Analytical Data
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Gene name
AAO
- Application
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Alternative Names
AAO；AO；L-ascorbate oxidase
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Species
E.coli
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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
P24792
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Expression Region
31-579aa
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AA Sequence
SQIRHYKWEVEYMFWAPDCNENIVMGINGQFPGPTIRANAGDTVVVELINKLHTEGVVIHWHGILQRGTPWADGTASISQCAINPGETFFYNFTVDNPGTFFYHGHLGMQRSAGLYGSLIVDPPQGKKEPFHYDGEINLLLSDWWHQSIHKQEVGLSSKPIRWIGEPQTILLNGRGQFDCSIAAKYDSNLEPCKLKGSEPCAPYIFHVMPKKTYRIRIASTTALAALNFAIGNHPLLVVEADGNYVQPFYTSDIDIYSGESYSVLITTDQNPSENYWVSVGTRGRHPNTPPGLTLLNYLPNSVSKLPTSPPPETPAWDDFDRSKNFTYRITAAMGSPKPPVKSNRRIFLLNTQNVINGYVKWAINDVSLALPPTPYLGAMKFNLLHAFDQNPPPEVFPEDYDIDTPPTNEKTKIGNGVYQFKIGEIVDVILQNANMMKENLSEIHPWHLHGHDFWVLGYGDGKFTAEEESSLNLKNPPLRNTVVIFPYGWTAIRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGRIPTKALACGGTAKSLINNP
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Molecular Weight
74.3 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
AAO (Aspergillus nidulans Amidohydrolase-Containing Protein) is a multifunctional enzyme that plays a crucial role in microbial metabolism, specifically in the hydrolysis of amides and peptide bonds. Research on AAO is particularly significant due to its potential applications in biotechnology and industrial processes, such as the degradation of complex organic compounds and bioremediation efforts. The enzyme is derived from the filamentous fungus Aspergillus nidulans, which is known for its ability to produce a variety of enzymes that can break down complex substrates. Scientists have been investigating the structure, function, and regulation of AAO to enhance its efficiency and stability for commercial use. Additionally, understanding the genetic and biochemical pathways governing AAO production can lead to advancements in enzyme engineering, allowing for tailored applications in food processing, pharmaceuticals, and waste management. As researchers continue to explore the functional mechanisms of AAO, there is a growing interest in the potential for using this enzyme in sustainable practices, reflecting an increasing demand for environmentally friendly solutions in various industries. Overall, the study of AAO represents a promising area of research at the intersection of microbiology, enzymology, and biotechnology.
