Recombinant Escherichia coli Outer membrane protein F (ompF)

Code CSB-YP365808ENV
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Source Yeast
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Code CSB-EP365808ENV-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP365808ENV
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Source Baculovirus
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Code CSB-MP365808ENV
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
ompF
Uniprot No.
Alternative Names
ompF; cmlB; coa; cry; tolF; b0929; JW0912; Outer membrane porin F; Outer membrane protein 1A; Outer membrane protein B; Outer membrane protein F; Outer membrane protein IA; Porin OmpF
Species
Escherichia coli (strain K12)
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Forms pores that allow passive diffusion of small molecules across the outer membrane.; (Microbial infection) It is also a receptor for the bacteriophage T2. Is the major receptor for colicin E5.; (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA-EC536-mediated toxicity.
Gene References into Functions
  1. Trimeric porins, such as ompF, have specific lipopolysaccharide binding sites that are essential for porin biogenesis. PMID: 27493217
  2. Klebsiella pneumoniae OmpK35 and OmpK36 produced larger more permeable channels than their Escherichia coli homologs OmpF and OmpC. PMID: 27645385
  3. Two different centered monoclinic crystals of the E. coli outer-membrane protein OmpF originate from the same building block PMID: 26620074
  4. The site of lipopolysaccharide binding means that ColN will preferably bind at the interface and thus position itself close to the surface of its translocon component, OmpF. PMID: 24589252
  5. they studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. PMID: 23812713
  6. Presence of ordered aliphatic chains close to a positively charged area on the porin surface suggests a position for a lipopolysaccharide binding site on the surface of the major E. coli porins. PMID: 22484237
  7. Data report the structure of the OmpF-OBS1 complex that shows the colicin bound within the porin lumen spanning the membrane bilayer. PMID: 21098297
  8. This D37V mutant expressed reduced cation selectivity, in agreement with the view that D37 in wild-type OmpF is fully ionized, i.e., deprotonated. PMID: 20521145
  9. HPA3P, an analogue of the antimicrobial peptide HP(2-20) isolated from the N-terminal region of the Helicobacter pylori ribosomal protein interacts with OmpF in a voltage- and concentration-dependent manner. PMID: 20180000
  10. These data suggest that OmpF plays a key role in the transportation of positively charged polypyridyl chlororuthenium complexes into E. coli. PMID: 20176402
  11. Separate pathways of anions and cations across the constriction zone of the OmpF pore. PMID: 19932117
  12. study shows that quite different factors account for the selectivity of large channels. The elucidation of these factors is essential for understanding large channel selectivity and its regulation in vivo. PMID: 19134471
  13. deletions of single extracellular loops affect pH sensitivity but not voltage dependence; study has provided some clues on the molecular determinants that underlie two major forms of modulation of OmpF porin activity by transmembrane voltage and acidic pH PMID: 15469993
  14. for the classical porins OmpF and OmpC, our results show that the Cpx envelope stress response system plays a role in regulating their expression PMID: 16077119
  15. OmpR allows distinct stepwise regulation of ompF and ompC transcription, which minimizes their overlapping expression upon changes in the medium osmolarity to achieve the reciprocal expression of ompF and ompC PMID: 16618701
  16. D127 is not a key residue in the control mechanism of the voltage-dependent gating of OmpF PMID: 16858566
  17. OmpF or OmpC can function in the translocon complex of the colicin E2 R-domain and its BtuB receptor PMID: 17548346
  18. Colicin is closely associated with the OmpF-lipid interface, providing evidence that this peripheral pathway may play a role in colicin transmembrane transport. PMID: 18334212
  19. The incremental electron density could be modelled as an extended poly-glycine peptide of at least seven residues. It overlapped the Mg2+ binding site obtained without T83, explaining the absence of peptide binding in the presence of Mg2+. PMID: 18636093

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Subcellular Location
Cell outer membrane; Multi-pass membrane protein.
Protein Families
Gram-negative porin family
Database Links
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