I6034
α-L-Iduronidase human
recombinant, expressed in mouse NSO cells
Synonym(s):
IDUA
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recombinant
expressed in mouse NSO cells
Quality Level
form
solution
specific activity
≥7,500 units/μg protein
mol wt
83 kDa
impurities
≤1.0 EU/μg Endotoxin
shipped in
wet ice
storage temp.
−20°C
General description
α-L-Iduronidase (IDUA) is mapped to human chromosome 4p16.3. The mature IDUA protein is glycosylated and comprises triosephosphate isomerase (TIM) barrel domain, β-sandwich, helix-loop-helix region and an immunoglobin-like domain. α-L-Iduronidase is classified under glycoside hydrolase (GH) family 39.
Application
α-L-Iduronidase may be used for leukocyte assay in the study of a-L-Iduronidase deficiency in new born.
Biochem/physiol Actions
In lysosomal degradation process α-L-Iduronidase plays a crucial role. It hydrolyzes the non-reducing terminal α-L-iduronic acid residues in glycosaminoglycans (GAGs), including dermatan sulfate and heparan sulfate.
Mutation in the α-L-Iduronidase is implicated in Mucopolysaccharidosis I (MPS I) . This enzyme defect leades to accumulation of dermatan and heparan sulfate . MPS I pathophysiology is accompanied with deformation of the skull, mental retardation and hernias.
Catalyzes the hydrolysis of unsulfated α-L-iduronosidic linkages in dermatan sulfate
Physical properties
Expressed as C-terminal histine-tagged protein (residues 1-653) with a caluclated molecular mass of 71 kDa migrating at ~83 kDa under SDS-PAGE reducing conditions.
Unit Definition
One unit will produce 1 picomole of 4-methylumbelliferone from 4-methylumbelliferyl-α-L-iduronide per minute at pH 3.5 at 25 °C.
Physical form
Supplied as a solution in 40 mM sodium acetate , 400 mM NaCl and 20% (v/v) glycerol, pH 5.0
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Xu He et al.
Plant molecular biology, 79(1-2), 157-169 (2012-03-24)
Processes associated with late events of N-glycosylation within the plant Golgi complex are a major limitation to the use of plant-based systems to produce recombinant pharmaceutical proteins for parenteral administration. Specifically, sugars added to the N-glycans of a recombinant protein
Dan Wang et al.
Molecular genetics and metabolism, 105(1), 116-125 (2011-11-08)
Suppression therapy utilizes compounds that suppress translation termination at in-frame premature termination codons (PTCs) to restore full-length, functional protein. This approach may provide a treatment for diseases caused by nonsense mutations such as mucopolysaccharidosis type I-Hurler (MPS I-H). MPS I-H
Patricia I Dickson et al.
Molecular genetics and metabolism, 106(1), 68-72 (2012-03-10)
Intrathecal enzyme replacement therapy is an experimental option to treat central nervous system disease due to lysosomal storage. Previous work shows that MPS I dogs receiving enzyme replacement with recombinant human alpha-l-iduronidase into the cisterna magna showed normal brain glycosaminoglycan
Haiying Bie et al.
Nature chemical biology, 9(11), 739-745 (2013-09-17)
Mucopolysaccharidosis type I (MPS I), caused by mutations in the gene encoding α-L-iduronidase (IDUA), is one of approximately 70 genetic disorders collectively known as the lysosomal storage diseases. To gain insight into the basis for MPS I, we crystallized human
Min Jung Kwak et al.
BMC medical genetics, 17(1), 58-58 (2016-08-16)
Mucopolysaccharidosis I (MPS I) is an autosomal recessive lysosomal storage disorder caused by a lack of the lysosomal enzyme α-L-iduronidase (IDUA). To date, more than 200 IDUA mutations have been reported. However, only a few types of mutations are recurrent
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