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Lectins, glycoproteins with non-enzymatic and non-immunogenic origins, play essential roles in various biological processes. This study presents the purification and characterization of a lectin-like protein isolated from the seeds of Datura stramonium L., a member of the Solanaceae family. The purification of the lectin-like protein involved a dual method, employing both ammonium sulphate precipitation and anion exchange chromatography utilizing DEAE-Sepharose. Analysis via SDS-PAGE showed a distinct band, displaying an estimated molecular weight of approximately 30 kDa., indicative of the purified protein's homogeneity. Additionally, the purified protein exhibited hemagglutination activity towards human B and O red blood cells, underscoring its lectin-like properties. Periodic acid Schiff (PAS) staining confirmed the glycoprotein nature of the purified protein. Furthermore, its anti-proliferative activity against human cancer Caco-2 cell lines was evaluated through MTT assay, revealing promising results. This study elucidates the purification and characterization of a lectin-like protein from Datura stramonium L. seeds, providing valuable insights into its potential biological functions and diagnostic research applications.