Anti-GLB1/Beta-galactosidase antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

GLB1 also known as beta-galactosidase is an enzyme that catalyzes the hydrolysis of beta-galactosides into monosaccharides. The protein has a molecular mass of approximately 76 kDa. Researchers observe this enzyme expression in the lysosome where it functions to break down complex carbohydrates. Its activity depends on proper glycosylation and correct folding usually occurring within specific cellular compartments.

Biological function summary

GLB1 is integral to the degradation and recycling of glycoproteins and glycolipids in the cell. It forms part of the lysosomal enzyme complex responsible for processing macromolecules. Without its function the accumulation of substrates can occur affecting cellular metabolism. The enzyme ensures that metabolic waste is efficiently processed linking GLB1 to cellular homeostasis.

Pathways

Beta-galactosidase participates in the lysosomal storage and glycan metabolism pathways. It is important for the catabolism of glycoside forms of hormones and other biologically-active molecules. In these pathways GLB1 interacts with proteins such as hexosaminidase creating a network of lysosomal enzymes. These interactions enable coordinated degradation of glycoproteins maintaining balance within cellular systems.

Associated diseases and disorders

GLB1 mutations associate with conditions like GM1 gangliosidosis and Morquio syndrome type B. These are lysosomal storage disorders resulting from the accumulation of unmetabolized substrates. In these diseases hexosaminidase and other lysosomal enzymes show relationships with GLB1 illuminating complex interactions within cellular pathology. Therapeutic research aims to correct or enhance enzyme function seeking to alleviate disorder symptoms.