IDS Antibody
Iduronate 2-Sulfatase, Alpha-L-Iduronate Sulfate Sulfatase, Idursulfase, SIDS, Iduronate 2-Sulfatase 14 KDa Chain, Iduronate 2-Sulfatase 42 KDa Chain, Hunter Syndrome, EC 3.1.6.13, MPS2, Iduronate 2-sulfatase, Alpha-L-iduronate sulfate sulfatase, Idursulfase.
Description
Product Specs
Iduronate 2-Sulfatase, also known as IDS, is a member of the highly conserved sulfatase enzyme family. These enzymes catalyze the hydrolysis of O-sulfate and N-sulfate esters from various substrates. IDS plays a crucial role in the lysosomal degradation of the glycosaminoglycans (GAGs) heparan sulfate and dermatan sulfate. Specifically, IDS facilitates the hydrolysis of the 2-sulfate group present in the iduronate 2-sulfate (IDS) units of these GAGs.
The formulation contains 1mg/ml of IDS antibody in a buffer solution of PBS at pH 7.4, supplemented with 10% glycerol and 0.02% sodium azide.
This antibody has undergone rigorous testing using ELISA, Western blot analysis, and FACS analysis to confirm its specificity and reactivity. However, optimal results may vary depending on the specific application. Therefore, it is recommended to perform a titration with the reagent for each individual experiment to determine the most effective concentration.
Iduronate 2-Sulfatase, Alpha-L-Iduronate Sulfate Sulfatase, Idursulfase, SIDS, Iduronate 2-Sulfatase 14 KDa Chain, Iduronate 2-Sulfatase 42 KDa Chain, Hunter Syndrome, EC 3.1.6.13, MPS2, Iduronate 2-sulfatase, Alpha-L-iduronate sulfate sulfatase, Idursulfase.
IDS antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
PAT6H4AT.
Anti-human IDS mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IDS protein 26-550 amino acids purified from insect cell.
Mouse IgG2b heavy chain and k light chain.
Product Science Overview
Iduronate 2-Sulfatase is a member of the sulfatase family, sharing strong sequence similarity with other human sulfatases such as arylsulfatases A, B, and C . The enzyme’s primary function is to hydrolyze the 2-sulfate esters of iduronic acid residues in glycosaminoglycans . This hydrolysis is essential for the normal breakdown and recycling of these complex molecules within lysosomes.
Mutations in the IDS gene result in the production of a non-functional enzyme, leading to the progressive accumulation of undegraded glycosaminoglycans in various tissues and organs . This accumulation causes the symptoms associated with Hunter Syndrome, which include developmental delays, organomegaly, and skeletal abnormalities . The severity of the disease can vary widely, with some individuals experiencing mild symptoms and others facing severe complications.
Current therapeutic strategies for Hunter Syndrome include enzyme replacement therapy (ERT) with recombinant IDS, such as idursulfase . However, these treatments are limited in their ability to cross the blood-brain barrier, making them less effective for addressing central nervous system symptoms . Research is ongoing to develop novel therapies that can overcome this limitation, such as IDS fused with anti-human transferrin receptor antibodies, which have shown promise in preclinical studies .
Mouse anti-human IDS antibodies are valuable tools in scientific research and clinical diagnostics . These antibodies are used in various applications, including Western blotting, immunohistochemistry, immunocytochemistry, flow cytometry, and ELISA . They help detect and quantify IDS in human samples, facilitating the study of IDS function and the diagnosis of Hunter Syndrome .
