Analytical Data
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Gene name
omp1B
- Application
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Alternative Names
Major outer membrane porin, serovar B; MOMP; ompA; omp1B; Chlamydia trachomatis
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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
P23421
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Expression Region
L23-F394
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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
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Protein Description
OMP1B (Outer Membrane Protein 1B) is a significant protein found in the outer membrane of certain gram-negative bacteria, including pathogenic strains that are of considerable interest in medical microbiology. The research on OMP1B has gained traction due to its potential role in bacterial virulence, adherence, and immune evasion. Understanding the structure and function of OMP1B is crucial for unraveling the mechanisms by which these bacteria interact with their hosts and establish infections. Furthermore, OMP1B presents opportunities for vaccine development and therapeutic interventions, as it may serve as a target for neutralizing antibodies or an antigen for vaccine formulation. Studies have highlighted its ability to elicit immune responses, suggesting its importance in the development of strategies to combat bacterial infections. Recent advances in recombinant protein technology have facilitated the production and characterization of OMP1B, allowing researchers to explore its properties and interactions in detail. This research not only contributes to our fundamental understanding of bacterial pathogens but also has practical implications for public health, particularly in devising novel approaches to tackle antibiotic resistance and improve infection control measures. Overall, ongoing investigations into OMP1B hold promise for advancing both basic and applied sciences in the field of infectious diseases.
