Analytical Data
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Gene name
AANAT
- Application
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Alternative Names
AA-NAT; SNAT; Aralkylamine N-Acetyltransferase; Serotonin Acetyltransferase; Serotonin Acetylase; Serotonin N-Acetyltransferase; Melatonin Rhythm Enzyme
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q16613
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Expression Region
Met1~Cys207
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Molecular Weight
25kDa
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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
AANAT, or arylalkylamine N-acetyltransferase, is a crucial enzyme involved in the synthesis of melatonin, a hormone that regulates circadian rhythms and sleep-wake cycles. Research on AANAT has gained prominence due to its significant role in various physiological processes, including mood regulation, reproductive functions, and immune response. Understanding AANAT's structure and function can provide insights into how melatonin influences these biological systems and may contribute to developing treatments for sleep disorders, depression, and other related conditions. The purification and characterization of recombinant AANAT protein have been essential for studying the enzyme’s kinetics, substrate specificity, and regulatory mechanisms. Advances in recombinant DNA technology have enabled the expression of AANAT in various systems, facilitating the production of sufficient quantities for in-depth biochemical analyses. This research not only enhances our knowledge of melatonin biosynthesis but also opens new avenues for pharmacological interventions targeting circadian rhythm-related disorders. Overall, AANAT stands as a key player in the realm of chronobiology, and its study is vital for both basic research and clinical applications.
