Recombinant Human Aspartoacylase(ASPA)

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Code CSB-YP002223HU
Size US$1916Purchase it in Cusabio online store
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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

Purity Greater than 85% as determined by SDS-PAGE.
Target Names ASPA
Uniprot No. P45381
Research Area Signal Transduction
Alternative Names ACY 2; ACY-2; ACY2; ACY2_HUMAN; Aminoacylase 2; Aminoacylase-2; Aminoacylase2; ASP; ASPA; Aspartoacylase (aminoacylase 2; Canavan disease); Aspartoacylase (Canavan disease); Aspartoacylase; NUR 7; NUR7; OTTMUSP00000006437; RP23-213I10.1; Small lethargic
Species Homo sapiens (Human)
Source Yeast
Expression Region 1-313aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 39.7 kDa
Protein Length Full Length
Tag Info N-terminal 10xHis-tagged and C-terminal Myc-tagged
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.
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.
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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein 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 3-7 business days
Notes 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.

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Target Background

Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids.
Gene References into Functions
  1. report of 2 Egyptian sibling patients suspected of Canavan disease (CD); study revealed homozygosity for substitution T530C (Ile177Thr) in exon 4 of the ASPA gene in both sibs; substitution T530C (Ile177Thr) results in a novel missense mutation causing a CD phenotype with severe clinical characteristics PMID: 24036223
  2. Four ASPA missense mutations associated with Canavan disease are structurally characterized. PMID: 25003821
  3. Definitive evidence is presented to show that the recombinantly-expressed human aspartoacylase is not a glycoprotein. PMID: 24632142
  4. This is the first case report of ASPA mutation studies in Canavan disease from Indian subcontinent. PMID: 22878930
  5. a novel mutation Y88X within the aspartoacylase gene in a consanguineous family with an affected child diagnosed as Canavan disease. PMID: 22468686
  6. Human aspartoacylase gene expression was high not only in brain and kidney, but also in lung and liver. PMID: 22750302
  7. Gene ASPA (NM_000049) was undertaken to sequence for mutation analysis. PMID: 22219087
  8. We report on an Italian female patient with Canavan disease due to a missense mutation of the aspartoacylase gene and a 17p13.3 chromosomal microdeletion PMID: 22019069
  9. the ASPA gene was analysed in 22 unrelated non-Jewish patients with Canavan disease, and 24 different mutations were found PMID: 12638939
  10. Mild-onset presentation of Canavan's disease associated with novel G212A point mutation in aspartoacylase gene PMID: 16437572
  11. molecular weight of the purified enzyme is higher than predicted, suggesting the presence of post-translational modifications. Deglycosylation of aspartoacylase or mutation at glycosylation site causes decreased enzyme stability and catalytic activity PMID: 16669630
  12. a green fluorescent protein-human ASPA fusion protein larger than the permissible size for the nuclear pore complex was enzymatically active and showed mixed nuclear-cytoplasmic distribution. PMID: 16935940
  13. The finding that wild-type and Glu178Asp have the same K(m) but different k(cat) values confirms the idea that the carboxylate group contributes importantly to the enzymatic activity of aspartoacylase. PMID: 17027983
  14. the N-terminal domain of aspartoacylase adopts a protein fold similar to that of zinc-dependent hydrolases related to carboxypeptidases A PMID: 17194761
  15. These results show that aspartoacylase is a member of the caboxypeptidase A family and offer novel explanations for most loss-of-function aspartoacylase mutations associated with Canavan Disease. PMID: 17391648
  16. New structure of human aspartoacylase complexed with a catalytic intermediate analogue, N-phosphonomethyl- l-aspartate, supports a carboxypeptidase-type mechanism for hydrolysis of the amide bond of the substrate, N-acetyl- l-aspartate. PMID: 18293939

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Involvement in disease Canavan disease (CAND)
Subcellular Location Cytoplasm. Nucleus.
Protein Families AspA/AstE family, Aspartoacylase subfamily
Tissue Specificity Brain white matter, skeletal muscle, kidney, adrenal glands, lung and liver.
Database Links

HGNC: 756

OMIM: 271900

KEGG: hsa:443

STRING: 9606.ENSP00000263080

UniGene: Hs.171142

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