Analytical Data
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基因名
tfpQ
- Application
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别名
Beta pilin (Q pilin)
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种属
Moraxella bovis
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P07640
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表达区间
7-157aa
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分子量
20.9 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 TfpQ recombinant proteins is situated within the broader context of protein engineering and synthetic biology, aimed at understanding and exploiting the functional properties of proteins for various applications. TfpQ, a stem-like protein often associated with bacterial biofilm formation and adhesion, has garnered interest due to its potential roles in microbial ecology and pathogenesis. The ability to recombinantly express TfpQ offers insights into its structure-function relationships, enabling researchers to elucidate the molecular mechanisms underlying its activity. Additionally, TfpQ presents opportunities for biotechnological advancements, including the development of novel biomaterials and therapeutic agents targeting bacterial infections. Given the rising concern over antibiotic resistance, characterizing TfpQ's interactions and behavior could lead to innovative strategies for combating biofilm-related infections. The strategic manipulation of TfpQ through recombinant techniques can accelerate the discovery of new biological functions, thereby enhancing our understanding of microbial physiology and contributing to the fields of medicine, environmental science, and biotechnology. Overall, TfpQ recombinant protein research stands at the intersection of fundamental biology and applied sciences, promising significant implications for health and industry.
