Analytical Data
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基因名
lpxD
- Application
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别名
UDP-3-O-acylglucosamine N-acyltransferase(EC 2.3.1.-)
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种属
Burkholderia pseudomallei
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
A3NAT7
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表达区间
1-361aa
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分子量
44.2 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
The study of lpxD recombinant protein is rooted in the exploration of lipid A biosynthesis, a crucial component of the outer membrane of Gram-negative bacteria. Lipid A serves as an anchor for lipopolysaccharides (LPS), which are fundamental for bacterial viability, cellular structure, and pathogenicity. LpxD, an enzyme that catalyzes the acylation of glucosamine in lipid A biosynthesis, is essential for the production of biologically active lipid A. Given its pivotal role, LpxD has been identified as a potential target for developing new antibacterial agents, particularly in response to the growing threat of antibiotic resistance. By creating recombinant forms of LpxD, researchers aim to better understand its structure-function relationships and enzymatic mechanisms. This research not only advances our knowledge of bacterial biology but also paves the way for novel therapeutic strategies that could inhibit LPS biosynthesis, thereby helping to combat resistant bacterial infections. Consequently, recombinant LpxD serves as a valuable tool in both fundamental and applied microbiological research.
