Recombinant Human Alpha-L-iduronidase (IDUA)

Code: CSB-EP011000HUa2

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Size:

20ug100ug1mg

US$224

Quantity:

Express system: E.coli

Species: Homo sapiens (Human)

Tag Info: N-terminal 6xHis-SUMO-tagged

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Product Details
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Target Background

Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Activity

Not Test

Target Names

IDUA

Uniprot NO.

P35475

Research Area

Metabolism

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

28-653aa

Target Protein Sequence

APHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

82.9 kDa

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal 6xHis-SUMO-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

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.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Storage Condition

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.

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.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Troubleshooting and FAQs

Protein FAQs

Datasheet & COA

Please contact us to get it.

Images

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Customer Reviews and Q&A

■ Customer Reviews

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Target Background

Gene References into Functions

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
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
IDUA deletion mutation is associate with with mucopolysaccharidosis type I . PMID:28604952
10 unrelated Korean patients with Mucopolysaccharidosis I, p.L346R and c.704ins5 were most commonly found in Korean patients with Mucopolysaccharidosis I. PMID:27520059
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
A new IDUA variant that alters the structure of the signal peptide associated with mucopolysaccharidosis type I is reported. PMID:25256405
Amino acid substitutions in alpha-L-iduronidase determine the severity of mucopolysaccharidosis type I. PMID:24480078
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
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
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
Data show that alpha-l-iduronidase (hIDUA) enzyme activity was highly correlated with the N-glycan attached to N372. PMID:23959878
X-ray diffraction analysis of human alpha-L-iduronidase PMID:23143250
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
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
This paper, showed a heterogeneous pattern of mutations and polymorphisms in the IDUA gene among Tunisian patients. PMID:21521498
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
The identification of two novel alpha-L-iduronidase mutations should facilitate prenatal diagnosis and counseling for MPS I in Tunisia. PMID:21639919
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
This study reports a novel mutation in IDUA, expanding the mutational spectrum for mucopolysaccharidosis type I. PMID:21364962
Studies show that mouse Idua-W392X mutation is analogous to the human IDUA-W402X mutation commonly found in MPS I-H patients. PMID:19751987
This is the first report of IDUA mutations in Egyptian patients with mucopolysaccharidosis type I. PMID:19839758
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
Ninety percent of the MPS I patients in this study were genotyped and revealed 10 recurrent and thirteen novel IDUA gene mutations. PMID:12559846
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
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
analysis of Alpha-L-Iduronidase mutations in Mucopolysaccharidosis I in Tunisia PMID:16435195
Describe a cohort of 14 Hurler-Scheie patients homozygous for the p.Leu490Pro missense mutation in the alpha-L-iduronidase gene. PMID:17570076
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
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