Analytical Data
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Gene name
QA
- Application
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Alternative Names
QA；Complement C1q subcomponent subunit A
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Species
Human
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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
P02745
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Expression Region
1-245aa
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AA Sequence
MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAIRRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSRGQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFL
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Molecular Weight
26 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 QA (quorum-sensing autoinducer) reconstituted proteins has gained significant attention in the field of molecular biology and biotechnology due to their critical role in microbial communication and biofilm formation. Quorum sensing is a process by which bacterial populations regulate gene expression in response to environmental changes, allowing them to coordinate behaviors such as virulence, bioluminescence, and biofilm development. Understanding the mechanisms behind QA proteins can provide insights into microbial ecology and pathogenesis. Recent advancements in synthetic biology and protein engineering have enabled researchers to redesign and optimize these proteins for synthetic quorum-sensing systems. This research not only aims to elucidate the fundamental principles of bacterial communication but also seeks to explore practical applications, such as developing novel antimicrobial strategies, enhancing bioremediation efforts, and optimizing industrial fermentation processes. Through the reconstitution and characterization of QA proteins, scientists are uncovering the complexities of bacterial interactions and finding potential avenues to disrupt harmful biofilm-associated infections or manipulate microbial communities for biotechnological benefits. Such endeavors can lead to innovative solutions in healthcare and environmental sustainability, highlighting the importance of continued research into quorum-sensing mechanisms and their potential applications.
