Analytical Data
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Gene name
ACY3
- Application
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Alternative Names
rHuACY3, His; N-acyl-aromatic-L-amino acid amidohydrolase; ACY-3
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Species
Human
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Source
E. coli
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Tag
N-6*His
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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
M1-S319
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AA Sequence
HHHHHHMCSLPVPREPLRRVAVTGGTHGNEMSGVYLARHWLHAPAELQRASFSAVPVLANPAATSGCRRYVDHDLNRTFTSSFLNSRPTPDDPYEVTRARELNQLLGPKASGQAFDFVLDLHNTTANMGTCLIAKSSHEVFAMHLCRHLQLQYPELSCQVFLYQRSGEESYNLDSVAKNGLGLELGPQPQGVLRADIFSRMRTLVATVLDFIELFNQGTAFPAFEMEAYRPVGVVDFPRTEAGHLAGTVHPQLQDRDFQPLQPGAPIFQMFSGEDLLYEGESTVYPVFINEAAYYEKGVAFVQTEKFTFTVPAMPALTPAPSPAS
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Protein Length
Full Length
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Molecular Weight
35 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 Aminoacylase 3, is a member of the aminoacylase family of enzymes that play a vital role in the hydrolysis of N-acylamino acids into free amino acids. Its significance is underscored by its involvement in various physiological processes, including neuronal function, metabolism, and potential pathways related to neurodegenerative diseases. Recent studies have pointed to ACY3 as a key player in regulating the levels of bioactive lipids and signaling molecules, which can influence neuroinflammation and oxidative stress responses. Additionally, genetic polymorphisms in the ACY3 gene have been associated with cognitive function and certain psychiatric disorders, making it a target of interest for therapeutic interventions. The recombinant expression of ACY3 protein allows for in-depth functional studies, enabling researchers to elucidate its catalytic mechanisms, substrate specificity, and interactions with other biomolecules. Understanding the structure-function relationship of ACY3 is crucial for developing potential applications in treating metabolic disorders and enhancing cognitive health. The exploration of ACY3 as a therapeutic target highlights the importance of protein engineering and recombinant technologies in advancing our knowledge of enzymatic functions and their implications in human health.
