Cat: IPD-X40255

Recombinant Vibrio parahaemolyticus serotype O3:K6 ompK Protein ,His & SUMO

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Analytical Data

  • 基因名

    ompK

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    ompK; OMPK_VIBPA; Outer membrane protein ompK

  • 种属

    Vibrio parahaemolyticus serotype O3:K6

  • 表达系统

    E. coli

  • 标签

    N- His-SUMO

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P59570

  • 表达区间

    21-266aa

  • 分子量

    43.9 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 OmpK family of proteins, particularly OmpK35 and OmpK36, are outer membrane porins predominantly found in *Klebsiella pneumoniae,* a significant pathogen responsible for various infections, including pneumonia and bloodstream infections. These porins play a crucial role in the permeability of the bacterial outer membrane, regulating the passage of small molecules and contributing to antibiotic resistance. Understanding the structure and function of OmpK proteins is essential for developing novel therapeutic strategies, particularly in combating multidrug-resistant strains of *K. pneumoniae.* Recent studies have focused on the recombinant expression of OmpK proteins to facilitate detailed biochemical and biophysical analyses. This research is pivotal in elucidating the mechanisms of porin-mediated transport and resistance, and it may pave the way for engineered porins with enhanced functions or modified properties for biotechnological applications. Moreover, the increasing incidence of antibiotic resistance underscores the urgency in studying these porins to inform the design of new antibiotics or adjuvants that can restore the efficacy of existing drugs. Overall, the investigation of OmpK recombinant proteins stands at the intersection of microbiology, structural biology, and pharmacology, highlighting their potential implications in public health and infectious disease management.

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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
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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