Lectins are carbohydrate-binding proteins that can recognize various carbohydrates attached to proteins and lipids,  known as glycoconjugates, on cell surfaces and extracellular matrices. Galectins are a family of proteins first identified as galactoside-binding lectins in extracts of vertebrate tissue, and all share a common amino acid sequence, the carbohydrate recognition domain (CRD). They are known to perform a high diversity of functions inside the cells and in the extracellular space: they are regulators of cell cycle, inflammation, immune responses, cancer progression, cell adhesion, cell signalling events and so on. Regarding their overall structure galectins are clustered in three families: prototype galectins consisting of one CRD, chimera-type galectins with one CRD and a non-lectin domain (galectin-3), and tandem-repeat galectins which have two different CRDs linked by a short peptide[1]. Different galectins are specific for different oligosaccharides, as they differ in their ability to accommodate certain saccharides attached to galactose[2]. Evidence has accumulated that Galectin-1 and galectin-3 are also implicated in cancer cell proliferation, invasion and tumour angiogenesis. Galectin-1 is overexpressed in tumour cells and tumour-associated endothelial cells. Upregulation has been linked with poor clinical prognosis and metastases development in a wide range of malignancies[3].