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IDUA encodes an enzyme that hydrolyzes the terminal alpha-L-iduronic acid residues of two glycosaminoglycans, dermatan sulfate and heparan sulfate. Additionally we are shipping IDUA Antibodies (59) and IDUA Kits (18) and many more products for this protein.
Showing 6 out of 12 products:
In the absence of Fgfrl1a, larvae fail to express the transcription factor glial cells missing 2 (gcm2 (show GCM2 Proteins)), a gene necessary for cartilage and gill filament formation, in the ectodermal lining of the branchial arches.
A new IDUA variant that alters the structure of the signal peptide associated with mucopolysaccharidosis type I is reported.
Amino acid substitutions in alpha-L-iduronidase determine the severity of mucopolysaccharidosis type I.
The alpha-L-iduronidase missense mutation causing L238Q substitution, when paired with a nonsense mutation, is associated with significant, late-onset brain disease.
We conclude that this procedure for determining residual IDUA activity in fibroblasts of MPS I patients may be helpful to predict MPS I phenotype.
The IDUA structures and biochemical analysis of the disease-relevant P533R mutation have enabled us to correlate the effects of mutations in IDUA to clinical phenotypes.
Data show that alpha-l-iduronidase (hIDUA) enzyme activity was highly correlated with the N-glycan attached to N372.
X-ray diffraction analysis of human alpha-L-iduronidase
Transfer of a high level of human alpha-L-iduronidase gene into the central nervous system (CNS) of MPS I mutant mice susceptible to mucopolysaccharidosis (MPS) improves the outcome for MPS when a high level of CNS gene expression is achieved.
A previously unreported IDUA splice site mutation (NG_008103.1:g.21632G>C; NM_000203.3:c.1727+3G>C) causing a Hurler phenotype in a patient heterozygous for the common p.Q70X (NG_008103.1:g.5862C>T) mutation.
This paper, showed a heterogeneous pattern of mutations and polymorphisms in the IDUA gene among Tunisian patients.
This study demonstrated that the distribuation of bis (show BAG3 Proteins)(monoacylglycero)phosphate in brain of mucopolysaccharidosis 1 (Hurler) mouse.
Mucopolysaccharidosis type I, unique structure of accumulated heparan sulfate and increased N-sulfotransferase activity in mice lacking alpha-l-iduronidase.
Studies show that mouse Idua-W392X mutation is analogous to the human IDUA-W402X mutation commonly found in MPS I-H patients.
Data show that late-stage erythroid cells, transduced with a tissue-specific lentiviral vector, can deliver alpha-L-iduronidase continuously and can correct the disease phenotype in both viscera and CNS of MPS I mice.
The results indicate that Idua(-/-) mice present deficits in long-term memory for aversive training and reduced exploratory behavior.
IDUA(-/-) mice from adolescence to maturity, exhibited locomotor and anxiety-like compulsive behaviors, spatial learning and memory, visual recognition and short-term non-associative memory retention.
This gene encodes an enzyme that hydrolyzes the terminal alpha-L-iduronic acid residues of two glycosaminoglycans, dermatan sulfate and heparan sulfate. This hydrolysis is required for the lysosomal degradation of these glycosaminoglycans. Mutations in this gene that result in enzymatic deficiency lead to the autosomal recessive disease mucopolysaccharidosis type I (MPS I).
, fibroblast growth factor receptor-like 1