Analytical Data
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Gene name
AOAH
- Application
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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 90% as determined by SDS-PAGE.
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Uniprot
P28039
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Expression Region
Ser24~Gln300
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Molecular Weight
35kDa
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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
The recombinant protein AOAH (Acylamidase), a significant enzyme in the human body, has gained attention in biochemical and therapeutic research due to its role in the metabolism of fatty acids and its potential involvement in various physiological processes, including inflammation and immune response. AOAH specifically hydrolyzes acylated amino acids, which plays a crucial role in modulating lipid-mediated signaling pathways. Recent studies have highlighted its presence in various tissues, suggesting its importance in maintaining cellular homeostasis. Given its pivotal role in detoxifying harmful lipids and modulating immune responses, AOAH has emerged as a candidate for therapeutic applications in diseases associated with lipid dysregulation, such as metabolic disorders and inflammatory conditions. The advancement of biotechnology allows for the recombinant production of AOAH, enabling detailed studies of its structure, function, and biochemical properties. Additionally, understanding the mechanisms by which AOAH interacts with various substrates can provide insights into potential drug development strategies. Research into recombinant AOAH not only facilitates a deeper understanding of its enzymatic mechanisms but also opens avenues for the development of novel therapeutics targeting conditions where lipid metabolism is disrupted, thereby highlighting the importance of this enzyme in health and disease.
