Lectins are a heterogeneous group of carbohydrate-binding proteins that vary in size, structure, molecular organization, and binding patterns. They evoke diverse biological responses by specifically binding to cell surface glycans and function as recognition molecules. In this study, a lectin from the fruit of Phyllanthus reticulatus was purified using mucin-affinity chromatography. The Phyllanthus reticulatus lectin (PRL) is non-specific to blood groups, with its hemagglutination activity strongly inhibited by asialo-mucin and weakly inhibited by mucin, fetuin, asialo-fetuin, and ovalbumin. The purified PRL exists in a monomeric form and has an estimated molecular weight of approximately 36 kDa (as determined by SDS-PAGE) and 35.07 kDa (as determined by ESI-Q-TOF-MS/MALDI-TOF-MS). The hemagglutination activity of PRL remains stable at an acidic pH of 4.2 and at temperatures up to 60 °C. Glycan array analysis revealed a fine sugar specificity towards fucose and fucose-containing complex glycans. Notably, PRL exhibited a dose-dependent cytotoxic effect on T47D and SKBR3 breast cancer cell lines by inducing apoptosis, as assessed through MTT assay and annexin V/PI staining. These results suggest that PRL is a novel plant lectin with strong apoptotic effects on breast cancer cell lines and distinct carbohydrate specificity, highlighting its potential significance in cancer glycobiology.