Yeast protein expression technology is ideal for the large-scale production of proteins with a variety of post-translational modifications with well-defined genetic characteristics. CD Formulation integrates yeast expression technology into our internal protein production platform, offering the ultimate solution for your protein production. Our scientists have decades of experience and can provide you with high-quality, considerate yeast expression solutions that will effectively save you costs and time.
Yeast, the simplest eukaryotic expression system, is an excellent host for the production of functional recombinant proteins. It is easy to culture, low-cost and can be produced on a large scale while supporting post-translational modifications and correct folding of eukaryotic proteins. The system is also capable of producing membrane proteins and many recombinant transmembrane proteins. Common yeast expression hosts for the expression of recombinant proteins include Saccharomyces cerevisiae, Pichia pastoris, Hansenula polymorpha, Yarrowia lipolytica, Arxula adeninivorans, Kluyveromyces lactis, and Schizosaccharomyces pombe.
Fig. 1 Schematic of yeast expression vector. (Khatibi P, et al., 2014)
CD Formulation is one of the global leaders in the production of therapeutic proteins using yeast expression technology. Our yeast expression technology-based therapeutic protein production services cover all steps from DNA synthesis to vector construction to protein production. Our scientists optimize codons according to the codon preferences of different yeasts and improve protein production by considering gene dosage, integration site, transformant phenotype, and culture conditions.
Our services include but are not limited to:
Small-scale expression tests were performed on selected monoclonal strains.
YIp integration vectors cannot replicate autonomously and must be integrated into the genome by low-frequency homologous recombination. Usually, YIp vectors are integrated as a single copy. For overexpression of specific genes, the YIp plasmid has two yeast fragments, YFG1 and URA3 markers, which can be integrated at any genomic site.
YCp vectors are autonomously replicating vectors with a centromere sequence (CEN) and an autonomously replicating sequence (ARS). The copy number of YCp vectors is very low, only 1 to 3 per cell. Since these vectors are relatively unstable, they are not suitable for high-level expression, but can be used as routine cloning vectors.
The YEp vector is autonomously replicative. Since the fragment of the yeast 2 μm plasmid is the origin of replication, it is also responsible for the high copy number and high transformation frequency. Generally, this system is suitable for small-scale expression studies and is not recommended for large-scale production.
Our scientists commonly use Saccharomyces cerevisiae and Pichia pastoris expression systems for high-efficiency production of heterologous proteins.
Saccharomyces Cerevisiae | Pichia Pastoris |
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Published Data
Technology: Yeast Expression Technology
Journal: FEBS Lett.
IF: 2.96
Published: 2003
Results:
The authors introduce a new strategy to optimize the expression of functional membrane proteins (MPs) in Saccharomyces cerevisiae. This approach leverages the unfolded protein response (UPR) pathway—a stress signaling mechanism that detects the accumulation of unfolded proteins in the endoplasmic reticulum (ER). The results indicate that by adjusting the expression level of a protein to avoid or minimize the induction of the UPR, functional expression is increased.
Fig. 2 A novel yeast expression system with in vivo protein folding assay based on the UPR. (Guarrochena X, et al., 2003)
Thanks to our in-house advanced yeast expression platform, CD Formulation is committed to providing efficient and economical production of therapeutic proteins. Please feel free to contact us if you are interested in our services. Learn how our yeast expression technology can support your recombinant protein synthesis projects.
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