Analytical Data
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Gene name
ompP2
- Application
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Alternative Names
ompP2；Outer membrane Protein P2
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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
Q48216
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Expression Region
21-360aa
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AA Sequence
AVVYNNEGTNVELGGRLSVIAEQSNSTRKDQKQQHGELRNAGSRFHIKATHNFGDGFYAQGYLETRLVSDYQSSSDNFGNIITKYAYVTLGNKGFGEVKLGRAKTISDGITSAEDKEYGVLENKEYIPKDGNSVGYTFKGIDGLVLGANYLLAQKREAYKTATATPGEVIAQVISNGVQVGAKYDANNIIAGIAYGRTNYREDLATQDKSGKKQQVNGALSTLGYRFSDLGLLVSLDSGYAKTKNYKDKHEKRYFVSPGFQYELMEDTNVYGNFKYERNSVDQGKKAREHAVLFGVDHKLHKQVLTYIEGAYARTRTNDKGKTEKTEKEKSVGVGLRVYF
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Molecular Weight
44.7 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
OMP-P2, a recombinant protein derived from outer membrane protein P2 of Neisseria meningitidis, has garnered significant attention in the field of vaccine development and immunological research. As a major component of the bacterial outer membrane, OMP-P2 plays a critical role in the virulence and pathogenesis of meningococcal infections, which can lead to severe diseases such as meningitis and sepsis. Due to its immunogenic properties, OMP-P2 serves as a potential target for creating effective vaccines against Neisseria meningitidis, particularly in high-risk populations. Research into OMP-P2 focuses primarily on its ability to elicit robust immune responses, including both humoral and cellular immunity. Additionally, advancements in recombinant DNA technology have facilitated the expression and purification of OMP-P2, allowing for detailed characterization and evaluation of its immunogenicity and safety profiles. By understanding the structure-function relationships of OMP-P2, scientists aim to improve vaccine formulations and enhance their efficacy. Furthermore, studies on OMP-P2 contribute to the broader understanding of bacterial pathogenesis and the development of novel therapeutic strategies against infectious diseases. Overall, the exploration of OMP-P2 as a recombinant protein represents a promising avenue in ongoing efforts to combat Neisseria meningitidis and reduce the burden of meningococcal disease globally.
