Analytical Data
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Gene name
Outer membrane 蛋白 F/OmpF
- Application
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Alternative Names
Outer membrane protein 1A (Outer membrane protein B) (Outer membrane protein IA) (Porin OmpF) (cmlB) (coa) (cry) (tolF)
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02931
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Expression Region
23-362aa
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Molecular Weight
44.1 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
OmpF, a major outer membrane porin found in Escherichia coli, plays a crucial role in the transport of small molecules across the bacterial outer membrane. As a trimeric protein, OmpF facilitates the passive diffusion of ions and small hydrophilic compounds, which is essential for bacterial metabolism and survival. The study of OmpF is significant due to its potential applications in biotechnology and medicine, particularly in the development of drug delivery systems and antibiotic resistance research. Recombinant OmpF has been expressed in various systems, enabling researchers to investigate its structural and functional properties in detail. Moreover, the ability to manipulate OmpF allows for the design of biomaterials with enhanced permeability or selectivity, further expanding its use in nanotechnology and synthetic biology. Understanding the molecular mechanisms governing OmpF's function and its interactions with diverse substrates can lead to advancements in targeted therapies and the design of novel antimicrobial agents. Consequently, research on OmpF has broad implications for improving treatment strategies against bacterial infections and optimizing biotechnological applications.
