Analytical Data
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基因名
FTS
- Application
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别名
AKTIP. FTS
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9H8T0
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表达区间
1-292aa
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氨基酸序列
MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT
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分子量
57.86 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 FtsZ, a key protein in bacterial cell division, has gained significant attention in recent years due to its crucial role in forming the Z-ring at the future site of septum formation. FtsZ is a homolog of tubulin in eukaryotic cells and is essential for cytokinesis in prokaryotes. Understanding the mechanisms by which FtsZ assembles and functions is vital, as it offers potential targets for antibiotic development, particularly in an era of rising antibiotic resistance. Researchers have explored the structural and biochemical properties of FtsZ, revealing insights into its dynamic behavior and interactions with other cell division proteins. Additionally, modifications such as the creation of recombinant FtsZ proteins have facilitated in vitro studies, allowing scientists to dissect the protein's functional dynamics. Advances in techniques like cryo-electron microscopy and time-lapse fluorescence microscopy have furthered our understanding of the spatiotemporal regulation of FtsZ during cell division. This research not only enhances our comprehension of bacterial physiology but also holds promise for engineering novel antibacterial strategies by disrupting the FtsZ-mediated division process. Thus, ongoing investigations into FtsZ and its regulatory networks continue to be pivotal in the field of microbiology and antibiotic discovery.
