Analytical Data
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Gene name
FLII
- Application
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Alternative Names
FLII；FLIL；Protein flightless-1 homolog
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Species
Human
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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
Q13045
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Expression Region
495-827aa
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AA Sequence
VGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVREEMGDESEEFLQVFDNDISYIEGGTASGFYTVEDTHYVTRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFWEALGGEPSEIKKHVPEDFWPPQPKLYKVGLGLGYLELPQINYKLSVEHKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHRPRHATVSRSLEGTEAAAEQKLISEEDL
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Molecular Weight
44.6 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
The study of FLII (Fad-dependent luciferase interactor) recombinant protein has gained significant attention due to its potential applications in biotechnology and molecular biology. FLII is known for its role in bioluminescence, particularly in the context of luciferase enzymes, which have been extensively used as biosensors in cellular and environmental monitoring. Research into the recombinant expression of FLII aims to enhance our understanding of protein interactions and functions, as well as to exploit its luminescent properties for innovative applications. The ability to engineer FLII through recombinant DNA technology facilitates the production of modified variants with tailored functionalities, paving the way for advancements in imaging, drug discovery, and the development of reporter systems that can provide real-time insights into cellular processes. Moreover, as the scientific community increasingly focuses on sustainable and efficient alternatives in research, FLII-based systems could contribute to greener methodologies in various assays. Exploring FLII's structure-function relationships and optimizing its expression conditions in host systems are crucial for maximizing its utility and performance in experimental setups. Overall, the ongoing research on FLII recombinant protein holds promise for a wide range of applications, contributing to the advancement of science and technology in diverse fields.
