Recombinant Pseudomonas aeruginosa ompF Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-10246P

Recombinant Pseudomonas aeruginosa ompF Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-10246P
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Product Overview

Host Species Pseudomonas aeruginosa
Accession P13794
Synonym orpF Putative outer membrane porin F protein YE1563
Description Recombinant Pseudomonas aeruginosa ompF Protein (His tag) was expressed in E.coli. It is a Full length protein
Source E.coli
AA Sequence QGQNSVEIEAFGKRYFTDSVRNMKNADLYGGSIGYFLTDDVELALSYGEY HDVRGTYETGNKKVHGNLTSLDAIYHFGTPGVGLRPYVSAGLAHQNITNI NSDSQGRQQMTMANIGAGLKYYFTENFFAKASLDGQYGLEKRDNGHQGEW MAGLGVGFNFGGSKAAPAPEPVADVCSDSDNDGVCDNVDKCPDTPANVTV DANGCPAVAEVVRVQLDVKFDFDKSKVKENSYADIKNLADFMKQYPSTST TVEGHTDSVGTDAYNQKLSERRANAVRDVLVNEYGVEGGRVNAVGYGESR PVADNATAEGRAINRRVEAEVEAEAK
Molecular Weight 39 kDa including tags
Purity >85% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Has porin activity, forming small water-filled channels. Also has a structural role in determining cell shape and ability to grow in low-osmolarity medium.
Subcellular Location Cell outer membrane; Multi-pass membrane protein.
Protein Families OmpA family
Database References

Gene Functions References

  1. OprF (an outer membrane porin, highly conserved in the Pseudomonas) binds human C3b. PMID: 25964476
  2. LecB binds to the outer membrane protein OprF PMID: 23056489
  3. oprF transcription was increased in response to low NaCl or high sucrose concentrations, and this induced transcription was strongly impaired in the absence of SigX. PMID: 22685281
  4. Prevention of disulfide bond formation in OprF increases its pore-forming activity. PMID: 20978537
  5. This is the first study showing a link between OprF, PQS synthesis, T3SS, and virulence factor production PMID: 21189321
  6. Data show that the recombinant plasmid pIRES-tPA-OprF-MyD88 has been successfully constructed and tPA-OprF and MyD88 protein can be highly expressed in transfected cells. PMID: 19257978
  7. findings suggest that OprF could adopt two alternative conformations in the outer membrane and that folding is thermoregulated PMID: 15528532
  8. findings demonstrate that interferon-gamma binds to an outer membrane protein in Pseudomonas aeruginosa, OprF, resulting in the expression of a quorum-sensing dependent virulence determinant, the PA-I lectin PMID: 16051797
  9. analysis of OprF from Pseudomonas aeruginosa PMID: 16397890
  10. OprF exists in two different conformations PMID: 16595653
  11. analysis of Pseudomonas aeruginosa porin OprF PMID: 16617058
  12. Major outer membrane protein F (OprF) is identified as a protein with important functions; mutant Pseudomonas aeruginosa deficient in OprF negates the antibacterial role of host neutrophil elastase both in vitro and in a pneumonia model. PMID: 18802098

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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