Analytical Data
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Gene name
omp1C
- Application
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Alternative Names
Major outer membrane porin, serovar C; ompA; omp1; omp1C; Major outer membrane porin; serovar C; MOMP
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Species
Others
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Source
E. coli
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Tag
C-Myc;N-10*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08780
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Expression Region
L23-F397
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Protein Length
Full Length of Mature Protein
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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
OMP1C is a recombinant protein derived from the outer membrane protein 1C of certain bacteria, and it has attracted significant interest in the fields of microbiology and biotechnology. This protein plays a crucial role in the bacterial outer membrane structure and functions, particularly in relation to virulence and immune response evasion. Research on OMP1C is driven by its potential applications in vaccine development, as it may serve as an effective antigen to elicit immune responses against pathogenic infections. Furthermore, understanding the structure and function of OMP1C can provide insights into bacterial pathogenesis, potentially leading to the discovery of novel therapeutic targets. The ability to produce OMP1C as a recombinant protein allows for detailed studies of its biochemical properties and interactions with host immune systems, which can enhance our understanding of disease mechanisms and contribute to the development of innovative approaches for infection control. Overall, the investigation of OMP1C presents a promising avenue for advancing both basic research in microbial pathogenesis and applied research in vaccine design and antibiotic resistance mitigation.
