Analytical Data
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Gene name
Acetylornithine Deacylase
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简介
Acetylornithine deacylase protein catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), leading to the formation of succinic acid and LL-2,6-diaminopimelic acid (DAP) , plays a key role in cellular processes. This enzyme activity is integral to the bacterial biosynthesis of lysine and mesodiaminopimelic acid, both of which contribute to the structural integrity of the bacterial cell wall. Acetylornithine Deacylase Protein, Shigella sonnei (His) is the recombinant Acetylornithine Deacylase protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
dapE; Succinyl-diaminopimelate desuccinylase; SDAP desuccinylase; N-succinyl-LL-2; 6-diaminoheptanedioate amidohydrolase
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Species
Others
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q3YZ81
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Expression Region
M1-A375
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Protein Length
Full Length
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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
Acetylornithine deacylase (AOD) is an enzyme that plays a critical role in the arginine biosynthetic pathway, catalyzing the deacetylation of N-acetyl-L-ornithine to produce L-ornithine and acetate. This process is vital for various physiological functions, including nitrogen metabolism and the synthesis of polyamines, which are essential for cell growth and proliferation. The study of AOD is particularly significant in the context of microbial physiology and biotechnology, as it can influence the efficiency of arginine production in microbial systems. Recombinant protein production of AOD allows for detailed biochemical characterization, providing insights into its enzymatic mechanisms and potential biotechnological applications. Furthermore, understanding the structure-function relationship of AOD can facilitate the development of enzyme inhibitors, which could serve as therapeutic agents in managing conditions related to arginine metabolism. The production of AOD through recombinant DNA technology not only aids in its purification and characterization but also enhances our understanding of its ecological role in various microorganisms. This research is crucial as it could lead to innovative strategies in metabolic engineering to optimize arginine yields, which have implications in agricultural, industrial, and pharmaceutical sectors.











