Analytical Data
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Gene name
IDS
- Application
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Alternative Names
IDS;SIDS;Iduronate 2-sulfatase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22304
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Expression Region
26-550aa
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AA Sequence
SETQANSTTDALNVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQ NAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFSTIPQYFKE NGYVTMSVGKVFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPD GELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGY HKPHIPFRYPKEFQKLYPLENITLAPDPEVPDGLPPVAYNPWMDIRQRED VQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLAN STIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEAGE KLFPYLDPFDSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPVP SFHVELCREGKNLLKHFRFRDLEEDPYLPGNPRELIAYSQYPRPSDIPQW NSDKPSLKDIKIMGYSIRTIDYRYTVWVGFNPDEFLANFSDIHAGELYFV DSDPLQDHNMYNDSQGGDLFQLLMPLEHHHHHH
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Molecular Weight
60 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
IDS (Iduronate-2-sulfatase) is an enzyme crucial for the degradation of glycosaminoglycans, particularly in the lysosomal storage disease known as Hunter syndrome (Mucopolysaccharidosis II). The dysfunction of IDS leads to the accumulation of glycosaminoglycans in various tissues, resulting in severe clinical manifestations such as developmental delay, symptomatic skeletal abnormalities, and cardiovascular issues. Researchers have focused on IDS as a potential therapeutic target for enzyme replacement therapy (ERT), which aims to supplement the deficient enzyme in affected patients. Recent developments in recombinant DNA technology have enabled the production of IDS in various expression systems, enhancing its availability for clinical use. The study of IDS also extends to its structural biology to understand the enzyme's function and interactions at a molecular level. Insights gained from these studies provide a foundation for developing advanced therapeutic strategies, including gene therapy and substrate reduction therapy, offering hope for improved treatment outcomes for patients with Hunter syndrome. Understanding the protein’s folding, stability, and interaction with other cellular components is key to optimizing these therapeutic approaches, making IDS a significant focus of research in lysosomal storage disorders.
