Cat: IPD-X40126

Recombinant Pseudomonas aeruginosa oprF Protein ,His

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关键信息

  • 基因名

    oprF

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    oprF; PA1777; Outer membrane porin F

  • 种属

    Pseudomonas aeruginosa

  • 表达系统

    E. coli

  • 标签

    N- His

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P13794

  • 表达区间

    25-350aa

  • 分子量

    39.3 kDa

  • 内毒素

    < 1.0 EU per μg protein as determined by the LAL method.

  • 性状

    Freeze-dried powder

  • 缓冲液

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • 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

    点位突变 标签定制 buffer定制 全长蛋白定制

  • 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.

  • 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.

  • 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.

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背景信息

OprF is a major outer membrane protein found in Pseudomonas aeruginosa, a versatile opportunistic pathogen known for its antibiotic resistance and role in chronic infections, particularly in cystic fibrosis patients. Research on OprF has gained significance due to its multifaceted roles in bacterial pathogenesis, including biofilm formation, immune evasion, and interaction with host cells. The protein is also proposed as a potential target for vaccine development and therapeutic interventions. However, the functional mechanisms of OprF remain poorly understood, largely due to challenges in characterizing the protein in its native state. Consequently, the development of recombinant OprF proteins has emerged as a pivotal avenue for research, enabling detailed studies of its structure, function, and interactions. By producing OprF recombinantly, researchers can utilize various expression systems to generate large quantities of the protein, facilitating biochemical and immunological assays. Such studies are vital for elucidating the role of OprF in Pseudomonas aeruginosa virulence and for investigating its potential as a target for vaccine formulation and therapeutic design, ultimately contributing to the development of new strategies to combat infections caused by this pathogen.

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