Lectins are proteins or glycoproteins of non immune origin which reversible and specific carbohydrate binding inducing cellular agglutination. These proteins are present in virus, bacteria, plants and animals. In invertebrates, lectins are involved in various defense processes. In this study, Lectins from the marine sponge Tedania ignis were extracted with 50mM Borax, pH 7.5 buffer. Supernatant obtained was submitted to fractionation with ammonium sulfate 0-30% saturation and the precipitated was resuspended in the same buffer and fractionated with acetone at 1.0 volume. This proceeding was followed by chromatography on Sepharose 6B and the retained peak was eluted with 50mM Borax, 0.1M EDTA, pH 7.5 buffer. Tedania ignis lectin (TIL-I) isolated showed higher agglutinating activity for B type erythrocytes treated with papain. Among the monosaccharides tested, galactose and manose were the most effective inhibitors of lectin hemagglutination at 25 and 50 mM, respectively. TIL-I showed a molecular mass around 45 kDa by SDS-PAGE and revealed to be Mn⁺⁺ dependent, stable at temperatures up to 70 ^oC for 1hour and optimum pH of 7.5.