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This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The determination of antigen-antibody affinity is essential in the development of biotherapeutics. However, high throughput methods for affinity analysis in physiologically relevant and complex matrices such as neat serum or plasma are needed. We developed a high throughput method for affinity determination in neat serum by solution equilibrium analysis using Meso Scale Discovery technology (MSD-SEA). Here we present the results obtained in the analysis of carlumab (CNTO 888), an anti-CCL2 neutralizing antibody which binds its target with high affinity. The affinity of carlumab to CCL2 in PBS was determined using surface plasmon resonance (SPR), kinetic exclusion assay (KEA), isothermal titration calorimetry (ITC) and MSD-SEA. The affinity of carlumab to CCL2 in sera was determined using MSD-SEA. The results obtained by SPR, KEA and ITC are in agreement with the results obtained by MSD-SEA. Importantly, the results obtained in PBS are in agreement with the results obtained in neat pooled human sera. This work demonstrates the use of MSD-technology as a tool for solution equilibrium affinity determinations in neat serum and highlights its potential for HTP analysis of high affinity therapeutic candidates using physiologically relevant conditions. CCL2 Antibody Carlumab Affinity Biacore ProteOn KinExA MSD Serum Eilyn R Lacy1* Deborah Kwok1 Audrey Baker4 Shobha Seetharam2 Shalini Chaturvedi3 Linda A Snyder3 and Gordon D Powers1 2018-01-31T18:44:28+05:30 2018-01-31T18:44:30+05:30 2018-01-31T18:44:30+05:30 5 Adobe InDesign CS6 (Windows) uuid:832b0a49-d369-4c46-897a-22c2541c48fc xmp.did:FE00469DB0C7E411AEB789ACBE3823B3 xmp.id:B05025928806E811B70A85AFBE9920D0 proof:pdf converted from application/x-indesign to application/pdf Adobe InDesign CS6 (Windows) / 2018-01-31T18:44:28+05:30 xmp.iid:AF5025928806E811B70A85AFBE9920D0 xmp.did:FE00469DB0C7E411AEB789ACBE3823B3 xmp.did:FE00469DB0C7E411AEB789ACBE3823B3 default Eilyn R Lacy, Biologics Research, Janssen Biotherapeutics (JBIO),Janssen Research and Development, Spring House, USA, Tel: 1-(215) 628-7148; Fax: 1- (215)540-4882; E-mail: elacy@its.jnj.com Citation: Lacy ER, Kwok D, Baker A, Seetharam S, Chaturvedi S, et al. (2016) Affinity of Carlumab for CC-Chemokine Ligand 2 (CCL2) in Neat Human Sera. 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65535 f 0000000000 65535 f 0000000000 65535 f 0000000000 65535 f 0000000000 65535 f 0000000000 65535 f trailer <]>> startxref 116 %%EOF 492 0 obj <>stream application/pdf Affinity of Carlumab for CC-ChemokineLigand 2 (CCL2) in Neat Human Sera © 2016 Lacy ER, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The determination of antigen-antibody affinity is essential in the development of biotherapeutics. However, high throughput methods for affinity analysis in physiologically relevant and complex matrices such as neat serum or plasma are needed. We developed a high throughput method for affinity determination in neat serum by solution equilibrium analysis using Meso Scale Discovery technology (MSD-SEA). Here we present the results obtained in the analysis of carlumab (CNTO 888), an anti-CCL2 neutralizing antibody which binds its target with high affinity. The affinity of carlumab to CCL2 in PBS was determined using surface plasmon resonance (SPR), kinetic exclusion assay (KEA), isothermal titration calorimetry (ITC) and MSD-SEA. The affinity of carlumab to CCL2 in sera was determined using MSD-SEA. The results obtained by SPR, KEA and ITC are in agreement with the results obtained by MSD-SEA. Importantly, the results obtained in PBS are in agreement with the results obtained in neat pooled human sera. This work demonstrates the use of MSD-technology as a tool for solution equilibrium affinity determinations in neat serum and highlights its potential for HTP analysis of high affinity therapeutic candidates using physiologically relevant conditions. CCL2 Antibody Carlumab Affinity Biacore ProteOn KinExA MSD Serum Eilyn R Lacy1* Deborah Kwok1 Audrey Baker4 Shobha Seetharam2 Shalini Chaturvedi3 Linda A Snyder3 and Gordon D Powers1 2018-01-31T18:44:28+05:30 2018-01-31T18:44:34+05:30 2018-01-31T18:44:34+05:30 5 Adobe InDesign CS6 (Windows) uuid:6e289157-db7d-4d1b-9c94-d83ab267b5a1 xmp.did:FE00469DB0C7E411AEB789ACBE3823B3 xmp.id:B05025928806E811B70A85AFBE9920D0 proof:pdf converted from application/x-indesign to application/pdf Adobe InDesign CS6 (Windows) / 2018-01-31T18:44:28+05:30 xmp.iid:AF5025928806E811B70A85AFBE9920D0 xmp.did:FE00469DB0C7E411AEB789ACBE3823B3 xmp.did:FE00469DB0C7E411AEB789ACBE3823B3 default Eilyn R Lacy, Biologics Research, Janssen Biotherapeutics (JBIO),Janssen Research and Development, Spring House, USA, Tel: 1-(215) 628-7148; Fax: 1- (215)540-4882; E-mail: elacy@its.jnj.com Citation: Lacy ER, Kwok D, Baker A, Seetharam S, Chaturvedi S, et al. (2016) Affinity of Carlumab for CC-Chemokine Ligand 2 (CCL2) in Neat Human Sera. J Biochem Analyt Stud 2(1): http://dx.doi.org/10.16966/2576-5833.106 Adobe PDF Library 10.0.1 False endstream endobj 493 0 obj <> endobj 2151 0 obj <>/Metadata 492 0 R/Names 2152 0 R/Outlines 416 0 R/PageMode/UseOutlines/Pages 491 0 R/StructTreeRoot 494 0 R/Type/Catalog/ViewerPreferences<>>> endobj xref 0 1 0000000000 65535 f 492 2 0000722310 00000 n 0000730454 00000 n 2151 1 0000732043 00000 n trailer <]/Prev 116>> startxref 732247 %%EOF