Transient transfection of CHO-K1-S using serum-free medium in suspension: a rapid mammalian protein expression system
Abstract
With the recent completion of the human genome sequencing project, scientists now face the daunting challenge of deciphering the function of these newly found genes quickly and efficiently. For biotechnology, it is equally important to identify the therapeutically relevant genes as quickly as possible. Mammalian expression systems provide many advantages to aid in this task. Mammalian cell lines have the capacity for proper post-translational modifications, including proper protein folding and glycosylation. In response to these needs, a CHO-K1 cell line that grows in suspension and in serum-free media was initially established and designated CHO-K1-S. An antibody gene of interest was chosen as the target for optimization rather than a reporter gene system. A comparison of various lipid transfection reagents was made using recombinant protein expression as the endpoint readout. Various other parameters including lipid:DNA ratios, cell density, and transfections in shaker versus spinner flasks were tested using the CHO-K1-S cell line. As a result, a rapid and reliable transient transfection protocol was developed. Using this procedure, we have produced milligram/per liter quantities of bioactive recombinant proteins from several genes of interest.
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When the need for a quick and economical approach prevails, transient expression remains the best choice for protein production.
“When the need for a quick and economical approach prevails, transient expression remains the best choice for protein production (Rosser et al., 2005;Pham et al., 2006;Geisse, 2009;Chahal et al., 2011;Baldi et al., 2012).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Rosser et al., 2005
Transient expression is ideal for high throughput screening for hits identification and very helpful for early stage product characterization.
“Yet, it is ideal for high throughput screening for hits identification and very helpful for early stage product characterization (Ozturk and Hu, 2005;Rosser et al., 2005;Rita Costa et al., 2010).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Rosser et al., 2005
Cites
A new technique for the assay of infectivity of human adenovirus 5 DNA
Graham, F. L., & van der Eb, A. J. (1973) · Virology · doi:10.1016/0042-6822(73)90341-3 · Cited by 9,734 · see citing works
Boussif, O., Lezoualc’h, F., Zanta, M. A., Djavaheri‐Mergny, M., Scherman, D., DEMENEIX, B. A., & Behr, J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.16.7297 · Cited by 6,256 · see citing works
Electroporation for the efficient transfection of mammalian cells with DNA
Chu, G., Hayakawa, H., & Berg, P. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.3.1311 · Cited by 851 · see citing works
Baculovirus-mediated gene transfer into mammalian cells.
Boyce, F. M., & Bucher, N. L. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.6.2348 · Cited by 462 · see citing works
Condreay, J. P., Witherspoon, S. M., Clay, W. C., & Kost, T. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.127 · Cited by 419 · see citing works
Large-scale transient expression in mammalian cells for recombinant protein production
Wurm, F. M., & Bernard, A. (1999) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(99)80027-5 · Cited by 204 · see citing works
Transient gene expression: Recombinant protein production with suspension‐adapted HEK293‐EBNA cells
Meissner, P., Pick, H. M., Kulangara, A., Chatellard, P., Friedrich, K., & Wurm, F. M. (2001) · Biotechnology and Bioengineering · doi:10.1002/bit.1179 · Cited by 200 · see citing works
Recombinant baculoviruses as expression vectors for insect and mammalian cells
Kost, T. A., & Condreay, J. P. (1999) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(99)00005-1 · Cited by 156 · see citing works
Codon optimization for high-level expression of human erythropoietin (EPO) in mammalian cells
Kim, C. H., Oh, Y., & Lee, T.-H. (1997) · Gene · doi:10.1016/s0378-1119(97)00384-3 · Cited by 154 · see citing works
In Vivo Gene Transfer in Mouse Skeletal Muscle Mediated by Baculovirus Vectors
Pieroni, L., Maione, D., & Monica, N. L. (2001) · Human Gene Therapy · doi:10.1089/104303401750195845 · Cited by 128 · see citing works
Duisit, G., Saleün, S., Douthe, S., Barsoum, J., Chadeuf, G., & Moullier, P. (1999) · The Journal of Gene Medicine · doi:10.1002/(sici)1521-2254(199903/04)1:2 · Cited by 117 · see citing works
High levels of protein expression using different mammalian CMV promoters in several cell lines
Xia, W., Bringmann, P., McClary, J., Jones, P. P., Manzana, W., Zhu, Y., Wang, S., Liu, Y., Harvey, S., Madlansacay, M. R., et al. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.07.008 · Cited by 88 · see citing works
Self-citationJordan, M., Köhne, C., & Wurm, F. M. (1998) · Cytotechnology · doi:10.1023/a:1007917318181 · Cited by 75 · see citing works
Epstein-Barr virus-derived vectors for transient and stable expression of recombinant proteins.
Cachianes, G., Ho, C., Weber, R. F., Williams, S. R., Goeddel, D. V., & Leung, D. W. (1993) · PubMed · Cited by 56 · see citing works
Large scale transient expression with COS cells
Blasey, H. D., Aubry, J., Mazzei, G. J., & Bernard, A. R. (1996) · Cytotechnology · doi:10.1007/bf00767766 · Cited by 45 · see citing works
Pick, H. M., Meissner, P., Preuss, A. K., Tromba, P., Vogel, H., & Wurm, F. M. (2002) · Biotechnology and Bioengineering · doi:10.1002/bit.10309 · Cited by 34 · see citing works
Preuss, A. K., Connor, J. A., & Vogel, H. (2000) · Cytotechnology · doi:10.1023/a:1008150402616 · Cited by 11 · see citing works
Transient Transfection in Mammalian Cells
Schlaeǵer, E.-J., Legendre, J., Trzeciak, A. M., Kitas, E. A., Christensen, K., Deuschle, U., & Supersaxo, A. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-46860-3_18 · Cited by 5 · see citing works
A simple apparatus for the continuous growth of experimental tumor cells in vitro
Bloch, A., & Dutschman, G. E. (1973) · Biotechnology and Bioengineering · doi:10.1002/bit.260150114 · Cited by 1 · see citing works
Transient Transfection Induces Early Cytosolic Calcium Signaling in CHO-K1 Cells
Preuss, A. K., Pick, H. M., Wurm, F. M., & Vogel, H. (2005) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-46869-7_4 · Cited by 1 · see citing works
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Baldi, L., Hacker, D. L., Adam, M., & Wurm, F. M. (2007) · Biotechnology Letters · doi:10.1007/s10529-006-9297-y · Cited by 311 · see citing works
Therapeutic glycoprotein production in mammalian cells
Lalonde, M.-E., & Durocher, Y. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.028 · Cited by 296 · see citing works
Large-Scale transfection of mammalian cells for the fast production of recombinant protein
Pham, P. L., Kamen, A., & Durocher, Y. (2006) · Molecular Biotechnology · doi:10.1385/mb:34:2:225 · Cited by 236 · see citing works
Guidelines to cell engineering for monoclonal antibody production
Rita Costa, A., Elisa Rodrigues, M., Henriques, M., Azeredo, J., & Oliveira, R. (2010) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2009.10.002 · Cited by 178 · see citing works
Daramola, O., Stevenson, J., Dean, G., Hatton, D., Pettman, G., Holmes, W., & Field, R. (2014) · Biotechnology Progress · doi:10.1002/btpr.1809 · Cited by 134 · see citing works
Corchero, J. L., Gasser, B., Resina, D., Smith, W., Parrilli, E., Vázquez, F., Abasolo, I., Giuliani, M., Jäntti, J., Ferrer, P., et al. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2012.09.001 · Cited by 133 · see citing works
Segura, M. M., Garnier, A., Durocher, Y., Coelho, H., & Kamen, A. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21467 · Cited by 130 · see citing works
Reflections on more than 10 years of TGE approaches
Geisse (2009) · doi:10.1016/j.pep.2008.10.017 · Cited by 117 · see citing works
Recent advances in the production of proteins in insect and mammalian cells for structural biology
Nettleship, J. E., Assenberg, R., Diprose, J. M., Rahman-Huq, N., & Owens, R. J. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.02.006 · Cited by 104 · see citing works
Liu, C., Dalby, B., Chen, W., Kilzer, J. M., & Chiou, H. C. (2008) · Molecular Biotechnology · doi:10.1007/s12033-008-9051-x · Cited by 93 · see citing works
Gutiérrez-Granados, S., Cervera, L., Kamen, A., & Gòdia, F. (2018) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2017.1419459 · Cited by 92 · see citing works
Production systems for recombinant antibodies
Schirrmann, T. (2008) · Frontiers in bioscience · doi:10.2741/3024 · Cited by 89 · see citing works
High levels of protein expression using different mammalian CMV promoters in several cell lines
Xia, W., Bringmann, P., McClary, J., Jones, P. P., Manzana, W., Zhu, Y., Wang, S., Liu, Y., Harvey, S., Madlansacay, M. R., et al. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.07.008 · Cited by 88 · see citing works
Self-citationStructural genomics for membrane proteins
Lundstrom, K. H. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6252-y · Cited by 77 · see citing works
Müller, N., Derouazi, M., Tilborgh, F. V., Wulhfard, S., Hacker, D. L., Jordan, M., & Wurm, F. M. (2007) · Biotechnology Letters · doi:10.1007/s10529-006-9298-x · Cited by 74 · see citing works
Majors, B. S., Betenbaugh, M. J., Pederson, N. E., & Chiang, G. G. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.21917 · Cited by 70 · see citing works
Gaillet, B., Gilbert, R., Broussau, S., Pilotte, A., Malenfant, F., Mullick, A., Garnier, A., & Bernard Massie, B. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22698 · Cited by 59 · see citing works
Du, L., Zhao, G., Li, L., He, Y., Zhou, Y., Zheng, B., & Jiang, S. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.05.003 · Cited by 50 · see citing works
General Introduction: Recombinant Protein Production and Purification of Insoluble Proteins
Ferrer‐Miralles, N., Saccardo, P., Corchero, J. L., Xu, Z., & García‐Fruitós, E. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2205-5_1 · Cited by 45 · see citing works
Transient Recombinant Protein Expression in Mammalian Cells
Jäger, V., Büssow, K., & Schirrmann, T. (2014) · Cell engineering · doi:10.1007/978-3-319-10320-4_2 · Cited by 40 · see citing works
Link, N., Brunner, T. J., Dreesen, I. A. J., Stark, W. J., & Fussenegger, M. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21525 · Cited by 39 · see citing works
Lattenmayer, C., Loeschel, M., Schriebl, K., Steinfellner, W., Sterovsky, T., Trummer, E., Vorauer‐Uhl, K., Müller, D., Katinger, H. W. D., & Kunert, R. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.21183 · Cited by 35 · see citing works
Improvement strategies for transient gene expression in mammalian cells
Fu, Y., Han, Z., Cheng, W., Niu, S., Wang, T., & Wang, X. (2024) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-024-13315-y · Cited by 32 · see citing works
Using matrix attachment regions to improve recombinant protein production
Harraghy, N., Buceta, M., Regamey, A., Girod, P.-A., & Mermod, N. (2012) · Methods in Molecular Biology · doi:10.1007/978-1-61779-352-3_7 · Cited by 30 · see citing works
New frontiers in cell line development: challenges for biosimilars
Hou, J. J. C., Codamo, J., Pilbrough, W., Hughes, B. S., Gray, P. P., & Munro, T. P. (2011) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.2574 · Cited by 27 · see citing works
Codamo, J., Hou, J. J. C., Hughes, B. S., Gray, P. P., & Munro, T. P. (2011) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.2572 · Cited by 25 · see citing works
Gaillet, B., Gilbert, R., Amziani, R., Guilbault, C., Gadoury, C., Caron, A. W., Mullick, A., Garnier, A., & Bernard Massie, B. (2006) · Biotechnology Progress · doi:10.1021/bp060187j · Cited by 24 · see citing works
Insect Cells–Baculovirus System for the Production of Difficult to Express Proteins
Ősz, J., Radu, L., Abdulrahman, W., Kolb‐Cheynel, I., Troffer-Charlier, N., Birck, C., & Poterszman, A. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2205-5_10 · Cited by 20 · see citing works
Integrated approach to produce a recombinant, his‐tagged human α‐galactosidase a in mammalian cells
Corchero, J. L., Mendoza, R., Lorenzo, J., Rodríguez‐Sureda, V., Domı́nguez, C., Vázquez, E., Ferrer‐Miralles, N., & Villaverde, A. (2011) · Biotechnology Progress · doi:10.1002/btpr.637 · Cited by 17 · see citing works
The transient expression of CHIKV VLP in large stirred tank bioreactors
Chen, P., Demirji, J., Ivleva, V. B., Horwitz, J., Schwartz, R. M., & Arnold, F. (2019) · Cytotechnology · doi:10.1007/s10616-019-00346-x · Cited by 16 · see citing works
Enhancement of recombinant antibody production in HEK 293E cells by WPRE
Kim, K., Kim, M., Moon, J. H., Jeong, M. S., Kim, J., Lee, G. M., Myung, P.-K., & Hong, H. J. (2009) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-008-0221-2 · Cited by 14 · see citing works
Diepenbruck, C., Klinger, M., Urbig, T., Baeuerle, P. A., & Neef, R. (2012) · Molecular Biotechnology · doi:10.1007/s12033-012-9590-z · Cited by 13 · see citing works
Rossi, D. L., Rossi, E. A., Goldenberg, D. M., & Chang, C. (2011) · Biotechnology Progress · doi:10.1002/btpr.584 · Cited by 11 · see citing works
Heparan sulfate proteoglycan synthesis in CHO DG44 and HEK293 cells
Lee, S., Kim, M. G., Kim, N., Heo, W. D., & Lee, G. M. (2016) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-015-0688-6 · Cited by 11 · see citing works
Kakimoto, S., Tanabe, T., Azuma, H., & Nagasaki, T. (2009) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2009.06.017 · Cited by 11 · see citing works
Transient recombinant protein expression in mammalian cells : the role of mRNA level and stability
Wulhfard, S. (2009) · Infoscience (Ecole Polytechnique Fédérale de Lausanne) · doi:10.5075/epfl-thesis-4393 · Cited by 10 · see citing works
Growth kinetics and validation of near‐physiologically synchronized HEK293S Cultures
Salvador, A. E. C., Fuge, G., Jandt, U., & Zeng, A. (2015) · Engineering in Life Sciences · doi:10.1002/elsc.201400224 · Cited by 10 · see citing works
İz, S. G., Anıl-İnevi, M., Saglam‐Metiner, P., Ayyıldız-Tamis, D., & Kisbet, N. (2017) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-017-2540-2 · Cited by 10 · see citing works
Transient expression of osteopontin in HEK 293 cells in serum-free culture
Han, X., Sun, L., Fang, Q., Li, D., Gong, X., Wu, Y., Yang, S., & Shen, B. Q. (2006) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2006.12.013 · Cited by 10 · see citing works
Transient gene delivery for functional enrichment of differentiating embryonic stem cells
Wallenstein, E. J., Barminko, J., Schloss, R. S., & Yarmush, M. L. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.22027 · Cited by 10 · see citing works
Kim, W., Kim, M., Kim, Y., & Lee, G. M. (2012) · Process Biochemistry · doi:10.1016/j.procbio.2012.08.005 · Cited by 8 · see citing works
Hands-on experiments on glycemia regulation and type 1 diabetes
Mingueneau, M., Chaix, A., Scotti, N., Chaix, J., Reynders, A., Hammond, C., & Thimonier, J. (2015) · AJP Advances in Physiology Education · doi:10.1152/advan.00047.2015 · Cited by 8 · see citing works
Kim, W., Kim, Y. J., & Lee, G. M. (2014) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-014-0151-0 · Cited by 7 · see citing works
Bcl-2 overexpression in CHO cells improves polyethylenimine-mediated gene transfection
Lee, S., & Lee, G. M. (2013) · Process Biochemistry · doi:10.1016/j.procbio.2013.03.021 · Cited by 7 · see citing works
Du, L., Zhang, X., Liu, J., & Jiang, S. (2011) · Journal of Visualized Experiments · doi:10.3791/2444 · Cited by 7 · see citing works
Chitosan and Alginate in Aquatic Vaccine Development
Zubareva, A. A., Svirshchevskaya, E. V., Nedoluzhko, A., & Skorik, Y. А. (2025) · Polysaccharides · doi:10.3390/polysaccharides6040111 · Cited by 6 · see citing works
Recombinant Protein Production and Purification of Insoluble Proteins
Ferrer‐Miralles, N., Saccardo, P., Corchero, J. L., & García‐Fruitós, E. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1859-2_1 · Cited by 7 · see citing works
Transient Gene Expression‐Based Protein Production in Recombinant Mammalian Cells
Lee, J., Hansen, H. G., Park, S., Park, J., & Kim, Y. (2019) · doi:10.1002/9783527811410.ch3 · Cited by 6 · see citing works
Fang, Q., & Shen, B. (2010) · Electronic Journal of Biotechnology · doi:10.2225/vol13-issue5-fulltext-6 · Cited by 5 · see citing works
Naddafi, F., Shirazi, F. H., Talebkhan, Y., Tabarzad, M., Barkhordari, F., Farahani, Z. A., Bayat, E., Moazzami, R., Mahboudi, F., & Davami, F. (2018) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2018.1525562 · Cited by 5 · see citing works
Optimization in Transfection and Stable Production of β-galactosidase in Chinese Hamster Ovary Cells
Saifudin, N., Ibrahim, N., & Anuar, N. (2010) · Biotechnology(Faisalabad) · doi:10.3923/biotech.2011.86.93 · Cited by 3 · see citing works
Du, L., Zhang, X., Liu, J., & Jiang, S. (2011) · Journal of Visualized Experiments · doi:10.3791/2444-v · Cited by 3 · see citing works
Transient Gene Expression in Mammalian Cells: Promises and Challenges for Medical Biotechnology
Hacker, D. L., Baldi, L., Adam, M., & Wurm, F. M. (2009) · Encyclopedia of Industrial Biotechnology · doi:10.1002/9780470054581.eib568 · Cited by 3 · see citing works
Protein Therapeutic: Production, Application, and Future Scenario
Chaudhary, R., Balhara, M., & Chhillar, A. K. (2017) · Springer eBooks · doi:10.1007/978-981-10-5511-9_4 · Cited by 2 · see citing works
Antigenicity and immunogenicity of SARS-CoV-2 surface glycoprotein fragment in CHO cells
Karimi, S., Nazarian, S., Sotoodehnejadnematalahi, F., Dorostkar, R., & Amani, J. (2023) · Iranian Journal of Microbiology · doi:10.18502/ijm.v15i1.11929 · Cited by 2 · see citing works
YANG, Y., CHEN, L., Han, B., Chong-tao, X., & Pan, H. (2006) · Chinese journal of biotechnology/Shengwu gongcheng xuebao · doi:10.1016/s1872-2075(06)60031-9 · Cited by 2 · see citing works
Sauerwald, T. M., Lewis, A., Dorai, H., & Betenbaugh, M. J. (2011) · Elsevier eBooks · doi:10.1016/b978-0-08-088504-9.00056-8 · Cited by 1 · see citing works
A multidisciplinary guided practical on type I diabetes engaging students in inquiry-based learning
Mingueneau, M., Chaix, A., Scotti, N., Chaix, J., Reynders, A., Hammond, C., & Thimonier, J. (2015) · AJP Advances in Physiology Education · doi:10.1152/advan.00045.2015 · Cited by 1 · see citing works
Apoptosis: The Signaling Pathways and Their Control
Sauerwald, T. M., Lewis, A., Dorai, H., & Betenbaugh, M. J. (2011) · Elsevier eBooks · doi:10.1016/b978-0-444-64046-8.00030-6 · Cited by 1 · see citing works
Lundstrom, K. H. (2007) · Cell engineering · doi:10.1007/1-4020-5252-9_1 · Cited by 1 · see citing works
Wulhfard, S., Kiseljak, D., Baldi, L., Hacker, D. L., & Wurm, F. M. (2011) · Springer eBooks · doi:10.1007/978-94-007-0884-6_20
Design and development of miRNA and stem cell based micro/nano systems as lung disease therapy
Alhasan, L. (2016) · RMIT Research Repository (RMIT University Library) · doi:10.25439/rmt.27582078
Efficient Expression of sTNFRII-gAD-Fc Fusion Protein in CHO Cell
Wang, C., Liu, Y. M., Cai, Q., Yang, H., Ma, L., Gao, J., Provincial, Z., & Zhejiang, W. (2015)
Efficient Expression of sTNFRII-gAD-Fc Fusion Protein in CHO Cell
王, 彩. (2015) · Immunology Studies · doi:10.12677/is.2015.31001
Review Structural genomics for membrane proteins
Lundstrom, K. H. (2006)
Hsu, C., Jain, H. V., Williams, A., Wang, J., Lute, S. C., Beaucage, S. L., & Brorson, K. (2017) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1620
Nikfarjam, S., Liu, C., Laurence, E. J., Laurence, A. N., Chlebek, J. L., Ricci, D. P., Hoang-Phou, S. A., Laurence, T. A., & Coleman, M. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.05.668779
Rapid cell-free antibody fragment production and binding analysis via fluorescence correlation
Nikfarjam, S., Liu, C., Laurence, E. J., Laurence, A., Chlebek, J. L., Ricci, D. P., Hoang-Phou, S. A., Carrano, I. M., Laurence, T. A., & Coleman, M. A. (2026) · Methods · doi:10.1016/j.ymeth.2026.08.007
- Authors
- Rosser, M. P., Xia, W., Hartsell, S., McCaman, M., Zhu, Y., Wang, S., Harvey, S., Bringmann, P., & Cobb, R. R.
- Corresponding author
- Cobb, Ronald R.
- Venue
- Protein Expression and Purification
- Publisher
- Elsevier BV
- Published
- 2005-04
- Volume
- 40
- Issue
- 2
- Pages
- 237-243
- ISSN
- 1046-5928 (ISSN-L)
- OpenAlex
- W2045247083
- Cited by
- 68
- References
- 20
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 1 · 2019: 2 · 2018: 2 · 2017: 4 · 2016: 2 · 2015: 5 · 2014: 4 · 2013: 2 · 2012: 3
- FWCI
- 2.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Protein Expression and Purification (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- transient transfection, cell suspension culture, serum-free medium, recombinant antibody production, spinner flasks, post-translational modification
- MeSH terms
- Animals, Cloning, Molecular, Cricetulus, Cricetinae, Humans, Immunoglobulin Fc Fragments, Indicators and Reagents, Recombinant Proteins, Transfection, CHO Cells, Culture Media, Serum-Free, Mice
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