Recombinant Human Alpha-L-iduronidase (IDUA)

Code CSB-YP011000HU
Size $250
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
IDUA; Alpha-L-iduronidase; EC
Homo sapiens (Human)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

The IDUA (alpha-L-iduronidase) protein is a lysosomal enzyme that exists as a dimer and is essential for the degradation of glycosaminoglycans (GAGs) such as dermatan sulfate and heparan sulfate [1]. Mutations affecting the enzyme activity of IDUA can lead to mucopolysaccharidosis type I (MPS I), a lysosomal storage disorder characterized by the accumulation of GAGs [2]. The IDUA enzyme activity is typically measured using a fluorometric enzymatic assay, which quantifies the conversion of 4-methylumbelliferyl-α-L-iduronide to 4-methylumbelliferone [3]. The specific activity of the IDUA enzyme is crucial, as it determines the effectiveness of therapeutic interventions. For instance, the high brain uptake of a fusion protein containing IDUA can lead to a significant normalization of brain IDUA enzyme activity following administration [4].

Furthermore, the IDUA protein is subject to genetic variations, and mutations affecting its activity have been identified in patients with MPS I [5]. These mutations can significantly reduce the enzyme activity of IDUA, leading to the manifestation of MPS I symptoms [5]. Additionally, the IDUA protein can be engineered into fusion proteins, such as the HIRMAb-IDUA fusion protein, to enhance its targeted delivery across the blood-brain barrier [6]. This targeted delivery is crucial for the treatment of neurological manifestations of MPS I, as it allows for the restoration of IDUA enzyme activity in the brain [7].

In summary, the IDUA protein is a critical lysosomal enzyme involved in the degradation of GAGs, and its enzyme activity is essential for maintaining cellular homeostasis. Mutations affecting the enzyme activity of IDUA can lead to the development of MPS I, highlighting the significance of understanding the protein's function and its potential therapeutic applications.

[1] R. Boado, E. Hui, J. Lu, Q. Zhou, & W. Pardridge, "Reversal of lysosomal storage in brain of adult mps-i mice with intravenous trojan horse-iduronidase fusion protein", Molecular Pharmaceutics, vol. 8, no. 4, p. 1342-1350, 2011.
[2] G. Lee-Chen, S. Lin, Y. Tang, & Y. Chin, "Mucopolysaccharidosis type i: characterization of novel mutations affecting α‐ l‐iduronidase activity", Clinical Genetics, vol. 56, no. 1, p. 66-70, 1999.
[3] C. Janson, L. Romanova, P. Leone, Z. Nan, L. Belur, R. Mclvoret al., "Comparison of endovascular and intraventricular gene therapy with adeno-associated virus–α-l-iduronidase for hurler disease", Neurosurgery, vol. 74, no. 1, p. 99-111, 2014.
[4] R. Boado, E. Hui, J. Lu, & W. Pardridge, "Agt-181: expression in cho cells and pharmacokinetics, safety, and plasma iduronidase enzyme activity in rhesus monkeys", Journal of Biotechnology, vol. 144, no. 2, p. 135-141, 2009.
[5] D. Liu, Z. Jiang, L. Deng, H. Li, & H. Jiang, "Identification of an α‐l‐iduronidase (idua) m1t mutation in a chinese family with autosomal recessive mucopolysaccharidosis i", Annals of the New York Academy of Sciences, vol. 1526, no. 1, p. 114-125, 2023.
[6] R. Boado, Y. Zhang, Y. Zhang, C. Xia, Y. Wang, & W. Pardridge, "Genetic engineering of a lysosomal enzyme fusion protein for targeted delivery across the human blood‐brain barrier", Biotechnology and Bioengineering, vol. 99, no. 2, p. 475-484, 2007.
[7] R. Boado and W. Pardridge, "Brain and organ uptake in the rhesus monkey in vivo of recombinant iduronidase compared to an insulin receptor antibody–iduronidase fusion protein", Molecular Pharmaceutics, vol. 14, no. 4, p. 1271-1277, 2017.

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Target Background

Gene References into Functions
  1. Enzyme activities (acid alpha-glucosidase (GAA), galactocerebrosidase (GALC), glucocerebrosidase (GBA), alpha-galactosidase A (GLA), alpha-iduronidase (IDUA) and sphingomyeline phosphodiesterase-1 (SMPD-1)) were measured on ~43,000 de-identified dried blood spot (DBS) punches, and screen positive samples were submitted for DNA sequencing to obtain genotype confirmation of disease risk PMID: 27238910
  2. Using lysosomal storage disease mucopolysaccharidosis type I (MPS I) dogs tolerized to human IDUA as neonates, we evaluated intrathecal delivery of an adeno-associated virus serotype 9 vector expressing human IDUA as a therapy for the central nervous system manifestations of MPS PMID: 27386755
  3. IDUA deletion mutation is associate with with mucopolysaccharidosis type I . PMID: 28604952
  4. 10 unrelated Korean patients with Mucopolysaccharidosis I, p.L346R and c.704ins5 were most commonly found in Korean patients with Mucopolysaccharidosis I. PMID: 27520059
  5. Molecular studies results unveiled the predominance of(Pro533Arg) IDUA variation in a series of 13 Algerian patients with Mucopolysaccharidosis Type I presented mainly with an attenuated phenotype. PMID: 27196898
  6. A new IDUA variant that alters the structure of the signal peptide associated with mucopolysaccharidosis type I is reported. PMID: 25256405
  7. Amino acid substitutions in alpha-L-iduronidase determine the severity of mucopolysaccharidosis type I. PMID: 24480078
  8. The alpha-L-iduronidase missense mutation causing L238Q substitution, when paired with a nonsense mutation, is associated with significant, late-onset brain disease. PMID: 24368159
  9. We conclude that this procedure for determining residual IDUA activity in fibroblasts of MPS I patients may be helpful to predict MPS I phenotype. PMID: 23786846
  10. 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. PMID: 24036510
  11. Data show that alpha-l-iduronidase (hIDUA) enzyme activity was highly correlated with the N-glycan attached to N372. PMID: 23959878
  12. X-ray diffraction analysis of human alpha-L-iduronidase PMID: 23143250
  13. 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. PMID: 21397026
  14. 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. PMID: 21831683
  15. This paper, showed a heterogeneous pattern of mutations and polymorphisms in the IDUA gene among Tunisian patients. PMID: 21521498
  16. this study characterized the underlying IDUA mutations in a group of 102 newly studied European patients, including 37 Italians, whose condition has been clinically and biochemically diagnosed as MPS I. PMID: 21394825
  17. The identification of two novel alpha-L-iduronidase mutations should facilitate prenatal diagnosis and counseling for MPS I in Tunisia. PMID: 21639919
  18. study describes monozygotic twins with an attenuated form of mucopolysaccharidosis type I associated with a novel mutation of IDUA, who both showed cervical myelopathy as the initial and cardinal manifestation PMID: 21176924
  19. This study reports a novel mutation in IDUA, expanding the mutational spectrum for mucopolysaccharidosis type I. PMID: 21364962
  20. Studies show that mouse Idua-W392X mutation is analogous to the human IDUA-W402X mutation commonly found in MPS I-H patients. PMID: 19751987
  21. This is the first report of IDUA mutations in Egyptian patients with mucopolysaccharidosis type I. PMID: 19839758
  22. Results show that leukocyte IDUA from mucopolysaccharidosis I heterozygotes differs from the normal enzyme in terms of optimum pH, Km, Vmax and thermostability at 50 degrees C. PMID: 11825626
  23. Ninety percent of the MPS I patients in this study were genotyped and revealed 10 recurrent and thirteen novel IDUA gene mutations. PMID: 12559846
  24. 6 new mutations, c.1087C>T (p.R363C), c.1804T>A (p.F602I), c.793G>C, c.712T>A (p.L238Q), c.1727+2T>A, & c.1269C>G (p.S423R), in a total of 14 different mutations, & 13 polymorphisms , including the new c.246C>G (p.H82Q), were found in 10 MPS I pts. PMID: 15300847
  25. Model provides insights into why certain point mutations produce misfolded proteins and lead to severe mucopolysaccharidosis I, while other mutations produce proteins with minor structural perturbations and therefore the attenuated form of the disease. PMID: 15862278
  26. analysis of Alpha-L-Iduronidase mutations in Mucopolysaccharidosis I in Tunisia PMID: 16435195
  27. Describe a cohort of 14 Hurler-Scheie patients homozygous for the p.Leu490Pro missense mutation in the alpha-L-iduronidase gene. PMID: 17570076
  28. Analysis of the structural change in alpha-L-iduronidase of the severe mucopolysaccharidosis type I (MPS I) group and that of the attenuated disease, except for a couple of mutations, can help to predict the clinical outcome of MPS I. PMID: 18340403
  29. Mutations in the 130 C-terminal amino acids lead to clinical manifestations of Mucopolysaccharidosis type I , which indicates a functional importance of the C-terminus of the IDUA protein. PMID: 19396826

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Involvement in disease
Mucopolysaccharidosis 1H (MPS1H); Mucopolysaccharidosis 1H/S (MPS1H/S); Mucopolysaccharidosis 1S (MPS1S)
Subcellular Location
Protein Families
Glycosyl hydrolase 39 family
Tissue Specificity
Database Links

HGNC: 5391

OMIM: 252800

KEGG: hsa:3425

STRING: 9606.ENSP00000247933

UniGene: Hs.89560

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