Analytical Data
-
Gene name
oprF
- Application
-
Alternative Names
oprF; PA1777; Outer membrane porin F
-
Species
Pseudomonas aeruginosa
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P13794
-
Expression Region
25-350aa
-
Molecular Weight
39.3 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
OprF is a major outer membrane protein found in Pseudomonas aeruginosa, a versatile opportunistic pathogen known for its antibiotic resistance and role in chronic infections, particularly in cystic fibrosis patients. Research on OprF has gained significance due to its multifaceted roles in bacterial pathogenesis, including biofilm formation, immune evasion, and interaction with host cells. The protein is also proposed as a potential target for vaccine development and therapeutic interventions. However, the functional mechanisms of OprF remain poorly understood, largely due to challenges in characterizing the protein in its native state. Consequently, the development of recombinant OprF proteins has emerged as a pivotal avenue for research, enabling detailed studies of its structure, function, and interactions. By producing OprF recombinantly, researchers can utilize various expression systems to generate large quantities of the protein, facilitating biochemical and immunological assays. Such studies are vital for elucidating the role of OprF in Pseudomonas aeruginosa virulence and for investigating its potential as a target for vaccine formulation and therapeutic design, ultimately contributing to the development of new strategies to combat infections caused by this pathogen.
