Analytical Data
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Gene name
ACY3
- Application
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Alternative Names
ACY3；ASPA2；N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)
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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
Q96HD9
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Expression Region
1-319aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMCSLPVPREPLRRVAVTGGTHGNEMSG VYLARHWLHAPAELQRASFSAVPVLANPAATSGCRRYVDHDLNRTFTSSF LNSRPTPDDPYEVTRARELNQLLGPKASGQAFDFVLDLHNTTANMGTCLI AKSSHEVFAMHLCRHLQLQYPELSCQVFLYQRSGEESYNLDSVAKNGLGL ELGPQPQGVLRADIFSRMRTLVATVLDFIELFNQGTAFPAFEMEAYRPVG VVDFPRTEAGHLAGTVHPQLQDRDFQPLQPGAPIFQMFSGEDLLYEGEST VYPVFINEAAYYEKGVAFVQTEKFTFTVPAMPALTPAPSPAS
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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
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Protein Description
ACY3, or Arylsulfatase C, is an important enzyme involved in the hydrolysis of aryl sulfate compounds, playing a crucial role in various biological processes, including the metabolism of steroid hormones and the regulation of sulfate levels in tissues. Research on ACY3 recombinant protein has gained significance due to its potential applications in understanding inherited metabolic disorders, particularly those associated with sulfate metabolism. Mutations in the ACY3 gene can lead to severe neurological and metabolic disorders, prompting scientists to explore the structural and functional properties of ACY3 to elucidate its mechanisms of action. Additionally, the production of recombinant ACY3 provides a valuable tool for studying enzyme kinetics, substrate specificity, and the effects of potential inhibitors, thereby contributing to the development of therapeutic strategies aimed at addressing ACY3-related diseases. Detailed characterization of this protein through biochemical assays and structural biology techniques enhances our understanding of its role in human health and disease. Furthermore, the therapeutic potential of ACY3 as a target for drug development makes it a significant focus of research, especially in the context of personalized medicine, where specific metabolic pathways can be modulated to offer tailored treatments for affected individuals. As research progresses, the insights gained from recombinant ACY3 studies are expected to pave the way for innovative approaches in diagnostics and therapies for metabolic disorders linked to this enzyme.
