Anti-Galectin-8 antibody, Mouse monoclonal

Galectins specifically bind to β-galactosides. 15 mammalian galectins have been identified so far. Galectin 8 contains two CRDs connected by a short linker peptide.

Monoclonal Anti-Galectin 8 (mouse IgM isotype) is derived from the hybridoma VA-11.25 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a recombinant rat galectin 8.Galectins belong to a family of carbohydrate-binding proteins. Within this family of proteins, galectin 8 is unique, as it exists in many forms encoded by the same gene.

recombinant rat galectin 8.

Monoclonal Anti-galectin-8 antibody produced in mouse has been used for:

• immunoblotting
• immunocytochemistry
• enzyme linked immunosorbent assay (ELISA)

Galectins belong to a family of carbohydrate-binding proteins. These proteins share similarities in the carbohydrate recognition domain (CRD) and in their specificity for N-Acetyllactosamine-enriched glycoconjugates. The binding of galectins to saccharides modulates cell proliferation, cell death and cell migration, which are involved in cancer initiation and progression. Galectin 8 is a secreted protein that requires both of its CRDs to be active to modulate cell adhesion. It forms a complex with integrins and triggers integrin-mediated signaling cascades. On the contrary, excessive amounts of this protein negatively regulate cell adhesion by interacting with integrins. These signals assist in identifying regions available for cell adhesion and migration. It may be involved in neoplastic transformation.

The antibody has low cross-reactivity with galectin 3 and galectin 9.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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