推荐产品
产品线
BioUltra
检测方案
≥98% (SDS-PAGE)
形式
lyophilized powder
比活
15-30×106 light units/mg protein
组成
Protein, 10-35% E1%/280
灵敏度测量范围
≤1 femtomole ATP (using 0.2 μg of luciferase and suitably sensitive liquid scintillation counters or luminometers)
应用
diagnostic assay manufacturing
异质活性
ATPase ≤5 nmol/min-mg protein
Nucleoside diphosphokinase ≤20 nmol/min-mg protein
运输
wet ice
储存温度
−20°C
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一般描述
Firefly luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light.
应用
This enzyme has wide range of applications in biotechnology and development of biosensors. Luciferase can be used to detect trace amounts of ATP and is one of the most commonly utilized reporter genes for the study of gene expression. The bioluminescent reaction catalyzed by luciferase is one of the most sensitive analytical tools for measuring gene expression. Less than or equal to one femtomole of ATP can be detected using 0.2 μg of luciferase. This enzyme has been used in a study to identify the different characteristics of reporter genes in whole-cell bacterial sensors. Luciferase from Photinus pyralis has also been used in a study to develop a novel bioluminogenic assay for α-chymotrypsin.
生化/生理作用
Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging.
包装
Sold on the basis of protein content
其他说明
Arsenate free.
Firefly luciferase is also available in economical recombinant forms (Product Numbers SRE0045 and L9420)
单位定义
One light unit produces a biometer peak height equivalent to 0.02 μCi of 14C in PPO/POPOP cocktail. Light units measured in 50 μl assay mixture containing 5 pmol ATP and 7.5 nmol luciferin in Tris-glycine buffer, pH 7.6, at 25 °C.
外形
Lyophilized powder approximately 20% protein; balance is primarily NaCl, HEPES buffer salts, and carbohydrate.
制备说明
Chromatographically prepared and crystallized.
分析说明
Note: Prior to 1991, a unit of firefly luciferase activity was defined as that amount which will produce 1.0 nanomole of pyrophosphate per minute at pH 7.7, 25 °C, using a system containing 0.6 mM ATP and 0.1 mM D-luciferin. The former nanomolar unit is equivalent to approximately 1.3 x 106 light units.
Two contaminant, ATP-consuming activities are assayed for in this product, ATPase and nucleoside diphosphokinase. These impurities are found to be less than 5 nanomolar units/mg protein and less than 20 nanomolar units/mg protein, respectively.
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
Applied biochemistry and biotechnology, 168(3), 604-615 (2012-07-20)
Firefly luciferase catalyzes production of light from luciferin in the presence of Mg(2+)-ATP and oxygen. This enzyme has wide range of applications in biotechnology and development of biosensors. The low thermal stability of wild-type firefly luciferase is a limiting factor
PloS one, 7(1), e30061-e30061 (2012-01-19)
Bioluminescence imaging is routinely performed in anesthetized mice. Often isoflurane anesthesia is used because of its ease of use and fast induction/recovery. However, general anesthetics have been described as important inhibitors of the luciferase enzyme reaction. To investigate frequently used
Methods in molecular biology (Clifton, N.J.), 289, 303-314 (2004-10-27)
Protocols to study the regulation of a conserved multigene family (SPRR genes) during calcium-induced differentiation of cultured normal human keratinocytes (NHKs) are provided. Transfection of promoter-reporter (CAT or luciferase) constructs, combined with promoter truncation, can be used to study the
eLife, 9 (2020-12-16)
The AAA+ protein disaggregase, Hsp104, increases fitness under stress by reversing stress-induced protein aggregation. Natural Hsp104 variants might exist with enhanced, selective activity against neurodegenerative disease substrates. However, natural Hsp104 variation remains largely unexplored. Here, we screened a cross-kingdom collection
The Journal of clinical investigation, 122(12), 4606-4620 (2012-11-13)
The induction of persistent intraepithelial CD8+ T cell responses may be key to the development of vaccines against mucosally transmitted pathogens, particularly for sexually transmitted diseases. Here we investigated CD8+ T cell responses in the female mouse cervicovaginal mucosa after
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