Analytical Data
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Gene name
omp1A
- Application
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Alternative Names
Major outer membrane porin, serovar A; MOMP; ompA; omp1A; SA1/OT / Serovar A
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Species
Others
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Source
E. coli
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Tag
N-SUMO;N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23732
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Expression Region
L23-F396
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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
OMP1A (Outer Membrane Protein 1A) is a significant protein found in the outer membrane of certain bacteria, particularly those of the genus *Neisseria*. Its study has gained attention due to its potential role in pathogenesis, immunogenic properties, and applicability in vaccine development. As a model for understanding outer membrane proteins, OMP1A can provide insights into bacterial resistance mechanisms and host-pathogen interactions. Research on OMP1A focuses on its structure, function, and immunogenicity, revealing how it may elicit immune responses and offer protective effects when presented as a recombinant protein. Advances in recombinant DNA technology have facilitated the expression and purification of OMP1A, enhancing our ability to investigate its properties and interactions. Additionally, due to the rising concern of antibiotic resistance, OMP1A has emerged as a promising target for the development of novel therapeutic strategies. Overall, the study of OMP1A reaffirms the importance of outer membrane proteins in medical microbiology and their potential in contributing to innovative solutions for bacterial infections.
