Description
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, 10 bp deletion in exon 4 and 1 bp insertion in exon 4,
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-IDS, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, 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.
Iduronate 2-sulfatase also known as IDS or iduronate 2-sulfatase protein is an enzyme responsible for hydrolyzing the 2-sulfate groups from the sugar iduronate in glycosaminoglycans (GAGs) such as dermatan sulfate and heparan sulfate. This action is necessary for the lysosomal degradation of GAGs. The IDS protein has a molecular mass of approximately 76 kDa and predominantly resides in lysosomes. It is widely expressed across human tissues but shows higher expression levels in cells involved with significant lysosomal activities.
Biological function summary
IDS functions to ensure proper breakdown and recycling of GAGs preventing their excessive accumulation. Although IDS acts independently its proper functioning complements other enzymes within the lysosomal degradation system. This lysosomal catabolic activity helps maintain cellular homeostasis as GAGs need controlled degradation for effective cell and tissue functions.
Pathways
IDS plays an important role in the lysosomal degradation pathway. By participating in the catabolism of GAGs IDS works alongside other enzymes such as alpha-L-iduronidase. This interaction is part of the larger lysosomal storage and cellular turnover pathways. These pathways are essential for cellular regulation and help prevent the buildup of undegraded molecules that can disrupt cellular functions.
Faulty IDS activity leads to mucopolysaccharidosis type II also known as Hunter syndrome. This disorder arises from defective GAG breakdown resulting in their accumulation causing various systemic symptoms. IDS is closely related to other lysosomal storage disorder proteins like arylsulfatase B as both enzymes collaborate in GAG degradation. Proper comprehension of IDS and its functioning aids in understanding therapeutic approaches to managing associated disorders.
