Analytical Data
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基因名
folP
- Application
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别名
folP；dhpS；Dihydropteroate synthase
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种属
E.coli
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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
Q59919
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表达区间
1-267aa
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氨基酸序列
MTKTKIIGILNVTPDSFSDGGKYNSVDKAIARAKEMIDEGVDIIDVGGVSTRPGHTEVSLEEEMERVVPVVEQLVKLDVQISVDTYRSEVAEACLKLGATMINDQWAGLYDPKIFDVVSDYNAEIVLMHNGDGQREQPVVEEMLLSLLTQANKAEMAGIEKGNIWLDPGIGFAKSRSEEKEVMARLDELVATEYPVLLATSRKRFIKEMIGKETTPAERDEATAATTVYGIMKGIQAVRVHNVDLNVKLAQSIDFLKENEHERHHLS
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分子量
33.6 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
FolP (folate-dependent 4-hydroxyphenylpyruvate dioxygenase) is an important enzyme implicated in the folate biosynthesis pathway, which is essential for the production of nucleotides and amino acids in living organisms. In recent years, studies have highlighted the significance of FolP as a potential target for antibiotic and antifungal drug development, due to its unique mechanism of action and essential role in the metabolism of various pathogens. Unlike human cells, which acquire folate from dietary sources, many bacteria and fungi synthesize their own folate, making FolP an attractive target for selective inhibition. The recombinant expression of FolP allows researchers to investigate its structure, function, and inhibition more thoroughly. By producing FolP in a laboratory setting, scientists can employ various biochemical assays, structural biology techniques, and high-throughput screening methods to identify potential inhibitors. Furthermore, the study of FolP contributes to our understanding of microbial resistance mechanisms and the evolution of metabolic pathways, ultimately aiding in the design of novel therapeutics to combat resistant infections. This growing body of research underscores the importance of FolP in both fundamental biology and applied biomedical sciences, opening avenues for new drug discovery efforts against resistant pathogens.
