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anti-Human IDS Anticorps:
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Human Polyclonal IDS Primary Antibody pour IHC (p), IHC - ABIN449843
Keeratichamroen, Cairns, Wattanasirichaigoon, Wasant, Ngiwsara, Suwannarat, Pangkanon, Kuptanon, Tanpaiboon, Rujirawat, Liammongkolkul, Svasti: Molecular analysis of the iduronate-2-sulfatase gene in Thai patients with Hunter syndrome. dans Journal of inherited metabolic disease 2011
Dog (Canine) Monoclonal IDS Primary Antibody pour FACS, ICC - ABIN4321043
Bellesso, Salvalaio, Lualdi, Tognon, Costa, Braghetta, Giraudo, Stramare, Rigon, Filocamo, Tomanin, Moro: FGF signaling deregulation is associated with early developmental skeletal defects in animal models for mucopolysaccharidosis type II (MPSII). dans Human molecular genetics 2019
We also show that mucopolysaccharidosis type II patient fibroblasts harboring different mutations spanning the IDS gene exhibit perturbed FGF signaling-related markers expression. Our work opens a new venue to discover possible druggable novel key targets in mucopolysaccharidosis type II
Data demonstrate that iduronate sulfatase plays a critical role during early vertebrate development and its downregulation may be responsible for severe developmental defects, including a misshapen trunk and abnormal craniofacial cartilages.
Genetic analysis of 63 Chinese patients with mucopolysaccharidosis type II: Functional characterization of seven novel IDS variants
IDS structure revealed by X-ray crystallography provides essential insight into multiple mechanisms by which pathogenic mutations interfere with enzyme function, and a compelling explanation for severe Hunter syndrome phenotypes.
Study analyzed the genotype-phenotype relationship for 17 patients with mucopolysaccharidosis II and performed expression studies for 12 variants, nine of which have not been reported previously; speculated that very low or cell-type-specific IDS residual activity is sufficient to prevent the neuronal phenotype.
Study identified 16 novel mutations in the IDS gene and revealed that the severe type of mucopolysaccharidosis type II is strongly associated with large structural alteration of the gene.
Functional characterization of all the novel sequence variants identified in the study would be helpful to confirm the clinical significance and to determine the effect of these variations on the function of respective proteins (IDUA and IDS)
A splicing mutation, c.709-1G>A, was detected in the proband, for which his mother was heterozygous.
Extensive iduronate 2-sulfatase (Hunter syndrome) (IDS) gene deletions were identified in four mucopolysaccharidosis type II (MPSII) patients.
Two new mutations were discovered: p.K236N (c.708G>C) and p.Q80K (c.238C>A) which resulted in a severe phenotype and early death of Muccopolysaccharridosis Type II patients from Bulgaria and Macedonia.
p.Ser142Phe and p.Ile360Tyrfs*31 mutations caused the severe disease manifestation
This study evaluated a novel mutation in the IDS gene among 8 male Hunter syndrome patients; there was a quantitative deficiency of NK and B cell with normal responses in other immune parameters.
30 novel iduronate sulfatase mutations have been identified in mucopolysaccharidosis type II Latin American patients.
Identification of a splice site mutation in the IDS gene associated with mucopolysaccharidosis type II.
a novel (p.R468P) and five known (p.R88C, p.D148V, p.G224A, p.Y348X, and p.R468Q) IDS mutations were shown to result in proteins with little or no IDS activity and altered protein processing, when expressed in COS7 cells
A report of a novel IDS nonsense mutation resulting in mucopolysaccharidosis type II in several patients from a Chinese family.
genetically analyze patients with severe Hunter syndrome that showed a total deletion of the iduronate-2-sulphatase (IDS) gene
Family members with 3 generations of X-inactivation with Hunter syndrome have 1568A>G missence mutation in the IDS gene
LCR-initiated rearrangements at the IDS locus, completed with Alu-mediated recombination or non-homologous end joining
Hunter syndrome in Thailand is caused by a diverse set of defects affecting both IDS protein production and activity.
study describes a woman with mild manifestations of Hunter syndrome who gave birth to a daughter; both the mother and daughter carried the p.R443X mutation in exon 9 of the ID2S gene
The in vivo correction of heritable gene lesions at the RNA level operating via a correction mechanism akin to RNA-editing, was observed for IDS mutant transcript.
While the iduronate 2-sulfatase sp replacement results in increased enzyme secretion, the addition of the ApoB-BD allows efficient BBB transcytosis and restoration of sulphamidase activity in the brain of treated mice.
Iduronate-2-sulfatase (IDS) is localized in lysosomes in pancreatic islet cells and expression is regulated by glucose. IDS has a potential role in the normal pathway of lysosomal degradation of secretory peptides.
Ids crossing the blood-brain barrier corrects CNS defects in MPSII mice.
Iduronate-2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in this X-chromosome gene that result in enzymatic deficiency lead to the sex-linked Mucopolysaccharidosis Type II, also known as Hunter Syndrome. Iduronate-2-sulfatase has a strong sequence similarity with human arylsulfatases A, B, and C, and human glucosamine-6-sulfatase. Multiple alternatively spliced transcript variants that encode different protein isoforms have been described.
iduronate 2-sulfatase (Hunter syndrome)
, iduronate 2-sulfatase
, iduronate 2-sulfatase-like
, alpha-L-iduronate sulfate sulfatase
, iduronate 2-sulfatase 14 kDa chain
, iduronate 2-sulfatase 42 kDa chain
, iduronate sulfatase