Description
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, 1 bp deletion in exon 1 and 1 bp insertion in exon 1,
Disease:Adenocarcinoma
Product details:
We will provide viable cells that proliferate on revival.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-GNS, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--196°C, Appropriate long-term storage conditions--196°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The GNS protein also known as glucosamine (N-acetyl)-6-sulfatase is an enzyme with significant roles in the breakdown of glycosaminoglycans. Its molecular weight is around 63 kDa. GNS is frequently expressed in lysosomal compartments where it catalyzes the cleavage of sulfate groups from N-acetylglucosamine residues in heparan sulfate and other similar molecules. This process is critical for the degradation and recycling of complex carbohydrates in cells.
Biological function summary
Glucosamine (N-acetyl)-6-sulfatase activity influences cellular homeostasis by acting within the lysosomal hydrolase family. GNS participates in the breakdown and metabolism of glycosaminoglycans important for maintaining cellular integrity and signaling functions. It operates as a standalone enzyme rather than part of a larger complex. Through its enzymatic function GNS helps prevent the accumulation of partially degraded molecules inside lysosomes.
Pathways
Glucosamine (N-acetyl)-6-sulfatase activity plays a role in lysosomal storage pathways and in the catabolic processes of heparan sulfate. This enzyme works alongside other lysosomal proteins like iduronate sulfatase and alpha-L-iduronidase which are also involved in glycosaminoglycan degradation pathways. Proper function of these pathways is important for cellular waste management and nutrient recycling.
Altered GNS function relates to conditions such as mucopolysaccharidosis type IIID (Sanfilippo syndrome type D) and some forms of lysosomal storage diseases. Deficiencies in GNS disrupt normal lysosomal breakdown of glycosaminoglycans leading to accumulations that can cause cellular damage. This disorder often involves other metabolic proteins like heparan N-sulfatase and alpha-N-acetylglucosaminidase. Understanding the role of GNS offers insights into potential therapeutic approaches for related metabolic disorders.
