AGA Human, sf9
Description
Product Specs
Product Science Overview
Aspartylglucosaminidase (AGA) is an enzyme that plays a crucial role in the catabolism of N-linked oligosaccharides of glycoproteins. This enzyme is involved in the lysosomal breakdown of glycoproteins by cleaving asparagine from N-acetylglucosamines . The recombinant form of this enzyme, produced in Sf9 Baculovirus cells, is known as Aspartylglucosaminidase (Human Recombinant, sf9).
The recombinant AGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids, with a molecular mass of approximately 35.7 kDa . The enzyme is expressed with a 6-amino acid His tag at the C-terminus and is purified using proprietary chromatographic techniques . The physical appearance of the recombinant AGA is a sterile, filtered colorless solution, formulated in phosphate-buffered saline (pH 7.4) with 10% glycerol .
Aspartylglucosaminidase is an amidohydrolase enzyme that facilitates the catabolism of N-linked oligosaccharides of glycoproteins . It cleaves the asparagine residue from N-acetylglucosamines, which is one of the final steps in the lysosomal degradation of glycoproteins . This process is essential for the proper recycling of glycoproteins within the cell.
A deficiency in AGA activity leads to a lysosomal storage disorder known as aspartylglycosaminuria (AGU) . This genetic disorder results in the accumulation of glycoasparagines in the lysosomes, leading to various clinical symptoms, including developmental delay, intellectual disability, and skeletal abnormalities .
The recombinant AGA should be stored at 4°C if it will be used within 2-4 weeks. For longer storage periods, it is recommended to store the enzyme frozen at -20°C, with the addition of a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) to enhance stability . It is important to avoid multiple freeze-thaw cycles to maintain the enzyme’s activity .
Recombinant AGA is primarily used for laboratory research purposes. It is utilized in studies related to glycoprotein metabolism, lysosomal storage disorders, and enzyme replacement therapies . The enzyme’s ability to cleave asparagine from N-acetylglucosamines makes it a valuable tool for understanding the biochemical pathways involved in glycoprotein degradation.
