Recombinant Lectin Production in Mammalian Cells
Mammalian Cells: a Relatively Mature Eukaryotic Expression System
A mammalian cell expression system is a technology that uses mammalian cells as host cells to achieve protein expression by transfection to a foreign expression vector. At CD BioGlyco, we mainly provide expression services based on Chinese hamster ovary (CHO) cells and human embryonic kidney cells 293 (HEK293) because they are easy to process, grow fast, have extremely high transfection efficiency, and have highly efficient recombinant protein expression. In addition, we offer other cell line hosts including but not limited to:
- Various mouse myelomas such as NS0 murine myeloma cells
- Human cell lines such as human embryonic kidney (HEK) cells
- Green monkey kidney cells
- Baby hamster kidney (BHK) cells
A Good Recombinant Lectin Production Service in Mammalian Cells at CD BioGlyco
Our company has a complete set of recombinant lectin production solutions and experienced operators. According to the experimental requirements and the characteristics of the target protein, suitable lactating cell lines, such as CHO cells and HEK293 cells, are selected to ensure the efficient expression of the target protein. Every step is tightly controlled.
- Expression vectors: We achieve high levels of target expression by designing expression vectors, including selecting appropriate promoters, regulatory elements, and target protein-coding sequences.
- Culture conditions: We continuously optimize cell culture conditions to improve cell growth and protein expression efficiency.
- Optimal collection time: Our professional technicians select the appropriate time point for cell collection according to the expression kinetics of the target protein to obtain the optimal protein expression level.
Fig.1 The flowchart of recombinant lectin production service. (CD BioGlyco)
The Analysis of Recombinant Lectin in Mammalian Cells at CD BioGlyco
For purified recombinant lectins, we offer a wide range of analysis services.
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and western blotting
- Native MS
- Bacterial agglutination assay
- Liquid chromatography-tandem mass spectrometry (LC-MS/MS)
- Glycan Array
- Hemagglutination inhibition (HAI) assay
Publication
Paper Title: Expression and characterization of recombinant chicken mannose binding lectin
Expression System: HeLa R19 cells
Journal: Immunobiology
Published: 2017
IF: 3.152
Results: HeLa R19 cells expressing recombinant chicken mannose binding lectin (RcMBL) were purified and examined. The results showed that the recombinant lectin was similar to the natural sources regarding structural functions and activity. The monomer mass was 26 kDa, corresponding to the predicted mass. The glycan microarray and bioactivity detection of RcMBL showed the strongest binding to high-mannose glycans. RcMBL as a valuable tool to study the role of molecular MBL between pathogens helpd to determine the role of MBLs in infections in chickens and other birds.
Fig.2 Plot of analyzed data for RcMBL. (Zhang, et al., 2017)
Advantages of Us
- High level of expression: Our highly trained staff provides high levels of expression through an optimized mammalian cell expression system for large-scale lectin production.
- Authentic expression: The recombinant lectins we offer are structurally and functionally similar to those of natural sources.
- Regulatable expression system: Our experienced technicians achieve regulation and timing control of expression levels by selecting appropriate promoters and regulatory elements.
CD BioGlyco has a highly trained production team to serve our clients in the production of Recombinant Lectins. We offer a wide range of Expression Systems for clients to choose from and support both small and large-batch production services. The protein amount is changed according to the client's requirement, please feel free to contact us.
References
- Yin, J.; et al. Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes. J Biotechnol. 2007, 127(3): 335-47.
- Demain, A.L.; Vaishnav, P. Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv. 2009, 27(3): 297-306.
- Zhang, W.; et al. Expression and characterization of recombinant chicken mannose binding lectin. Immunobiology. 2017, 222(3): 518-528.
