Recombinant Human Aspartoacylase (ASPA)

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Code: CSB-MP002223HU

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20ug100ug1mg(1mg*1 or 500ug*2)

US$660

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Express system: Mammalian cell

Species: Homo sapiens (Human)

Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged

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Product Details
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Target Background

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

Mammalian cell

Expression Region

1-313aa

Target Protein Sequence

MTSCHIAEEHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVKKCTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSYDIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEHPSLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHFNEGKEFPPCAIEVYKIIEKVDYPRDENGEIAAIIHPNLQDQDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLNAKSIRCCLH
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

39.7 kDa

Protein Length

Full Length

Tag Info

N-terminal 10xHis-tagged and C-terminal Myc-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.

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.

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

3-7 business days
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.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Troubleshooting and FAQs

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Datasheet & COA

Please contact us to get it.

Images

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

Description

To make this Recombinant Human ASPA protein, the ASPA gene was isolated at first and cloned into an expression vector. CUSABIO has built a mature recombinant protein platform. This Recombinant Human ASPA protein was developed in the platform. It was expressed in Mammalian cell at the region of 1-313aa of the Human ASPA protein. N-terminal 10xHis tag and C-terminal Myc tag was fused with the expression vector for affinity and purification purposes. The purity is 85%+ determined by SDS-PAGE.

ASPA is an enzyme reported to be involved in the hydrolysis of N-acetyl-aspartate (NAA) into acetate and aspartate. A reduction in free acetate for lipid synthesis subsequent to loss of ASPA function is believed to contribute to disease etiology and could likely account for abnormalities in the lipid content of myelin. Early observations suggested an association of Canavan disease with oligodendrocytes due to loss of white matter as a result of the absence of functional ASPA. Thus, modification of aspartoacylase might be serve as a potential use in enzyme replacement therapy for the treatment of Canavan disease. Besides, extensive aspartoacylase expression in the rat central nervous system. Several findings provide strong support for a carboxypeptidase-type mechanism for the hydrolysis of the amide bond of the substrate, N-acetyl- l-aspartate.

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Target Background

Function(From Uniprot)

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

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
Four ASPA missense mutations associated with Canavan disease are structurally characterized. PMID:25003821
Definitive evidence is presented to show that the recombinantly-expressed human aspartoacylase is not a glycoprotein. PMID:24632142
This is the first case report of ASPA mutation studies in Canavan disease from Indian subcontinent. PMID:22878930
a novel mutation Y88X within the aspartoacylase gene in a consanguineous family with an affected child diagnosed as Canavan disease. PMID:22468686
Human aspartoacylase gene expression was high not only in brain and kidney, but also in lung and liver. PMID:22750302
Gene ASPA (NM_000049) was undertaken to sequence for mutation analysis. PMID:22219087
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
the ASPA gene was analysed in 22 unrelated non-Jewish patients with Canavan disease, and 24 different mutations were found PMID:12638939
Mild-onset presentation of Canavan's disease associated with novel G212A point mutation in aspartoacylase gene PMID:16437572
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
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
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
the N-terminal domain of aspartoacylase adopts a protein fold similar to that of zinc-dependent hydrolases related to carboxypeptidases A PMID:17194761
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
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