Analytical Data
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基因名
lpxD
- Application
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别名
lpxD；UDP-3-O-acylglucosamine N-acyltransferase
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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
P0CD76
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表达区间
1-354aa
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氨基酸序列
MSQSTYSLEQLADFLKVEFQGNGATLLSGVEEIEEAKTAHITFLDNEKYAKHLKSSEAGAIIISRTQFQKYRDLNKNFLITSESPSLVFQKCLELFITPVDSGFPGIHPTAVIHPTAIIEDHVCIEPYAVVCQHAHVGSACHIGSGSVIGAYSTVGEHSYIHPRVVIRERVSIGKRVIIQPGAVIGSCGFGYVTSAFGQHKHLKHLGKVIIEDDVEIGANTTIDRGRFKHSVVREGSKIDNLVQIAHQVEVGQHSMIVAQAGIAGSTKIGNHVIIGGQAGITGHICIADHVIMMAQTGVTKSITSPGIYGGAPARPYQEIHRQVAKVRNLPRLEERIAALEKLVQKLEALSEQH
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分子量
38.4 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
LpxD is a crucial enzyme in the biosynthesis of lipid A, an essential component of the outer membrane of Gram-negative bacteria. It catalyzes the transfer of acyl groups to UDP-GlcNAc, leading to the formation of the lipid A precursor. Given the importance of lipid A in maintaining bacterial integrity and serving as a target for the host immune system, LpxD has gained attention as a potential target for novel antibiotics. With the rise of antibiotic-resistant bacteria, understanding the structure and function of LpxD is vital for developing new therapeutic strategies. Researchers have focused on recombinant expression of LpxD to study its enzymatic activity and structure, allowing for the exploration of its mechanism and the identification of inhibitory compounds. Furthermore, structural studies through techniques like X-ray crystallography and cryo-electron microscopy have provided insights into the enzyme's active site and substrate interactions, paving the way for structure-based drug design. Overall, the study of recombinant LpxD not only enriches our understanding of bacterial lipid biosynthesis but also opens new avenues for combating antibiotic resistance through innovative antibiotic development.
