Analytical Data
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Gene name
ompP2
- Application
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Alternative Names
ompP2; Outer membrane protein P2; OMP P2
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Species
Haemophilus influenzae
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Source
E. coli
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Tag
N- His & C- Myc
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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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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
The ompP2 protein, derived from the outer membrane of bacteria, plays a crucial role in various biological processes and has garnered significant interest in the field of molecular biology and biotechnology. OmpP2 is part of the porin family, which facilitates the transport of small molecules across the bacterial outer membrane, thus impacting nutrient uptake, antibiotic resistance, and adaptation to environmental stresses. Research on ompP2 is essential for several reasons: it can provide insights into bacterial pathogenesis and survival mechanisms, serve as a potential target for novel antimicrobial therapies, and aid in the development of biosensors or drug delivery systems. Furthermore, the ability to recombinantly express and purify ompP2 allows for in-depth structural and functional analyses, contributing to our understanding of membrane proteins and their interactions. The exploration of ompP2 thus holds promise for both fundamental research in microbiology and practical applications in combating antibiotic resistance and enhancing biotechnological innovations. As a result, intensive studies aim to elucidate its structure-function relationship, revealing how this protein can be exploited for therapeutic and industrial purposes.
