Analytical Data
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Gene name
Outer membrane 蛋白 A/OmpA
- Application
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Alternative Names
omp1
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Species
Chlamydophila psittaci
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q00087
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Expression Region
23-392aa
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Molecular Weight
45.4 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
Related Products
Protein Description
Outer membrane protein A (OmpA) is a crucial component of the outer membrane of Gram-negative bacteria, playing significant roles in maintaining membrane integrity, facilitating nutrient transport, and contributing to bacterial pathogenesis. Due to its abundant expression and immunogenicity, OmpA has garnered attention as a potential target for vaccine development and therapeutic intervention. Research into OmpA has revealed its ability to form oligomers, its involvement in biofilm formation, and its role in host-pathogen interactions. Furthermore, the recombinant production of OmpA has become a focal point for functional studies, allowing for the exploration of its structural and biochemical properties without the complexities associated with the native bacterial context. This research not only aids in understanding the mechanistic details of OmpA's function but also enhances the development of OmpA-based applications, including diagnostics and drug delivery systems. The ongoing studies of OmpA emphasize its potential as a versatile platform for biotechnological applications, prompting further investigation into its recombinant forms and the implications for infectious disease management.
