Timelines and yields are target-dependent. Note: AtaGenix technical handbook does not include a dedicated yeast expression page — specific strains, timelines, and capabilities should be confirmed with the project team before publishing. Quote-based pricing.
Step 1 — Gene & Vector (optional): Codon optimization for yeast expression, gene synthesis, and subcloning into a yeast expression vector with appropriate signal peptide for secretion. Skipped if client provides a ready-to-use construct.
Step 2 — Pilot Expression (4–5 weeks): Transformation into Pichia or S. cerevisiae strains, clone screening by SDS-PAGE and Western Blot to identify top expressers, and expression optimization (induction conditions, temperature, time). Pilot purification confirms feasibility before scale-up.
Step 3 — Scale-up & Purification (~2 weeks): Large-scale fermentation under optimized conditions (flask or bioreactor). Chromatography-based purification workflow tailored to your protein. Concentration and buffer exchange to your specifications.
Step 4 — QC & Delivery: Comprehensive quality control including SDS-PAGE, Western Blot, analytical SEC, HPLC, and endotoxin testing. Protein delivered with a detailed QC report including purity, concentration, and identity confirmation.
Yeast sits between E. coli and insect cells in terms of capability and cost. It offers eukaryotic folding and simple glycosylation with microbial speed and scalability. Choose yeast when your protein needs more than E. coli can provide, but mammalian or insect cell costs are not justified.
| Feature | E. coli | Yeast | Insect | Mammalian |
|---|---|---|---|---|
| Glycosylation | None | High-mannose | Paucimannose | Complex / human |
| Secretion | Limited | Excellent | Good | Good |
| Scalability | High | Very high | Moderate | Moderate |
| Relative Cost | $ | $–$$ | $$ | $$$ |
Pichia pastoris is the preferred choice for secreted protein production — it grows to very high cell densities and secretes very few native proteins, making purification straightforward. Saccharomyces cerevisiae is a GRAS (Generally Recognized As Safe) organism with well-established genetics, making it suitable for food-grade and regulatory-friendly applications. AtaGenix offers both and will recommend the best host for your specific target.
The pilot expression phase (transformation, clone screening, optimization) takes approximately 4 to 5 weeks. Scale-up expression and purification adds approximately 2 weeks. If gene synthesis and vector construction are needed, add additional time at the start of the project.
Choose yeast when your protein needs eukaryotic folding, disulfide bonds, or simple glycosylation, but insect cell or mammalian costs are not justified. Yeast is especially strong for secreted proteins (simplified purification), industrial enzymes (high-density fermentation at low cost), and GRAS-requirement applications. For non-glycosylated targets, E. coli is faster and cheaper. For complex or human-type glycosylation, choose insect cell or mammalian.
Every project includes SDS-PAGE (purity), Western Blot (identity), analytical SEC (aggregation), HPLC, and endotoxin testing. A detailed QC report is delivered with your purified protein. Additional characterization such as mass spectrometry, activity assays, and stability testing are available upon request.
Yeast glycosylation produces high-mannose type glycans which differ from mammalian complex glycans. Timelines and yields are target-dependent. Note: AtaGenix technical handbook does not include a dedicated yeast expression page — specific strains, timelines, and capabilities should be confirmed with the project team before publishing. Quote-based pricing.
Explore real-world yeast protein expression case studies from AtaGenix. Our Pichia pastoris and Saccharomyces cerevisiae platforms deliver high-yield recombinant proteins with proper folding and glycosylation — supporting enzyme production, diagnostic antigen development, and antibody screening applications.
AtaGenix provides highly specific anti-tauN368 monoclonal antibodies to support Alzheimer’s disease research using the hTau368 transgenic mouse model. These antibodies enable precise detection of truncated tau fragments in Western blot and immunofluorescence experiments, validating tau accumulation, phosphorylation, and associated cognitive deficits in the hippocampus. With exceptional specificity and stability, AtaGenix’s solutions empower researchers to explore tau pathology mechanisms and advance tau-targeted therapeutic development.
Contact Us
+86-27-87001869
info@atagenix.com
Building C, R & D Building, No. 666, Shendun 4th Road, Donghu New Technology Development Zone, Wuhan
