Analytical Data
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Gene name
yafQ
- Application
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Alternative Names
/
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Species
Haemophilus influenzae
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P44041
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Expression Region
1-102aa
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Molecular Weight
19.4 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
YafQ is a well-characterized protein found in *Escherichia coli* that belongs to the YafQ family of proteins, which are associated with stress response and cellular regulation. The increasing interest in YafQ has been driven by its potential role in modulating bacterial virulence and biofilm formation, crucial factors in chronic infections. As a member of the larger family of biofilm-regulating proteins, YafQ has been shown to influence the synthesis of signaling molecules and affect the expression of genes involved in biofilm development. For researchers, understanding YafQ's functional mechanisms could provide insights into bacterial behavior in response to environmental stressors and may identify novel targets for antimicrobial therapy. The recombinant expression of YafQ in various systems facilitates the exploration of its functional properties and interactions with other cellular components. There is a growing body of literature examining the structural and biochemical properties of YafQ, highlighting its potential as a therapeutic target. Moreover, studying this protein’s role in bacterial communication systems, like quorum sensing, enhances our understanding of microbial ecology and pathogenesis. Consequently, the research on YafQ not only contributes to the fundamental knowledge of bacterial physiology but also holds promise for developing strategies to combat resistant bacterial strains and improve clinical outcomes for infections related to biofilm formation.
