Analytical Data
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Gene name
ffp
- Application
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Alternative Names
ffp；sfp；4'-phosphopantetheinyl transferase ffp
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MKIYGIYMDRPLSQEETDRLMSFVSAEKREKCRRFYHKEDAHRTLLGDVLVRSVISEQYQLNKADIRFSAQEYGKPCIPDLPNAHFNISHSGHWVIGAFDSDPIGVDIEKMKPISLGIAERFFSKNEYSDLLSKHKDEQNDYFYHLWSMKESFIKQEGKGLSLPLDSFSVRLHEDGRVSVELPEHHTPCFIKTYEVDPGYKMAVCAARPDFPEDITMISYEALL
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Molecular Weight
25.9 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 research on FFP (Fusion-Formed Proteins) recombinant proteins has gained significant momentum due to their potential applications in various fields, including biotechnology, medicine, and environmental science. FFPs are engineered proteins created by combining multiple protein domains or functional units, which allows for the tailoring of specific properties and activities. This approach is particularly relevant in the context of drug development, where the ability to enhance the stability, solubility, and binding affinity of therapeutic proteins can lead to more effective treatments. Additionally, FFPs play a crucial role in the development of vaccines, biomaterials, and diagnostic tools, reflecting their versatility. Recent advances in genetic engineering techniques, such as CRISPR and synthetic biology, have facilitated the design and production of these proteins, paving the way for innovative solutions to address complex biological challenges. Understanding the structure-function relationship of FFPs is also essential for optimizing their performance in industrial applications, including enzyme engineering and biocatalysis. Overall, the exploration of FFP recombinant proteins represents a thriving area of research with the potential to transform both scientific knowledge and practical applications.
