Analytical Data
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基因名
pfo
- Application
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别名
Theta-toxin Thiol-activated cytolysin
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种属
Clostridium perfringens
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0C2E9
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表达区间
29-500aa
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分子量
68.7 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 research on PFO (perfringolysin O) recombinant protein has gained significant attention due to its potential applications in various fields, including medical diagnostics, therapeutics, and biotechnology. PFO is a pore-forming toxin produced by the bacterium Clostridium perfringens, and it plays a crucial role in pathogenicity by disrupting cellular membranes. Understanding the structure and function of PFO at the molecular level can provide valuable insights into its mechanisms of action and how it can be utilized or inhibited. In recent years, advances in recombinant DNA technology have made it possible to produce PFO in a laboratory setting, allowing researchers to study its properties in detail without the complications associated with working directly with the pathogenic bacterium. Additionally, PFO has been explored as a molecular tool for targeted drug delivery and as a component in vaccine development, given its ability to form pores in lipid membranes that can be harnessed for therapeutic purposes. The ability to manipulate PFO through recombinant techniques opens new avenues for enhancing its efficacy and safety in biomedical applications, making it a promising candidate for further investigation in the realms of immunology and molecular therapy. Moreover, ongoing research aims to delineate the functional domains of PFO and to develop modified versions with improved biocompatibility and specificity, thereby expanding its utility in various scientific and clinical applications.












