<p>Protein A chromatography is widely used for antibody purification; however, conventional resins require low pH elution conditions that may compromise product stability. Recently, protein A resins enabling milder pH elution have been introduced to mitigate aggregation and fragmentation but may reduce recovery. This study evaluates the performance of a newly developed Protein A resin designed for mild pH elution, with the aim of achieving high recovery and impurity clearance simultaneously. The developed resin was compared with commercial Protein A resins using monoclonal antibodies and Fc-fusion proteins across elution pH conditions from 3.5 to 5.0. The developed resin enabled efficient elution at pH ≥ 4.5, whereas conventional Protein A resins showed no detectable elution peaks under these conditions. Across the tested pH range, the developed resin achieved high recovery (&gt; 98%) while maintaining low impurity levels, including reduced host cell protein and host cell DNA. Product quality was preserved, with low fragment levels (&lt; 3%) and high monomer (&gt; 96%) even at pH 5.0. Similar performance trends were observed for Fc-fusion proteins. Comparable virus clearance at pH 5.0 indicated higher elution pH did not affect viral removal. These results indicate that the developed resin enables high-yield purification under mild elution conditions while maintaining low impurity levels and preserving product quality. Efficient elution and high recovery across a broader pH range may provide an operational window for biopharmaceuticals purification processes. In addition, impurity removal at low elution pH conditions suggests the developed resin could reduce downstream polishing steps.</p>