Analytical Data
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Gene name
traY
- Application
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Alternative Names
traY；Relaxosome Protein TraY
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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
P33789
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Expression Region
1-20aa
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AA Sequence
MKEPKSNIRKLIDIGGLIGR
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Molecular Weight
18.2 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
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Protein Description
TraY protein, a key regulator in the process of bacterial conjugation, plays a critical role in the transfer of genetic material between bacteria. This process not only facilitates the spread of antibiotic resistance but also contributes to genetic diversity within microbial communities. TraY is known to be part of the plasmid-encoded tra (transfer) operon, responsible for the initiation and regulation of the conjugation process in Gram-negative bacteria. Research into the TraY protein has gained significance due to the increasing incidence of multi-drug resistant bacteria and the urgent need for new strategies to combat these pathogens. Understanding the structural and functional aspects of TraY can provide insights into its role in the early stages of conjugation, including the formation of the mating pair and the stabilization of the DNA transfer process. Furthermore, the study of TraY offers potential avenues for the development of novel antimicrobial therapies that could inhibit plasmid transfer, thereby curbing the spread of resistance genes. Advances in recombinant DNA technology have enabled scientists to produce TraY in vitro, allowing for detailed biochemical and biophysical studies. These investigations can elucidate the protein's interactions with other components of the conjugation machinery and identify potential inhibitors. Overall, TraY protein research is crucial not only for understanding bacterial conjugation mechanisms but also for developing innovative strategies to address the global challenge of antibiotic resistance.
