Analytical Data
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Gene name
pilA
- Application
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Alternative Names
pilA；Type IV major pilin Protein PilA
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Species
E.coli
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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
P04128
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Expression Region
24-182aa
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AA Sequence
AATTVNGGTVHFKGEVVNAACAVDAGSVDQTVQLGQVRTASLAQEGATSSAVGFNIQLNDCDTNVASKAAVAFLGTAIDAGHTNVLALQSSAAGSATNVGVQILDRTGAALTLDGATFSSETTLNNGTNTIPFQARYFATGAATPGAANADATFKVQYQ
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Molecular Weight
31.8kDa
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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
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Protein Description
PilA is a key component of the type IV pili, which are hair-like appendages on the surface of many bacteria, playing critical roles in adhesion, motility, and biofilm formation. The study of PilA recombinant protein has gained attention due to its importance in understanding bacterial pathogenesis and host interaction. In specific bacteria, such as Pseudomonas aeruginosa, PilA is essential for various physiological processes, including surface attachment and the initiation of infections, making it a potential target for therapeutic interventions. Research on PilA recombinant proteins focuses on elucidating their structure and function, as well as their interactions with other cellular components. The expression and purification of recombinant PilA from host systems enable researchers to conduct biophysical and biochemical analyses, paving the way for the development of novel antibacterial strategies. Understanding the molecular mechanisms involving PilA can contribute to designing effective vaccines or inhibitors that disrupt pilus formation, ultimately aiding in the control of bacterial infections. Moreover, recombinant PilA proteins are explored in vaccine development, as they can elicit immune responses that may provide protection against infections caused by pilus-expressing pathogens. Overall, the study of PilA recombinant proteins is crucial for advancing our knowledge of bacterial biology and developing new approaches to combat antibiotic-resistant bacteria.
