Mammalian cell surface display is a powerful technology for screening antibodies with high specificity and affinity. Our company has successfully developed a cutting-edge mammalian cell surface display platform that accelerates the antibody discovery process and provides a powerful screening platform for identifying lead drug candidates with excellent binding properties.
Overview of Mammalian Cell Surface Display
Mammalian cell surface display relies on the fusion of antibody genes with genes encoding cell surface proteins, such as membrane proteins or receptors. This fusion allows the antibodies to be presented on the surface of mammalian cells, preserving their native conformation and interaction with target antigens. This display system is well suited for the selection of antibody fragments (e.g., scFv, Fab) and full-length antibodies.
Fig. 1 The process of mammalian cell surface display. (Valldorf B, et al., 2022)
Our Services
Our company has successfully established a state-of-the-art mammalian cell surface display platform. By leveraging the unique properties of mammalian cells, we have created an efficient and versatile system for single domain antibody (adAb) generation, screening and optimization. This innovative approach enhances your ability to develop novel therapeutic antibodies and helps advance the field of biologics-based therapeutics.
Workflow of Mammalian Cell Surface Display
sdAb Library Construction
Construct diverse sdAb libraries by cloning the genes encoding sdAbs into a mammalian cell surface display vector. The libraries consist of a diverse collection of antibody fragments, enabling the screening of a wide range of potential binders.
Transfection of Mammalian Cells and Antibody Display
The constructed sdAb library vector is then transfected into mammalian cells using transfection techniques like lipid-based transfection or viral transduction. This step ensures that the vector is successfully inserted into the host cells, allowing for the expression of the fusion protein on the cell surface.
Screening and Enrichment
Next, we screen mammalian cells by fluorescence-activated cell sorting (FACS) or magnetic-activated cell sorting (MACS) to isolate cells that display the desired sdAbs. During the selection process, the cells expressing sdAbs with high affinity and specificity for the target antigen are enriched.
Cloning and Sequencing
Clone the genes encoding the enriched sdAbs from the sorted cells and sequence them to determine their amino acid sequences. This step helps in identifying and characterizing the sdAbs with the desired binding properties.
Characterization and Optimization
Our scientists use methods such as ELISA, surface plasmon resonance (SPR), or cell-based assays to evaluate the affinity, specificity, and other properties of the selected sdAbs. If necessary, we will perform additional rounds of mutagenesis and screening to improve the characteristics of the sdAb.
Technical Advantages and Optional Mammalian Cell Types
Technical Advantages
- Provide a more native-like environment
- Complex library diversity
- High affinity and specificity
- High-Throughput Screening
- Compatibility with mammalian expression systems
Optional Mammalian Cell Types
- Human embryonic kidney 293 (HEK293) cells
- Murine myeloma NS0 cells
- Hamster ovary cells
- HEK293T Cells
- And More
Our Advantages
Time-saving services with high efficiency
Professional and experienced team
Cutting edge technology platform
Numerous service cases and customer praise
Through the integration of cutting-edge technologies, our company continues to drive advancements in antibody discovery, offering tailored solutions for various therapeutic challenges. If you are interested in our services, please don't hesitate to contact us for further information and pricing details.
References
- Valldorf B, Hinz S C, Russo G, et al. Antibody display technologies: selecting the cream of the crop[J]. Biological chemistry, 2022, 403(5-6): 455-477.
- Soga K, Abo H, Qin S Y, et al. Mammalian cell surface display as a novel method for developing engineered lectins with novel characteristics[J]. Biomolecules, 2015, 5(3): 1540-1562.