Analytical Data
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Gene name
oprP
- Application
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Alternative Names
oprP；Porin P
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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
P05695
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Expression Region
30-440aa
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AA Sequence
GTVTTDGADIVIKTKGGLEVATTDKEFSFKLGGRLQADYGRFDGYYTNNGNTADAAYFRRAYLEFGGTAYRDWKYQINYDLSRNVGNDSAGYFDEASVTYTGFNPVNLKFGRFYTDFGLEKATSSKWVTALERNLTYDIADWVNDNVGTGIQASSVVGGMAFLSGSVFSENNNDTDGDSVKRYNLRGVFAPLHEPGNVVHLGLQYAYRDLEDSAVDTRIRPRMGMRGVSTNGGNDAGSNGNRGLFGGSSAVEGLWKDDSVWGLEGAWALGAFSAQAEYLRRTVKAERDREDLKASGYYAQLAYTLTGEPRLYKLDGAKFDTIKPENKEIGAWELFYRYDSIKVEDDNIVVDSATREVGDAKGKTHTLGVNWYANEAVKVSANYVKAKTDKISNANGDDSGDGLVMRLQYVF
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Molecular Weight
61.2 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
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Protein Description
OprP is a porin protein found in Pseudomonas aeruginosa, a versatile and opportunistic pathogen known for its resistance to antibiotics and ability to thrive in various environments. The study of OprP is significant due to its role in nutrient transport, particularly in the uptake of phosphate, which is essential for bacterial survival and virulence. Understanding the structure and function of OprP can provide insights into the metabolic adaptations of Pseudomonas aeruginosa, as well as its interaction with host organisms. The interest in OprP also stems from its potential as a target for novel antimicrobial therapies. Research has focused on the recombinant expression of OprP, which allows for detailed biochemical and biophysical studies, including investigations into its transport mechanisms and interactions with other cellular components. By elucidating the functional properties of OprP, researchers hope to leverage this knowledge to combat infections caused by Pseudomonas aeruginosa, contributing to the development of new strategies for treating drug-resistant bacterial infections. Overall, the study of OprP represents a crucial intersection of microbiology, biochemistry, and therapeutic development, addressing the pressing challenge of antibiotic resistance.
