Recombinant Human Iduronate 2 sulfatase/SIDS protein (GST tag N-Terminus)
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Recombinant Human Iduronate 2 sulfatase/SIDS protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 312 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
SIDS, IDS, Iduronate 2-sulfatase, Alpha-L-iduronate sulfate sulfatase, Idursulfase
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Iduronate 2 sulfatase/SIDS protein (GST tag N-Terminus) (AB158721)
ab158721 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
Specifications
Form
Liquid
General info
Function
Lysosomal enzyme involved in the degradation pathway of dermatan sulfate and heparan sulfate.
Sequence similarities
Belongs to the sulfatase family.
Post-translational modifications
Synthesized as a 75-kDa precursor form in the endoplasmic reticulum (ER), and then processed by proteolytic cleavage through various intermediates to yield a 55-kDa mature form, with the release of an 18 kDa polypeptide.. The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Subcellular localisation
Lysosome
Target data
Product promise
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