Cat: PA2000-1394

Recombinant Human OT Protein,His

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Analytical Data

  • 基因名

    OT

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    OT;OT;Oxytocin-neurophysin 1

  • 种属

    Human

  • 表达系统

    E. coli

  • 标签

    His tag N-Terminus

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P01178

  • 表达区间

    1-125aa

  • 氨基酸序列

    MAGPSLACCLLGLLALTSACYIQNCPLGGKRAAPDLDVRKCLPCGPGGKGRCFGPNICCAEELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAVLGLCCSPDGCHADPACDAEATFSQR

  • 分子量

    12.7 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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Protein Description

The study of outer membrane transporter (OT) proteins has gained significant attention due to their crucial role in the cellular processes of gram-negative bacteria. These proteins are responsible for the transport of essential nutrients, metabolites, and drugs across the outer membrane, which acts as a permeability barrier. Understanding the structure and function of OT proteins is vital for several reasons: first, they are key to bacterial survival in hostile environments; second, they can contribute to antibiotic resistance by mediating the uptake or efflux of antimicrobial agents; and third, they serve as potential targets for drug development aimed at disrupting bacterial infections. The research on OT proteins encompasses various approaches, including structural biology, biochemistry, and genomics, which aim to elucidate their mechanisms of transport and interaction with substrates. Additionally, advances in techniques such as cryo-electron microscopy and X-ray crystallography have provided invaluable insights into their 3D structures, paving the way for the design of novel inhibitors. Given the rise of multidrug-resistant bacterial strains, the exploration of OT proteins is not only significant for basic science but also holds promise for improving therapeutic strategies against bacterial infections. Understanding these complex systems can ultimately contribute to the development of new antibiotics and enhance our ability to combat pathogenic bacteria effectively.

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Proteintech Group, Inc
5500 Pearl Street, Suite 400
Rosemont, IL 60018, USA
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IPODIX North America (HQ)
Proteintech Group, Inc
5500 Pearl Street, Suite 400
Rosemont, IL 60018, USA
1-888-478-4522
proteintech@ptglab.com
IPODIX North America (HQ)
Proteintech Group, Inc
5500 Pearl Street, Suite 400
Rosemont, IL 60018, USA
1-888-478-4522
proteintech@ptglab.com
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