Analytical Data
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基因名
lpxC
- Application
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别名
lpxC；asmB；envA；UDP-3-O-acyl-N-acetylglucosamine deacetylase
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0A725
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表达区间
1-305aa
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氨基酸序列
MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAPSAVLA
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分子量
49.8 kDa
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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
LPXC is a key enzyme in the bacterial fatty acid synthesis pathway, specifically involved in the biosynthesis of the essential lipid component, mycobacterial cell walls. It catalyzes the conversion of long-chain fatty acids into shorter fatty acyl-CoA derivatives, playing a crucial role in maintaining the integrity and functionality of the bacterial membrane. Given its significance in bacterial physiology and pathogenicity, LPXC has emerged as a target for antibiotic development, particularly against Mycobacterium tuberculosis, the causative agent of tuberculosis. Research on recombinant LPXC has provided insights into its enzymatic mechanisms, structural biology, and potential as an antibiotic target. By producing LPXC as a recombinant protein, scientists can study its biochemical properties in detail, evaluate its interactions with potential inhibitors, and explore its role in bacterial survival under various environmental stresses. Ultimately, LPXC represents a promising candidate for novel therapeutic strategies aimed at combating antibiotic resistance and improving treatment outcomes for bacterial infections.
