Human Galectin-8/LGALS8 Recombinant Protein (RPES4696)

Human Galectin-8/LGALS8 Recombinant Protein

The Galectin family of lectins, which contain homologous carbohydrate recognition domains (CRDs), comprises beta-galactoside binding lectins with specificity for Nacetyllactosamine containing glycoproteins. They are also equipped with hemagglutination activity, which is due to their bivalent carbohydrate binding qualities. Galectins are present both inside and outside cells. Galectins, despite their lack of a classical signal peptide, can be secreted by one or more unknown non-classical secretory pathways. They have various effects on a variety of cellular activities including adhesion, migration, polarization, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may be involved in a variety of pathologies, including autoimmune diseases, allergic responses, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins are divided into the prototype galectins (1, 2, 5, 7, 10, 11, 13), which contain one CRD and exist as a monomer or a noncovalent homodimer. The chimera galectins (Galectin3) with one CRD linked to a non-lectin domain, and the tandem repeat Galectins (4, 6, 8, 9, 12) made up of two CRDs connected by a linker peptide. Galectins lack a typical signal peptide and are found in the cytosol, where they have intracellular roles. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly. Members of the galectin family have diverse tissue distribution profiles and vary in their carbohydrate-binding specificities. Each family member may preferentially bind to a specific group of cell surface glycoproteins. Human Galectin-8/LGALS8 Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.