Analytical Data
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Gene name
omp38
- Application
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Alternative Names
omp38；ompA；Outer membrane Protein Omp38
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6RYW5
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Expression Region
20-356aa
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AA Sequence
ANAGVTVTPLLLGYTFQDSQHNNGGKDGNLTNGPELQDDLFVGAALGIELTPWLGFEAEYNQVKGDVDGASAGAEYKQKQINGNFYVTSDLITKNYDSKIKPYVLLGAGHYKYDFDGVNRGTRGTSEEGTLGNAGVGAFWRLNDALSLRTEARATYNADEEFWNYTALAGLNVVLGGHLKPAAPVVEVAPVEPTPVAPQPQELTEDLNMELRVFFDTNKSNIKDQYKPEIAKVAEKLSEYPNATARIEGHTDNTGPRKLNERLSLARANSVKSALVNEYNVDASRLSTQGFAWDQPIADNKTKEGRAMNRRVFATITGSRTVVVQPGQEAAAPAAAQ
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Molecular Weight
44.0 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
OMP38 is a recombinant protein derived from the outer membrane protein of *Neisseria meningitidis*, a bacterium responsible for meningitis and other severe infections. This protein has garnered significant attention in the field of vaccine development due to its immunogenic properties and role as an important component in the outer membrane complex of the pathogen. The study of OMP38 aims to elucidate its structure, function, and potential as a vaccine candidate against Neisseria-associated diseases. Research has shown that OMP38 can elicit strong immune responses, making it a suitable target for the design of subunit vaccines. Furthermore, investigations into the recombinant expression of OMP38 in various systems have provided insights into its biological activity and stability, which are crucial for vaccine formulation. By understanding the molecular mechanisms underpinning the immune response triggered by OMP38, researchers hope to enhance vaccine efficacy and contribute to the development of safer and more effective prophylactic measures against meningococcal infection. As antibiotic resistance becomes a growing concern, the exploration of alternative strategies, such as OMP38-based vaccines, is increasingly important for public health initiatives aimed at combating bacterial diseases.
