Analytical Data
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Gene name
srtA
- Application
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Alternative Names
Sortase A; Surface protein sorting A; srtA; Staphylococcus aureus (strain NCTC 8325 / PS 47); Hydrolase; Protease; Thiol protease; 3.4.22.70
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q2FV99
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Expression Region
Q60-K206, P94S, D160N, D165A, G167E, K196T
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Protein Length
Partial
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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 research on srtA (sortase A) recombinant proteins is primarily driven by the importance of sortase enzymes in bacterial pathogenesis and their potential as targets for therapeutic intervention. SrtA plays a crucial role in the process of anchoring surface proteins to the cell wall of Gram-positive bacteria, such as Staphylococcus aureus, which is associated with various infectious diseases. This enzyme facilitates the covalent attachment of substrate proteins that are vital for bacterial adherence, colonization, and immune evasion. Given the rising incidence of antibiotic resistance, there is an urgent need for innovative approaches in developing anti-infective strategies. Studying srtA recombinantly enables researchers to elucidate the enzyme's structure, function, and mechanism of action, providing insights into its role in bacterial virulence. Moreover, recombinant srtA can be utilized in high-throughput screening assays for novel inhibitors that may serve as potential drug candidates. The findings from this research contribute not only to our understanding of bacterial biology but also hold promise for the development of new antimicrobial therapies that could circumvent current resistance mechanisms. Thus, the exploration of srtA recombinant proteins is a significant area of study, reflecting the broader efforts to combat bacterial infections in an era of increasing antibiotic resistance.
