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. Author manuscript; available in PMC: 2026 Sep 1.
Published in final edited form as: Carbohydr Res. 2026 Jun 26;567:110019. doi: 10.1016/j.carres.2026.110019

Fig. 5.

Fig. 5.

ELISA analysis of the binding of synthetic antibody glycoforms to their respective receptors. A) ELISA binding of trastuzumab glycoforms to FcγRIIIA. 0.5 μg/mL of FcγRIIIA V158 was coated in a 96 well plate overnight and allowed to bind with synthetic trastuzumab glycoforms in five-fold serial dilutions starting at a concentration of 3.0 μM. Observed EC50 values are 72 nM for GalNAc2-Trastuzumab (3) and 59 nM for G2-Trastuzumab (1). B) ELISA based C1q binding to h3F6-IgG glycoforms. C1q (5 μg/mL) was coated in a 96 well plate overnight and allowed to bind with homogeneous GalNAc2-3F6 (10) and G2–3F6 (8) glycoforms in four-fold serial dilutions starting at a concentration of 5.0 μM. C) ELISA binding of trastuzumab glycoforms to Siglec-2. 2 μg/mL of Siglec-2 was coated in a 96 well plate overnight and allowed to bind with homogeneous sialylated trastuzumab glycoforms (4 and 5) in three-fold serial dilutions starting at a concentration of 22 μM). Data are presented as mean ± s.d., n=3 biological replicates.