Differentiation of pluripotent cells to generate lentoid bodies is important for the understanding of the lens development and investigating the processes critical for lens morphogenesis. This Study was initiated to investigate a comprehensive proteome profiling of the peripheral blood mononuclear cell (PBMC)-originated, induced pluripotent stem cell (iPSC)-derived lentoid bodies through mass spectrometry-based protein sequencing. Briefly, a small aliquot of blood sample was ascertained to collect PBMCs that were reprogrammed to iPSCs using the Sendai-virus delivery system. The PBMC-originated, iPSCs were differentiated into lentoid bodies employing the “fried egg” method using feeder-free conditions. The quantitative real-time PCR (qRT-PCR) confirmed the expression of lens-associated markers, which exhibited at least an order magnitude increased expression in lentoid bodies at differentiation day 25. Subsequently, the total cellular protein was extracted from lentoid bodies at day 25, digested with trypsin, fractionated into 24 fractions and subjected to an mass spectrometry-based label-free quantitative proteomics. mass spectrometry-based proteome profiling revealed 9,473 proteins in iPSC-derived lentoid bodies at differentiation day 25. In here, we report a comprehensive proteome of PBMC-originated, iPSC-derived lentoid bodies at day 25, which will help in better understanding processes critical for the development of the ocular lens.