Development of a VHH-Based Erythropoietin Quantification Assay

Molecular Biotechnology

Volumn 57, Issue 8, 2015, Pages 692-700

  Kol, Stefan ^a   Kallehauge, Thomas Beuchert ^a   Adema, Simon ^b   Hermans, Pim ^b  

^a Chalmers University of Technology   (Denmark)

^b BAC BV Life Technologies   (Netherlands)

Author keywords

Biolayer interferometry; Chinese hamster ovary (CHO) cells; EPO; Erythropoietin; Quantification assay; VHH

Indexed keywords

ANTIBODIES; CELL CULTURE; INTERFEROMETRY;

CELL LINES; CHINESE HAMSTER OVARY CELLS; ERYTHROPOIETIN (EPO); HIGH THROUGHPUT; PH-DEPENDENT; QUANTIFICATION ASSAYS; SINGLE-DOMAIN ANTIBODIES; SUPERNATANTS;

ERBIUM COMPOUNDS;

ERYTHROPOIETIN; NANOBODY; RITUXIMAB; EPO PROTEIN, HUMAN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

ANIMAL CELL; ARTICLE; BIOLAYER INTERFEROMETRY; BIOSENSOR; CAMELID; CONTROLLED STUDY; ELISA KIT; IMMUNOSENSOR; INTERFEROMETRY; IONIC STRENGTH; NONHUMAN; PH; SUPERNATANT; ANIMAL; CAMEL; CHEMISTRY; CHO CELL LINE; CRICETULUS; HAMSTER; HUMAN; IMMUNOASSAY; IMMUNOLOGY;

CAMELIDAE; CRICETULUS GRISEUS;

ANIMALS; CAMELUS; CHO CELLS; CRICETINAE; CRICETULUS; ERYTHROPOIETIN; HUMANS; HYDROGEN-ION CONCENTRATION; IMMUNOASSAY; SINGLE-CHAIN ANTIBODIES;

EID: 84937975476     PISSN: 10736085     EISSN: 15590305     Source Type: Journal    
DOI: 10.1007/s12033-015-9860-7     Document Type: Article

References (15)

1. Lee, J. S., Ha, T. K., Lee, S. J., & Lee, G. M. (2012). Current state and perspectives on erythropoietin production. Applied Microbiology and Biotechnology,95, 1405–1416.
2. Lai, P. H., Everett, R., Wang, F. F., Arakawa, T., & Goldwasser, E. (1986). Structural characterization of human erythropoietin. Journal of Biological Chemistry,261, 3116–3121.
3. Krantz, S. B. (1991). Erythropoietin. Blood,77, 419–434.
4. Walsh, G. (2014). Biopharmaceutical benchmarks 2014. Nature Biotechnology,32, 992–1000.
5. Abdiche, Y., Malashock, D., Pinkerton, A., & Pons, J. (2008). Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet. Analytical Biochemistry,377, 209–217.
6. Concepcion, J., Witte, K., Wartchow, C., Choo, S., Yao, D., Persson, H., et al. (2009). Label-free detection of biomolecular interactions using BioLayer interferometry for kinetic characterization. Combinatorial Chemistry and High Throughput Screening,12, 791–800.
7. Muyldermans, S. (2013). Nanobodies: natural single-domain antibodies. Annual Review of Biochemistry,82, 775–797.
8. HH antibody fragments and their high level secretion by Saccharomyces cerevisiae. Journal of Biotechnology,78, 11–21.
9. McCue, J. T., Selvitelli, K., & Walker, J. (2009). Application of a novel affinity adsorbent for the capture and purification of recombinant factor VIII compounds. Journal of Chromatography A,1216, 7824–7830.
10. Kotin, R. M. (2011). Large-scale recombinant adeno-associated virus production. Human Molecular Genetics,20, R2–R6.
11. Hermans, P., Adams, H., & Detmers, F. (2014). Purification of antibodies and antibody fragments using CaptureSelect affinity resins. Methods in Molecular Biology,1131, 297–314.
12. Eifler, N., Medaglia, G., Anderka, O., Laurin, L., & Hermans, P. (2014). Development of a novel affinity chromatography resin for platform purification of lambda fabs. Biotechnology Progress,30, 1311–1318.
13. Hermans, P., Grit, G., & Blokland, S. (2013). CaptureSelect affinity ligands for antibody detection and characterization. http://www.fortebio.com/documents/ForteBio_App_Note_9.pdf.
14. Eustace, D. (2011). Quantitation of recombinant human factor IX (rFIX) in bioreactor harvest samples using bio-layer interferometry. http://www.fortebio.com/doc_download.html?docid=188.
15. Boersma, Y. L., & Pluckthun, A. (2011). DARPins and other repeat protein scaffolds: Advances in engineering and applications. Current Opinion in Biotechnology,22, 849–857.