Cat: IPD-X27735

Recombinant E.coli Outer membrane porin C/OmpC Protein,His & SUMO

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Analytical Data

  • Gene name

    Outer membrane porin C/OmpC

  • 简介

    Outer membrane porin C/OmpC Protein facilitates substance transport across the bacterial outer membrane, forming homotrimeric pores for passive diffusion of small molecules, crucial for maintaining cell envelope permeability. Outer membrane porin C/OmpC Protein, E.coli (Myc, His-SUMO) is the recombinant E. coli-derived Outer membrane porin C/OmpC protein, expressed by E. coli , with N-His, C-Myc, N-SUMO labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ompC; Z3473; ECs3104; Outer membrane porin C; Outer membrane protein 1B; Outer membrane protein C; Porin OmpC

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    N-His;C-Myc;N-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8XE41

  • Expression Region

    A22-F367

  • AA Sequence

    AEVYNKDGNKLDLYGKVDGLHYFSDDKSVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGSVSGEGMTNNGREALRQNGDGVGGSITYDYEGFGIGAAVSSSKRTDDQNSPLYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGVINGRNYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF

  • Protein Length

    Full Length of Mature Protein

  • Endotoxin

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

  • Form

    Freeze-dried powder

  • Buffer formulation

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

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    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.

  • Storage & Shelf Life

    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.

  • Shipping

    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

Outer membrane porin C (OmpC) is a significant protein found in the outer membrane of Gram-negative bacteria, particularly in Escherichia coli. Its primary function is to form water-filled channels that facilitate the transport of small molecules, including nutrients and ions, across the bacterial outer membrane. Due to its critical role in antibiotic resistance and cellular permeability, OmpC has become a focal point of research aimed at understanding bacterial physiology and developing novel therapeutic strategies. Recombinant OmpC protein can be produced through molecular cloning techniques, which allows researchers to obtain it in significant amounts for structural and functional studies. Investigating the properties of OmpC, including its structural conformation and interaction with various substrates, provides insights into its mechanism of action and potential applications in antibiotic design. Additionally, the study of OmpC in the context of membrane biophysics and its involvement in bacterial survival in hostile environments illustrates its importance in microbiology and biotechnology. Overall, research on recombinant OmpC not only enhances our understanding of bacterial function but also paves the way for innovative approaches to combat antibiotic resistance and improve drug delivery systems.

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