Analytical Data
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Gene name
troA
- Application
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Alternative Names
Tromp-1 (troMP1)
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Species
Treponema pallidum
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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
P96116
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Expression Region
23-308aa
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Molecular Weight
38.2 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
Related Products
Protein Description
The study of troA recombinant protein centers around its role in bacterial physiology and antibiotic resistance. TroA, or the "transition metal transport protein A," is crucial for the uptake of essential metal ions, such as zinc and manganese, which are vital for various enzymatic processes and maintain cellular homeostasis in bacteria. Researchers have identified that bacteria, including pathogens, often rely on metal acquisition systems like troA to thrive in the host environment and evade immune responses. Moreover, understanding the molecular mechanisms by which troA mediates metal transport could provide insights into bacterial survival strategies and contribute to the development of novel antimicrobial therapies. By producing troA as a recombinant protein, scientists aim to elucidate its structural and functional properties, investigate its interactions with metal ions, and explore its potential as a target for drug design. This research not only enhances our understanding of bacterial nutrient acquisition but also holds promise for addressing the pressing challenge of antibiotic resistance in medical microbiology.
