Recombinant Escherichia coli Type 1 fimbrin D-mannose specific adhesin (fimH)

In Stock
Code CSB-YP362349ENV
Size $436
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
fimH
Uniprot No.
Research Area
Others
Alternative Names
fimH; b4320; JW4283Type 1 fimbrin D-mannose specific adhesin; Protein FimH
Species
Escherichia coli (strain K12)
Source
Yeast
Expression Region
22-300aa
Target Protein Sequence
FACKTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYPFPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRQTNNYNSDDFQFVWNIYANNDVVVPTGGCDVSARDVTVTLPDYPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASFSPAQGVGVQLTRNGTIIPANNTVSLGAVGTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
31.1kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or 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
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is 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°C/-80°C. 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
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

Customer Reviews and Q&A

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 Q&A
Q:

Because this is “In Stock” and lyophilized protein, does that mean the free endotoxin removal is not available?
I understand that the likelihood of endotoxin presence is low in yeast expressed proteins however it is still possible through contamination of reagents etc. If we want to order this protein is the endotoxin removal service request still available and would it still be noted on the COA?

A:
Thanks for your inquiry. If you need the endotoxin removal service, we can firstly dissolve the lyophilized protein and then process the endotoxin removal,
To guarantee the final endotoxin level is less than 1.0 EU per 1μg of the protein by the LAL method, which will be shown on the COA report.
And the endotoxin removed protein will be provided in liquid form.

Target Background

Function
Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.
Gene References into Functions
  1. Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain. PMID: 29180452
  2. Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions. PMID: 28246638
  3. A mutant missing the type 1 pilus-associated adhesin FimH displayed somewhat reduced persistence within the gut. PMID: 29311232
  4. The authors demonstrated that FimH residues E50 and T53 are crucial for adhesion under flow conditions. PMID: 27816993
  5. In the absence of tensile force, the FimH pilin domain allosterically accelerates spontaneous ligand dissociation from the FimH lectin domain by 100,000-fold. PMID: 26948702
  6. mouse urothelium responds to the adhesion of type 1-fimbriated UPEC by activating dual ligand/receptor system, one between FimH adhesin and uroplakin Ia and another between lipopolysaccharide and Tlr4. PMID: 26549759
  7. Luteolin decreased the attachment and invasion of UPEC in bladder epithelial cells down-regulating the expression of adhesin fimH gene PMID: 25051393
  8. Data indicate that thiazolylaminomannosides prevented bacterial attachment to the gut by blocking the FimH bacterial adhesin. PMID: 23795713
  9. New promising vaccine combinations based on the FliC antigen against urinary tract infections caused by uropathogenic Escherichia coli. PMID: 23220068
  10. analyzed mutational patterns in the fimH gene of mucosa-associated E. coli strains isolated from IBD and non-IBD pediatric patients to investigate microevolution of this genetic trait; study found some FimH variants that seem to be more involved than others in evolution of inflammatory bowel disease pathogenesis PMID: 22290143
  11. FimH elicits an immune response that enhances cell adhesion of Escherichia coli. PMID: 21768279
  12. Study presents the crystal structure of FimH incorporated into the multiprotein fimbrial tip, where the anchoring (pilin) domain of FimH interacts with the mannose-binding (lectin) domain and causes a twist in the beta sandwich fold of the latter. PMID: 20478255
  13. Co-immunoprecipitation experiments in the presence of alpha-methyl mannose verified the binding of Escherichia coli FimH to ATP synthase beta-subunit of human brain microvascular endothelial cells. PMID: 20067530
  14. the single A62S mutation altered phase variation, reducing the proportion of piliated cells, reduced mannose binding 8-fold, and decreased bladder colonization 30-fold in vivo compared to wild-type PMID: 20018753
  15. FimH adhesin activated the murine microglial cell line, BV-2, which resulted in the production of nitric oxide and the release of tumor necrosis factor-alpha. PMID: 16036224
  16. analysis of trimannose versus monomannose interactions with the FimH adhesin of Escherichia coli PMID: 16624825
  17. Stability of the FimH-mannose bond. PMID: 16933977
  18. findings indicate that FimH induces host cell signalling cascades that are involved in E. coli K1 invasion of human brain microvascular endothelial cells (HBMEC) and CD48 is a putative HBMEC receptor for FimH PMID: 17222190
  19. Functional trade-offs may determine the natural populational instability of this mutation or other pathoadaptive FimH mutations that confer dramatic increases in 1M binding strength. PMID: 17502398
  20. analysis of how interdomain interactions in the FimH adhesin of Escherichia coli regulate the affinity to mannose PMID: 17567583
  21. Data show that removal of the cysteine bond in the mannose-binding domain of FimH did not affect FimH-mannose binding under static or low shear conditions, but the adhesion level was substantially decreased under increased fluid flow. PMID: 17697252
  22. integrin-like allosteric link between the binding pocket and the interdomain conformation can serve as the basis for the catch bond property of FimH and, possibly, other adhesive proteins. PMID: 18174167
  23. Deletion of fimH resulted in lost of agglutination ability. PMID: 18438011
  24. Naturally occurring mutations in the signal peptides of the adhesive, tip-associated subunit of type 1 fimbriae (FimH) are positively selected in uropathogenic Escherichia coli. PMID: 18664574
  25. The authors show by cryo-electron microscopy that FimH binding to the extracellular domain of UP Ia induces global conformational changes in the entire UP receptor complex, including a coordinated movement of the tightly bundled transmembrane helices. PMID: 19577575

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Subcellular Location
Fimbrium.
Protein Families
Fimbrial protein family
Database Links

KEGG: ecj:JW4283

STRING: 316407.85677063

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