Analytical Data
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Gene name
patA
- Application
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Alternative Names
PAT-1
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Species
Nostoc sp.
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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
P39048
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Expression Region
1-379aa
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Molecular Weight
50.2 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
PatA is a protein that plays a significant role in the pathogenesis of certain bacterial species, particularly in the context of antibiotic resistance mechanisms. Research into PatA has gained prominence due to its involvement in the biosynthesis of cyclic di-GMP, a crucial secondary messenger that regulates various cellular processes, including biofilm formation and virulence factors. The understanding of PatA's structure and function is critical, as it offers insights into potential targets for novel antimicrobial therapies. By generating recombinant forms of PatA, researchers aim to elucidate its biochemical properties and the mechanisms by which it contributes to bacterial survival and adaptation. Studies involving the expression and purification of PatA can lead to the identification of specific inhibitors, offering a strategic approach to combat bacterial infections that exhibit multidrug resistance. Furthermore, investigating the interactions of PatA with other molecular players within the bacterial cell can enhance our comprehension of its role in cellular signaling pathways, thus potentially guiding the development of more effective treatment options. As antibiotic resistance continues to pose a global health threat, the exploration of proteins like PatA is essential for advancing our understanding of bacterial physiology and enabling innovative solutions for infection control.
