Galectin-1 human

Galectin-1 is a member of the family of animal lectins, which selectively binds β-galactoside residues.

A common function of galectins is to cross-link structures containing N-acetyl-lactosamine located at the cell surface and within the extracellular matrix. They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. They have variable affinity for more complex oligosaccharides. Other activities of galectin-1 include cell differentiation and inhibition of CD45 protein phosphatase activity.

Galectin-1 has been implicated in metastasis and aggregation of cancer cells based on its association with the glycoprotein 90K. Galectin-1 may play a significant role in cancer through apoptosis, cell adhesion and migration, regulation of the cell cycle and tumor evasion of immune responses.

Galectin-1 has been implicated in metastasis and aggregation of cancer cells based on its association with the glycoprotein 90K. Galectin-1 may play a significant role in cancer through apoptosis, cell adhesion, migration, cell cycle regulation and tumor evasion of immune responses.

Lyophilized from a 5 mg/mL solution in phosphate buffered saline containing 8 mM DTT and 150 mM lactose.