Analytical Data
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Gene name
folD
- Application
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Species
Pseudomonas aeruginosa
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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
A6V726
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Expression Region
1-284aa
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Molecular Weight
38.0 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 folded recombinant proteins has gained significant importance in the fields of biotechnology and medicine due to their critical roles in various biological processes and therapeutic applications. Recombinant proteins, which are produced through the expression of genes in host organisms, allow for the creation of proteins that may be present in low abundance in nature or even entirely synthetic proteins with customized functions. Understanding the folding mechanisms of these proteins is essential, as proper folding is vital for their structural integrity, biological activity, and stability. Misfolded proteins can lead to various diseases, including neurodegenerative disorders. Consequently, researchers are focusing on optimizing expression systems, improving folding pathways, and enhancing yield and purity during protein production. Advancements in purification techniques and analytical methods have further enabled the characterization of protein structures and functions. As a result, folded recombinant proteins are becoming pivotal in drug development, diagnostics, and vaccine design, exemplifying their utility in both basic and applied sciences. The ongoing exploration of their properties continues to contribute to innovations in therapeutic strategies, offering potential solutions for a range of health challenges.
