Mammalian cell expression is the main system for recombinant protein production. It can handle the complex post-translational modifications, folding, and assembly of recombinant proteins, thus obtaining protein complexes that are superior to other systems. CD Formulation integrates mammalian cell expression technology into our internal protein production platform, offering the ultimate solution for your protein production.
Mammalian expression systems are the first choice for producing most mammalian proteins with native structure and activity due to the physiologically relevant environment. The system can achieve high levels of post-translational processing and functional activity, and can effectively produce biologically active and correctly folded recombinant proteins, which are suitable for producing antibodies, vaccines, and other therapeutic proteins. However, the cultivation of mammalian systems demands a more rigorous and regulated milieu compared to other expression systems.
Fig. 1 Schematic workflow of transient expression process in mammalian cells. (Fu Y, et al., 2024)
CD Formulation is one of the global leaders in the production of therapeutic proteins using mammalian cell expression technology. With our in-house proprietary mammalian cell expression platform, our scientists can efficiently produce a variety of therapeutic proteins, including monoclonal antibodies, recombinant proteins, and fusion proteins.
Our services include but are not limited to:
Codon optimization of target sequence according to the codon preference of CHO or HEK293.
Choose the appropriate vector type according to the experimental purpose and clone the cDNA into the expression vector.
Two methods for producing recombinant proteins in mammalian cells: stably transfected cell lines and transiently transfected cell lines.
Category | Application | Specification |
Stable Transfection | Consistently express recombinant proteins at high yields. |
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Transient Transfection | It is suitable for small to large-scale expression cultures. |
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We have developed proprietary mammalian cell expression platforms based on HEK293 and CHO cell lines, allowing for high-throughput delivery and high-quality recombinant protein expression.
HEK293 Cell | CHO Cell |
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CD Formulation provides a flexible option for mammalian protein expression to produce functional mammalian proteins with appropriate post-translational modifications such as disulfide bonds, glycosylation, and phosphorylation.
Mammalian transient protein expression technology enables rapid and flexible protein production, especially for the expression of human and other mammalian proteins. This technology can specifically produce natively folded proteins with post-translational modifications (such as glycosylation), which are often difficult to achieve in other expression systems.
Constitutive mammalian systems utilize efficient expression vectors to enable the production of large amounts of protein. This enables extremely high levels of recombinant protein production in adherent or suspension-adapted mammalian cells.
Inducible mammalian expression systems can regulate protein expression using a CMV promoter and a tetracycline resistance control element. This system can effectively repress transcriptional activity and release this repression when needed. In the repressed state, these cell lines have low basal expression levels, while expression levels are significantly increased upon induction with tetracycline.
Published Data
Technology: Mammalian Cell Expression Technology
Journal: Sci Rep.
IF: 3.8
Published: 2019
Results:
The authors developed a fully human expression system based on HEK293 cells for stable and high-titer recombinant protein production. GLUL (encoding glutamine synthetase) was first knocked out using the CRISPR-Cas9 system. An expression vector using human GLUL as a selection marker was then generated for recombinant human erythropoietin (EPO) as our model protein. The selection was performed using methionine sulfoximine (MSX) to select high EPO-expressing cells. The results showed EPO production up to 92700 U/mL in a 2 L stirred fed-batch bioreactor, and the N-glycosylation of the produced EPO was similar to the endogenous human protein, and no non-human glycan epitopes were detected.
Fig. 2 Generation of HEK293 GLUL knockout (KO) cells. (Chin CL, et al., 2019)
Thanks to our in-house advanced mammalian cell 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 mammalian cell expression technology can support your recombinant protein synthesis projects.
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