Analytical Data
-
基因名
FLII
- Application
-
别名
FLII；FLIL；Protein flightless-1 homolog
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q13045
-
表达区间
495-827aa
-
氨基酸序列
VGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVREEMGDESEEFLQVFDNDISYIEGGTASGFYTVEDTHYVTRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFWEALGGEPSEIKKHVPEDFWPPQPKLYKVGLGLGYLELPQINYKLSVEHKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHRPRHATVSRSLEGTEAAAEQKLISEEDL
-
分子量
44.6 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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 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.
