Analytical Data
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Gene name
FLP1
- Application
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Alternative Names
Protein Able
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Species
Saccharomyces cerevisiae
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P03870
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Expression Region
1-423aa
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Molecular Weight
54.1 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
FLP1 recombinase is a site-specific recombinase derived from the yeast Saccharomyces cerevisiae, specifically from the FLP (.flip recombinase) gene. It plays a crucial role in genetic engineering and synthetic biology due to its ability to catalyze the excision, integration, and inversion of specific DNA sequences at defined recognition sites known as FRT (FLP Recognition Target) sites. The study of FLP1 recombinase has gained prominence because of its applications in creating knockout and transgenic organisms, facilitating gene editing, and aiding in the development of advanced therapeutic strategies, including gene therapy and the generation of model organisms for disease studies. Researchers have focused on understanding the molecular mechanisms underlying FLP1 activity, its interactions with DNA, and the factors influencing recombination efficiency. Additionally, the engineering of FLP1 for enhanced specificity and efficiency has opened new avenues for its use in genome editing technologies. Current research also explores the potential of FLP1 recombinase in combination with other genetic tools, such as Cre-lox systems, to create sophisticated genetic circuits and manipulate the genome in a more versatile manner. Overall, the ongoing investigations into FLP1 recombinase not only highlight its importance in fundamental biological research but also emphasize its significance in practical applications, with the aim of advancing genetic manipulation techniques and developing innovative therapeutic approaches.
