Analytical Data
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Gene name
tfpQ
- Application
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Alternative Names
tfpQ；Fimbrial Protein Q
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Species
Moraxella bovis
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P07640
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Expression Region
7-157aa
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AA Sequence
FTLIELMIVIAIIGILAAIALPAYQDYISKSQTTRVVGELAAGKTAVDAALFEGKTPKLGKAANDTEEDIGLTTTGGTARSNLMSSVNIGGGAFATGAGTLEATLGNRANKDIAGAVITQSRDAEGVWTCTINGSAAPGWKSKFVPTGCKE
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Molecular Weight
20.9 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
The study of tfpQ recombinant protein is situated within the broader context of bacterial pathogenesis and the development of novel therapeutic strategies. TfpQ is a key component of the type IV pili (T4P) system in certain bacteria, which plays a crucial role in adhesion, motility, and biofilm formation. These pili are vital for the bacteria’s ability to colonize host tissues and are implicated in various infectious diseases, making them attractive targets for drug development and vaccine design. Understanding the structure and function of the tfpQ protein can provide insights into T4P assembly and regulation, potentially revealing unique vulnerabilities in pathogenic bacteria. Recent advances in genetic engineering and protein expression techniques enable the production of recombinant tfpQ, facilitating the study of its properties and interactions. By investigating the immunogenicity and functional properties of tfpQ, researchers aim to develop effective strategies for preventing bacterial infections, particularly in the face of rising antibiotic resistance. Furthermore, exploring the role of tfpQ in bacterial virulence can enhance our understanding of microbial ecology and the host-pathogen relationship, paving the way for innovative therapeutic approaches against infections.
