Analytical Data
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Gene name
Outer membrane 蛋白 X/OmpX
- Application
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Alternative Names
ompX; Z1036; ECs0892; Outer membrane protein X
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Species
Escherichia coli O157:H7
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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
P0A919
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Expression Region
24-171aa
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Molecular Weight
23.8 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 protein X (OmpX) is a well-characterized porin protein found in the outer membrane of Escherichia coli and other Gram-negative bacteria. Its primary function involves facilitating the transport of small molecules and ions across the outer membrane, playing a crucial role in bacterial survival and adaptation to different environments. Given its significant role, OmpX has garnered considerable interest for its potential applications in pharmaceutical and biotechnological fields. Research on recombinant OmpX has focused on elucidating its structural and functional properties to better understand its mechanisms of action. Additionally, the ability to express OmpX recombinantly allows for studies on its interactions with other proteins and its potential as a target for drug development, particularly in the quest to combat antibiotic resistance. Furthermore, OmpX has been explored as a candidate for vaccine development due to its immunogenic properties. Recent advances in recombinant DNA technology and protein expression systems have facilitated the production of OmpX in various expression hosts, enabling scientists to produce large amounts of functional protein for detailed biochemical and biophysical studies. This research is crucial for understanding bacterial pathogenesis and developing innovative strategies to manage bacterial infections and resistance.
