Analytical Data
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Gene name
ffp
- Application
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Alternative Names
Fengycin synthase-activating enzyme (sfp)
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Species
Bacillus subtilis
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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
Q9F4F7
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Expression Region
1-224aa
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Molecular Weight
31.0 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
FFP (Fractionated Freeze-Preserved) recombinant proteins represent a significant advancement in the field of biotechnology and protein engineering. The development of these proteins is rooted in the need for therapeutic agents that can be produced reliably and safely, particularly for use in medicine and research. Traditional methods of protein production often faced challenges such as low yield, high cost, and the risk of contamination with pathogens. FFP recombinant proteins, produced through recombinant DNA technology, offer a controlled and scalable solution, allowing for the mass production of proteins with specific functionalities. The freeze-preservation process enhances the stability and shelf-life of these proteins, making them suitable for various applications, including vaccine development, enzyme therapy, and research tools. Moreover, the study of FFP recombinant proteins has opened avenues for innovative treatments in areas like immunology, oncology, and genetic disorders. As the understanding of protein structure and function deepens, ongoing research in this area continues to explore novel formulations and delivery methods, further expanding the potential of FFP recombinant proteins in therapeutic contexts. The integration of advanced bioprocessing techniques and analytical methods ensures that these proteins meet rigorous quality standards, paving the way for their use in clinical applications and ultimately improving patient outcomes.
