Analytical Data
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Gene name
OMP
- Application
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Alternative Names
OMP;Olfactory marker Protein
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Species
Human
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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
P47874
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Expression Region
1-163aa
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AA Sequence
MAEDRPQQPQLDMPLVLDQGLTRQMRLRVESLKQRGEKRQDGEKLLQPAESVYRLNFTQQQRLQFERWNVVLDKPGKVTITGTSQNWTPDLTNLMTRQLLDPTAIFWRKEDSDAIDWNEADALEFGERLSDLAKIRKVMYFLVTFGEGVEPANLKASVVFNQL
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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
OMP (Outer Membrane Protein) refers to a class of proteins located in the outer membrane of Gram-negative bacteria. These proteins play critical roles in various biological processes, including nutrient transport, immune evasion, and maintaining membrane integrity. Research on OMPs has gained significant interest due to their potential applications in vaccine development, drug delivery systems, and as targets for antibiotics. Understanding the structure and function of these proteins is crucial for elucidating bacterial pathogenesis and developing new therapeutic strategies. Moreover, the ability to produce recombinant OMPs using techniques like recombinant DNA technology allows researchers to study these proteins in detail, facilitating the identification of epitopes for vaccine design and the development of diagnostic tools. OMPs have also been employed as carriers for the delivery of foreign antigens, enhancing the immune response in various vaccine formulations. Given the rising issue of antibiotic resistance, exploring OMPs as novel drug targets presents a promising avenue for overcoming challenges in current antimicrobial therapies. Thus, ongoing research into OMPs not only deepens our understanding of fundamental bacterial biology but also opens new pathways for innovative biomedical applications.
