Analytical Data
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Gene name
ASPA
- Application
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Alternative Names
ASPA；ACY2；ASP；Aspartoacylase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P45381
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Expression Region
1-313aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK LTLNAKSIRC CLH
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Molecular Weight
38 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ASPA (aspartoacylase) is an enzyme primarily involved in the metabolism of N-acetylaspartate (NAA), a compound that plays a significant role in central nervous system function. Mutations in the ASPA gene lead to a rare genetic disorder known as Canavan disease, characterized by severe neurodegeneration and cognitive impairment, predominantly affecting young children. The lack of functional ASPA results in the accumulation of NAA in the brain, contributing to the pathological features of the disease. Given the severity of Canavan disease and the absence of effective treatments, researchers have focused on characterizing and potentially developing therapeutic options that target ASPA. This includes the study of recombinant ASPA proteins, which are being investigated for their potential to restore enzyme activity in affected tissues, thereby reducing the toxic buildup of NAA. Furthermore, the exploration of ASPA structure-function relationships helps in understanding how mutations affect enzyme activity, which could aid in the design of small-molecule chaperones to enhance residual ASPA activity. Overall, research into ASPA and its recombinant forms not only holds promise for treating Canavan disease but also enhances our understanding of enzyme functionality within the nervous system.
