Analytical Data
-
Gene name
ompF
- Application
-
Alternative Names
ompF；SLAM；Signaling lymphocytic activation molecule
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P02931
-
Expression Region
23-362aa
-
AA Sequence
AEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF
-
Molecular Weight
44.5 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
OmpF is a major outer membrane porin found in Escherichia coli, which plays a critical role in the transport of small molecules across the bacterial outer membrane. As a model for studying membrane proteins, OmpF has garnered significant interest due to its relatively simple structure and functional importance in bacterial physiology. Research into the recombinant expression of OmpF enables scientists to explore its biophysical properties, transport mechanisms, and interactions with antibiotics, which can provide insights into bacterial resistance mechanisms. Additionally, understanding OmpF's structure-function relationship is vital for the development of novel antimicrobial strategies and biomaterials. The challenges of producing functional OmpF in heterologous systems, such as inclusion body formation and proper folding, have driven advances in biotechnology, improving expression systems and refolding protocols. This research holds promise not only for fundamental microbiology but also for clinical applications, as better understanding of porins may lead to innovative approaches in combatting multidrug-resistant bacterial infections.
