Table 2.

Epitope binning of H7 monoclonal antibodies by biolayer interferometry

mAba	Saturating mAbb
	7B5	7E3	1A10	1E9	98	5A6	62	H5 2C6
7B5	0.0103	0.0133	0.0081	0.3313	0.3983	0.2563	0.1542	−0.0378
7E3	0.0097	0.0108	0.0085	0.3177	0.3918	0.2586	0.1542	−0.0368
1A10	−0.0022	−0.0013	0.0091	0.3324	0.404	0.2774	0.1763	−0.0271
1E9	0.2266	0.2311	0.2137	0.0176	0.0194	−0.0235	−0.0752	−0.1449
98	0.2775	0.278	0.2835	0.0551	0.0345	0.0211	−0.0629	−0.095
5A6	0.2009	0.1989	0.1799	0.0605	0.0686	0.014	−0.0752	−0.1967
62	0.288	0.2918	0.3048	0.1954	0.1578	0.1404	0.0142	−0.0544
H5 2C6	0.4263	0.4378	0.3934	0.3993	0.4355	0.3149	0.2337	−0.0039

^aCompeting mAb—Data presented is the raw nanometer shift caused by the binding of the competing antibody. To differentiate between competing antibodies that are blocked by the saturating antibody and those that are not, a threshold equal to the highest self‐binding signal in the panel is set: 0.0345 (mAb 98). The threshold value is then used to color‐code the matrix data in either red or green, to distinguish between competing antibodies that are or are not blocked by the saturating antibody.

^bSaturating mAb—H7 antigen was captured onto the SAX sensor surface using biotin tag and the loaded sensor first exposed to the indicated saturating mAb.