Analytical Data
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Gene name
AOAH
- Application
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Alternative Names
AOAH；Acyloxyacyl hydrolase
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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
P28039
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Expression Region
35-575aa
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AA Sequence
LSNGHTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEKLFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFCKQNTGQPLCHLYPLPKETWKFTLQKARQIVKKSPILKYSRSGSDICSLPVLAKICQKIKLAMEQSVPFKDVDSDKYSVFPTLRGYHWRGRDCNDSDESVYPGRRPNNWDVHQDSNCNGIWGVDPKDGVPYEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDSTVGIKEKSIYLRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPVPAMTTPEKLYSNVMQTLKHLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQLSNTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNEVALLLLADHFWKKVQLQWPQILGKENPFNPQIKQVFGDQGGH
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Molecular Weight
62.4 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
Related Products
Protein Description
The study of AOAH (Acyl-CoA thioesterase 1) recombinant proteins has gained significant attention in recent years due to their crucial role in lipid metabolism and potential therapeutic applications. AOAH is involved in the deacylation of various acyl-CoA substrates, thereby influencing several metabolic pathways, including fatty acid metabolism and membrane lipid remodeling. Understanding the functional mechanisms and regulatory pathways of AOAH can provide insights into metabolic diseases, such as obesity and diabetes, where lipid dysregulation plays a pivotal role. Researchers have utilized recombinant DNA technology to produce and purify AOAH proteins, allowing for comprehensive biochemical analyses and structural studies. This has led to the identification of specific enzyme kinetics, substrate specificity, and potential post-translational modifications that may affect its activity. Additionally, understanding the interactions of AOAH with other cellular components could unveil new regulatory mechanisms within lipid metabolism. The ongoing research aims to explore the therapeutic potential of AOAH modulation in various lipid-related disorders, highlighting the relevance of this protein in both fundamental biology and clinical applications. As such, the investigation of AOAH recombinant proteins represents a promising frontier in metabolic research, with the potential to contribute to novel treatment strategies for metabolic diseases.
