Analytical Data
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基因名
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 is the recombinant Acetylornithine Deacylase protein, expressed by E. coli , with tag free.
- Application
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别名
dapE; Succinyl-diaminopimelate desuccinylase; SDAP desuccinylase; N-succinyl-LL-2; 6-diaminoheptanedioate amidohydrolase
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种属
Others
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q3YZ81
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表达区间
M1-A375
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蛋白长度
Full Length
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
