Recombinant E.Coli Type 1 Fimbrin D-Mannose Specific Adhesin (FIMH) Protein (His)

Name: Recombinant E.Coli Type 1 Fimbrin D-Mannose Specific Adhesin (FIMH) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03427P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Escherichia coli (strain K12) fimH.

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Product Overview

Description	Recombinant E.Coli Type 1 Fimbrin D-Mannose Specific Adhesin (FIMH) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P08191
Target Symbol	FIMH
Synonyms	fimH; b4320; JW4283Type 1 fimbrin D-mannose specific adhesin; Protein FimH
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	FACKTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYPFPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRQTNNYNSDDFQFVWNIYANNDVVVPTGGCDVSARDVTVTLPDYPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASFSPAQGVGVQLTRNGTIIPANNTVSLGAVGTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ
Expression Range	22-300aa
Protein Length	Full Length of Mature Protein
Mol. Weight	33.1 kDa
Research Area	Microbiology
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	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.
Subcellular Location	Fimbrium.
Protein Families	Fimbrial protein family
Database References	KEGG: ecj:JW4283 STRING: 316407.85677063

Gene Functions References

Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain. PMID: 29180452
Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions. PMID: 28246638
A mutant missing the type 1 pilus-associated adhesin FimH displayed somewhat reduced persistence within the gut. PMID: 29311232
The authors demonstrated that FimH residues E50 and T53 are crucial for adhesion under flow conditions. PMID: 27816993
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
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
Luteolin decreased the attachment and invasion of UPEC in bladder epithelial cells down-regulating the expression of adhesin fimH gene PMID: 25051393
Data indicate that thiazolylaminomannosides prevented bacterial attachment to the gut by blocking the FimH bacterial adhesin. PMID: 23795713
New promising vaccine combinations based on the FliC antigen against urinary tract infections caused by uropathogenic Escherichia coli. PMID: 23220068
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
FimH elicits an immune response that enhances cell adhesion of Escherichia coli. PMID: 21768279
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
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
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
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
analysis of trimannose versus monomannose interactions with the FimH adhesin of Escherichia coli PMID: 16624825
Stability of the FimH-mannose bond. PMID: 16933977
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
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
analysis of how interdomain interactions in the FimH adhesin of Escherichia coli regulate the affinity to mannose PMID: 17567583
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
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
Deletion of fimH resulted in lost of agglutination ability. PMID: 18438011
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
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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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.