Recombinant E.Coli Outer Membrane Protein F (OMPF) Protein (His&Myc)

Name: Recombinant E.Coli Outer Membrane Protein F (OMPF) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-03468P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant E.Coli Outer Membrane Protein F (OMPF) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P02931
Target Symbol	OMPF
Synonyms	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)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	AEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF
Expression Range	23-362aa
Protein Length	Full Length of Mature Protein
Mol. Weight	44.1 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cell outer membrane; Multi-pass membrane protein.
Protein Families	Gram-negative porin family
Database References	KEGG: ecj:JW0912 STRING: 316385.ECDH10B_0999

Gene Functions References

Trimeric porins, such as ompF, have specific lipopolysaccharide binding sites that are essential for porin biogenesis. PMID: 27493217
Klebsiella pneumoniae OmpK35 and OmpK36 produced larger more permeable channels than their Escherichia coli homologs OmpF and OmpC. PMID: 27645385
Two different centered monoclinic crystals of the E. coli outer-membrane protein OmpF originate from the same building block PMID: 26620074
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
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
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
Data report the structure of the OmpF-OBS1 complex that shows the colicin bound within the porin lumen spanning the membrane bilayer. PMID: 21098297
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
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
These data suggest that OmpF plays a key role in the transportation of positively charged polypyridyl chlororuthenium complexes into E. coli. PMID: 20176402
Separate pathways of anions and cations across the constriction zone of the OmpF pore. PMID: 19932117
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
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
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
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
D127 is not a key residue in the control mechanism of the voltage-dependent gating of OmpF PMID: 16858566
OmpF or OmpC can function in the translocon complex of the colicin E2 R-domain and its BtuB receptor PMID: 17548346
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
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

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.