Luciferase
(Synonyms: 荧光素酶) 目录号 : GC36492
Luciferase，来自Vibrio fischeri，可用于评估生物发光细菌的光发射和氧消耗动力学。
Cas No.:9014-00-0
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Luciferase from Vibrio fischeri has also been used in a study to investigate the sensitivity of dark mutants of various strains of luminescent bacteria to reactive oxygen species.
| Cas No. | 9014-00-0 | SDF | |
| 别名 | 荧光素酶 | ||
| 分子式 | 分子量 | ||
| 溶解度 | Water: 50 mg/mL | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Using Luciferase Reporter Assays to Identify Functional Variants at Disease-Associated Loci
Methods Mol Biol 2018;1706:303-319.PMID:29423806DOI:10.1007/978-1-4939-7471-9_17.
The genomic era, highlighted by large scale, genome-wide association studies (GWAS) for both common and rare diseases, have identified hundreds of disease-associated variants. However, most of these variants are not disease causing, but instead only provide information about a potential proximal functional variant through linkage disequilibrium. It is critical that these functional variants be identified, so that their role in disease risk can be ascertained. Luciferase assays are an invaluable tool for identifying and characterizing functional variants, allowing investigations of gene expression, intracellular signaling, transcription factors, receptor activity, and protein folding. In this chapter, we provide an overview of the different ways that Luciferase assays can be used to validate functionality of a variant.
Split-luciferase complementary assay: applications, recent developments, and future perspectives
Anal Bioanal Chem 2014 Sep;406(23):5541-60.PMID:25002334DOI:10.1007/s00216-014-7980-8.
Bioluminescent systems are considered as potent reporter systems for bioanalysis since they have specific characteristics, such as relatively high quantum yields and photon emission over a wide range of colors from green to red. Biochemical events are mostly accomplished through large protein machines. These molecular complexes are built from a few to many proteins organized through their interactions. These protein-protein interactions are vital to facilitate the biological activity of cells. The split-luciferase complementation assay makes the study of two or more interacting proteins possible. In this technique, each of the two domains of Luciferase is attached to each partner of two interacting proteins. On interaction of those proteins, Luciferase fragments are placed close to each other and form a complemented Luciferase, which produces a luminescent signal. Split Luciferase is an effective tool for assaying biochemical metabolites, where a domain or an intact protein is inserted into an internally fragmented Luciferase, resulting in ligand binding, which causes a change in the emitted signals. We review the various applications of this novel luminescent biosensor in studying protein-protein interactions and assaying metabolites involved in analytical biochemistry, cell communication and cell signaling, molecular biology, and the fate of the whole cell, and show that luciferase-based biosensors are powerful tools that can be applied for diagnostic and therapeutic purposes.
Re-engineering of Bacterial Luciferase; For New Aspects of Bioluminescence
Curr Protein Pept Sci 2018;19(1):16-21.PMID:27875968DOI:10.2174/1389203718666161122104530.
Bacterial luminescence is the end-product of biochemical reactions catalyzed by the Luciferase enzyme. Nowadays, this fascinating phenomenon has been widely used as reporter and/or sensors to detect a variety of biological and environmental processes. The enhancement or diversification of the Luciferase activities will increase the versatility of bacterial luminescence. Here, to establish the strategy for Luciferase engineering, we summarized the identity and relevant roles of key amino acid residues modulating Luciferase in Vibrio harveyi, a model luminous bacterium. The current opinions on crystal structures and the critical amino acid residues involved in the substrate binding sites and unstructured loop have been delineated. Based on these, the potential target residues and/or parameters for enzyme engineering were also suggested in limited scale. In conclusion, even though the accurate knowledge on the bacterial Luciferase is yet to be reported, the structure-guided site-directed mutagenesis approaches targeting the regulatory amino acids will provide a useful platform to re-engineer the bacterial Luciferase in the future.
Expanding Luciferase reporter systems for cell-free protein expression
Sci Rep 2022 Jul 7;12(1):11489.PMID:35798760DOI:10.1038/s41598-022-15624-6.
Luciferases are often used as a sensitive, versatile reporter in cell-free transcription-translation (TXTL) systems, for research and practical applications such as engineering genetic parts, validating genetic circuits, and biosensor outputs. Currently, only two luciferases (Firefly and Renilla) are commonly used without substrate cross-talk. Here we demonstrate the expansion of the cell-free Luciferase reporter system, with two orthogonal Luciferase reporters: N. nambi Luciferase (Luz) and LuxAB. These luciferases do not have cross-reactivity with the Firefly and Renilla substrates. We also demonstrate a substrate regeneration pathway for one of the new luciferases, enabling long-term time courses of protein expression monitoring in the cell-free system. Furthermore, we reduced the number of genes required in TXTL expression, by engineering a cell extract containing part of the Luciferase enzymes. Our findings lead to an expanded platform with multiple orthogonal luminescence translation readouts for in vitro protein expression.
Split-Luciferase Complementation for Analysis of Virus-Host Protein Interactions
Methods Mol Biol 2022;2400:55-62.PMID:34905190DOI:10.1007/978-1-0716-1835-6_6.
Productive viral infection entails highly regulated and sequential protein-protein interactions between viral factors and between virus and host factors. Deciphering such interactions is of paramount importance for a better understanding of virus infection cycles and the development of new strategies for virus prevention and control. In this protocol, we describe a split-luciferase complementation (SLC ) assay for the detection of protein-protein interaction in Nicotiana benthamiana leaves following agroinfiltration-mediated transient protein expression. In this assay, the firefly Luciferase protein is divided into two halves, each expressed as a fusion to a prey or bait protein, respectively. Interaction of the two candidate proteins brings the two otherwise nonfunctional halves into close proximity to restore the Luciferase activity, which catalyzes the substrate D-luciferin to emit luminescence. The SLC assay allows for noninvasive, quantitative measurement of dynamic protein interactions in living cells within their native cellular compartments.