An N-acetyl-D- lactosamine (LacNAc) specific lectin from tubers of Alocasia cucullata was purified by affinity chromatography on asialofetuin-linked amino activated silica. The pure lectin showed a single band in SDS-PAGE at pH 8.8 and was a homotetramer with a subunit molecular mass of 13.5 kDa and native molecular mass of 53 kDa. It was heat stable up to 55 degrees C for 15 min and showed optimum hemagglutination activity from pH 2 to 11. The lectin was affected by denaturing agents such as urea ( 2 M), thiourea (2 M) and guanidine -HCl (0.5 M) and did not require Ca2+ and Mn2+ for its activity. It was a potent mitogen at 10 mu g/ml towards human peripheral blood mononuclear cells with 50% growth inhibitory potential towards SiHa ( human cervix) cancer cell line at 100 mu g/ml.