Alpha-Galactosidase Human Recombinant
Galactosidase-Beta 1 E.coli Recombinant
Galactosidase-Beta 1 Human Recombinant
GLB1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 662 amino acids (24-677 a.a.) and having a molecular mass of 74.6 kDa.
GLB1 is fused to an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Alpha-Galactosidase E.coli Recombinant
N-Acetylgalactosaminidase Alpha Human Recombinant
Galactosidases are enzymes (glycoside hydrolases) that catalyze the hydrolysis of galactosides into monosaccharides . They are classified into two main types based on the glycosidic linkage they hydrolyze: alpha-galactosidase and beta-galactosidase . Alpha-galactosidase hydrolyzes substrates containing α-galactosidic residues, such as glycosphingolipids or glycoproteins . Beta-galactosidase, on the other hand, breaks down the disaccharide lactose into glucose and galactose .
Key Biological Properties: Galactosidases possess both hydrolytic and transgalactosylation properties . They are essential for the breakdown of complex carbohydrates into simpler sugars.
Expression Patterns and Tissue Distribution: Beta-galactosidase is widely expressed in various tissues, including the liver, kidneys, and intestines . Alpha-galactosidase is predominantly found in lysosomes and is encoded by the GLA gene .
Primary Biological Functions: Galactosidases play a crucial role in carbohydrate metabolism by breaking down galactosides into monosaccharides . This process is vital for energy production and carbon sourcing.
Role in Immune Responses and Pathogen Recognition: Galactosidases are involved in the degradation of glycoproteins and glycolipids, which can influence immune responses and pathogen recognition .
Mechanisms with Other Molecules and Cells: Galactosidases catalyze the hydrolysis of glycosidic bonds through a double-displacement mechanism . This involves the transfer of a sugar residue from a glycosyl donor to an acceptor.
Binding Partners and Downstream Signaling Cascades: Beta-galactosidase interacts with various substrates, including lactose, ganglioside GM1, and lactosylceramides . These interactions can trigger downstream signaling cascades that regulate metabolic processes.
Transcriptional Regulation: The expression of beta-galactosidase is regulated by the lac operon in bacteria, which is activated in the presence of lactose and repressed when glucose levels are sufficient .
Post-Translational Modifications: Galactosidases undergo various post-translational modifications, including glycosylation, which can affect their stability and activity .
Biomedical Research: Galactosidases are used as biomarkers in gene expression studies and enzyme-linked immunosorbent assays (ELISAs) .
Diagnostic Tools: Beta-galactosidase is employed in diagnostic assays for lactose intolerance and other metabolic disorders .
Therapeutic Strategies: Alpha-galactosidase is used in enzyme replacement therapy for Fabry disease, a genetic disorder caused by the deficiency of this enzyme .
Development to Aging and Disease: Galactosidases play a significant role throughout the life cycle. During development, they are involved in the breakdown of maternal milk lactose in infants . In adults, they aid in the digestion of dietary lactose and other galactosides . Deficiencies in galactosidase activity can lead to metabolic disorders such as galactosialidosis and Morquio B syndrome .