Analytical Data
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Gene name
Outer membrane porin C/OmpC
- Application
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Alternative Names
Outer membrane protein 1B Porin OmpC
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Species
Escherichia coli O157:H7
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8XE41
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Expression Region
22-367aa
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Molecular Weight
58.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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 crucial integral membrane protein found in the outer membrane of gram-negative bacteria, particularly Escherichia coli. It plays a vital role in facilitating the passive diffusion of small molecules, including nutrients and waste products, across the membrane. Given its significance in bacterial physiology and its potential as a target for antibiotic development, OmpC has garnered considerable interest in molecular biology and biotechnology research. The study of OmpC has also provided insights into the mechanisms of antibiotic resistance, as alterations in porin expression can affect bacterial susceptibility to various antibiotics. Moreover, OmpC's ability to form channels in liposomal systems has led to its exploration in the development of drug delivery systems and nanotechnology applications. The production of recombinant OmpC proteins has been essential for studying its structural and functional properties. Researchers have successfully expressed OmpC in various host systems, allowing for the characterization of its biophysical properties and the investigation of its interactions with different ligands. Understanding the details of OmpC's structure and function is critical for harnessing its potential in medical and biotechnological applications, including vaccine development and the design of novel antimicrobial agents. The ongoing research surrounding OmpC reflects the broader effort to exploit bacterial proteins for innovative solutions to combat antibiotic resistance and improve therapeutic strategies.
