Analytical Data
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Gene name
ACY1
- Application
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Alternative Names
ACY1;Aminoacylase-1
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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
Q03154
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Expression Region
1-408aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMTSKGPEEEHPSVTLFRQYLRIRTVQPKPD YGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSH TDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKV EGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAGFALDEGIANP TDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFR EKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPD VDFKAFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFSRV CKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLH EAVFLRGVDIYTRLLPALASVPALPSDS
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Molecular Weight
48 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
ACY1, or acylase 1, is an important enzyme involved in the hydrolysis of N-acylated amino acids, playing a crucial role in the metabolism of amino acid signaling molecules and the regulation of various physiological processes. Its dysfunction has been linked to several metabolic disorders and neurodegenerative diseases. Research on recombinant ACY1 proteins aims to elucidate the enzyme's structure-function relationships, substrate specificity, and catalytic mechanisms. These studies are essential for understanding the enzyme's role in health and disease, as well as for developing potential therapeutic interventions. By leveraging techniques such as molecular cloning, heterologous expression, and kinetic analysis, researchers can produce large quantities of active ACY1, allowing for in-depth biochemical and pharmacological studies. Understanding ACY1's role could lead to advancements in treating conditions associated with its dysregulation, highlighting the enzyme’s significance in both basic and applied biomedical research.











