Galectin-1 (Gal-1) is canonically referred to as a ‘galactose-binding lectin’ with several mportant functional and structural characteristics in the immune system. As a target for pharmaceutical research that is gaining in its significance for cancer biology, it is surprising that studies have not focused on Gal-1 structures outside of the mammalian taxa. For this reason, a recombinant Zebrafish Galectin-1 (zGal-1) was utilised as a novel homologous model for hGal-1. On determining the zGal-1 3D structure, several insights were gained through a range of biochemical, biophysical and computational techniques. The results showed similarities between structural characteristics of the reduced forms of hGal-1 and zGal-1. A collection of glycan array data by in-house analysis and analysis of internet databases was also undertaken to evaluate the similarities and differences across vertebrate Galectins. Gal-1 binding glycan array profiles indicated its strong panhomologous affinity for numerous fucosylated and sulphated glycans.