Beta-galactosidase/GLB1 Protein, Human (HEK293, His)

The Beta-galactosidase (GLB1) protein functions as an enzyme that cleaves beta-linked terminal galactosyl residues from various substrates, including gangliosides, glycoproteins, and glycosaminoglycans. Despite lacking direct beta-galactosidase catalytic activity, GLB1 plays essential functional roles in elastogenesis, contributing to the formation of extracellular elastic fibers and the development of connective tissue. Intriguingly, GLB1 is identified as the elastin-binding protein (EBP), a crucial component of the non-integrin cell surface receptor found on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin-producing cells, GLB1 associates with tropoelastin intracellularly, serving as a recycling molecular chaperone that facilitates the secretion of tropoelastin and supports its assembly into elastic fibers. This multifaceted functionality positions GLB1 as a key player in both enzymatic processes and structural roles related to tissue development and maintenance.