Dataset of the binding kinetic rate constants of anti-PCSK9 antibodies obtained using the Biacore T100, ProteOn XPR36, Octet RED384, and IBIS MX96 biosensor platforms
Here we provide data from a head-to-head comparison study using four biosensor platforms: GE Healthcare׳s Biacore T100, Bio-Rad׳s ProteOn XPR36, ForteBio׳s Octet RED384, and Wasatch Microfluidics׳s IBIS MX96. We used these instruments to analyze the binding interactions of a panel of ten high-affini...
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Format: | Article |
Language: | English |
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Elsevier
2016-09-01
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Series: | Data in Brief |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340916304802 |
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author | Danlin Yang Ajit Singh Helen Wu Rachel Kroe-Barrett |
author_facet | Danlin Yang Ajit Singh Helen Wu Rachel Kroe-Barrett |
author_sort | Danlin Yang |
collection | DOAJ |
description | Here we provide data from a head-to-head comparison study using four biosensor platforms: GE Healthcare׳s Biacore T100, Bio-Rad׳s ProteOn XPR36, ForteBio׳s Octet RED384, and Wasatch Microfluidics׳s IBIS MX96. We used these instruments to analyze the binding interactions of a panel of ten high-affinity monoclonal antibodies with their antigen, human proprotein convertase subtilisin kexin type 9 (PCSK9). For each instrument, binding curves obtained at multiple densities of surface antibodies were fit to the 1:1 Langmuir kinetic model, and the association and dissociation rate constants and corresponding affinity constants were calculated. The data supplied in this article accompany the research article entitled, “Comparison of biosensor platforms in the evaluation of high affinity antibody–antigen binding kinetics” (Yang et al., 2016) [1], which further discusses the strengths and weaknesses of each biosensor platform with an emphasis on data consistency, comparability, and operational efficiency. Keywords: Biacore, ProteOn, Octet, MX96, Antibody–antigen interactions, Optical biosensor |
first_indexed | 2024-12-14T16:28:32Z |
format | Article |
id | doaj.art-da62cba09ddb4d67ad9066a28e27132f |
institution | Directory Open Access Journal |
issn | 2352-3409 |
language | English |
last_indexed | 2024-12-14T16:28:32Z |
publishDate | 2016-09-01 |
publisher | Elsevier |
record_format | Article |
series | Data in Brief |
spelling | doaj.art-da62cba09ddb4d67ad9066a28e27132f2022-12-21T22:54:38ZengElsevierData in Brief2352-34092016-09-01811731183Dataset of the binding kinetic rate constants of anti-PCSK9 antibodies obtained using the Biacore T100, ProteOn XPR36, Octet RED384, and IBIS MX96 biosensor platformsDanlin Yang0Ajit Singh1Helen Wu2Rachel Kroe-Barrett3Department of Immune Modulation and Biotherapeutics Discovery, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT 06877, United StatesThe Fu Foundation School of Engineering and Applied Science, Columbia University, New York, United StatesDepartment of Immune Modulation and Biotherapeutics Discovery, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT 06877, United StatesDepartment of Immune Modulation and Biotherapeutics Discovery, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT 06877, United States; Correspondence to: Department of Immune Modulation and Biotherapeutics Discovery, Boehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road, Ridgefield, CT 06877-0368, United States.Here we provide data from a head-to-head comparison study using four biosensor platforms: GE Healthcare׳s Biacore T100, Bio-Rad׳s ProteOn XPR36, ForteBio׳s Octet RED384, and Wasatch Microfluidics׳s IBIS MX96. We used these instruments to analyze the binding interactions of a panel of ten high-affinity monoclonal antibodies with their antigen, human proprotein convertase subtilisin kexin type 9 (PCSK9). For each instrument, binding curves obtained at multiple densities of surface antibodies were fit to the 1:1 Langmuir kinetic model, and the association and dissociation rate constants and corresponding affinity constants were calculated. The data supplied in this article accompany the research article entitled, “Comparison of biosensor platforms in the evaluation of high affinity antibody–antigen binding kinetics” (Yang et al., 2016) [1], which further discusses the strengths and weaknesses of each biosensor platform with an emphasis on data consistency, comparability, and operational efficiency. Keywords: Biacore, ProteOn, Octet, MX96, Antibody–antigen interactions, Optical biosensorhttp://www.sciencedirect.com/science/article/pii/S2352340916304802 |
spellingShingle | Danlin Yang Ajit Singh Helen Wu Rachel Kroe-Barrett Dataset of the binding kinetic rate constants of anti-PCSK9 antibodies obtained using the Biacore T100, ProteOn XPR36, Octet RED384, and IBIS MX96 biosensor platforms Data in Brief |
title | Dataset of the binding kinetic rate constants of anti-PCSK9 antibodies obtained using the Biacore T100, ProteOn XPR36, Octet RED384, and IBIS MX96 biosensor platforms |
title_full | Dataset of the binding kinetic rate constants of anti-PCSK9 antibodies obtained using the Biacore T100, ProteOn XPR36, Octet RED384, and IBIS MX96 biosensor platforms |
title_fullStr | Dataset of the binding kinetic rate constants of anti-PCSK9 antibodies obtained using the Biacore T100, ProteOn XPR36, Octet RED384, and IBIS MX96 biosensor platforms |
title_full_unstemmed | Dataset of the binding kinetic rate constants of anti-PCSK9 antibodies obtained using the Biacore T100, ProteOn XPR36, Octet RED384, and IBIS MX96 biosensor platforms |
title_short | Dataset of the binding kinetic rate constants of anti-PCSK9 antibodies obtained using the Biacore T100, ProteOn XPR36, Octet RED384, and IBIS MX96 biosensor platforms |
title_sort | dataset of the binding kinetic rate constants of anti pcsk9 antibodies obtained using the biacore t100 proteon xpr36 octet red384 and ibis mx96 biosensor platforms |
url | http://www.sciencedirect.com/science/article/pii/S2352340916304802 |
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