基本信息
货号：12500 (1mg/1mL)
储存方式：保持在-20 oC。到期日为自收到之日起一年。
CAS号：61970-00-1
分子量：~60kDa
形式：液体（1mg / mL）
测量范围：≤1飞摩尔ATP敏感度（使用0.2μg荧光素酶和适当敏感的液体闪烁计数器或发光计）
生物应用
该重组萤火虫荧光素酶是从来自北美萤火虫（Photinus pyralis）的克隆基因表达的酶，其提供使用生物发光试剂检测ATP或荧光素底物进行研究或生产试剂盒所需的可靠性和可靠性。 该重组酶可以潜在地消除可能在从天然来源纯化的荧光素酶中发现的季节性和区域变异性的可能性。
该酶与荧光素，ATP和O2的反应导致光的发射。 荧光素酶可用于检测痕量的ATP。 萤火虫荧光素酶也是基因表达研究中最常用的报告基因之一。 荧光素酶催化的生物发光反应是测量基因表达的最灵敏的分析工具之一。 通过使用0.2μg荧光素酶可以检测小于或等于1飞摩尔的ATP。
参考文献
1. McElroy, W.D. (1947) The Energy Source for Bioluminescence in an isolated System. Proc. Natl. Acad. Sci. USA 33,342.
2. de Wet JR, Wood KV, Helinski DR, DeLuca M, (1985) Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli, Proc. Natl. Acad. Sci USA 82,7870-7873.
3. Khan, H.A. (2003) Bioluminometric assay of ATP in mouse brain: Determinant factors for enhanced test sensitivity, J. Bioscience 28, 379-382.
4. Drew, B and C. Leeuwenburgh (2003) Method for measuring ATP production in isolated mitochondria: ATP production in brain and liver mitochondria fo Fischer-344 rats with age and caloric restriction, Am J. Physiol. Regul. Integr. Comp. Physiol., 285, R1260-R1268.
5. Hara, K. Y. and Mori, H. (2006) An efficient method for quantitative determination of cellular ATP synthetic activity, J Biomol Screen 11, 310-7.
6. Sun, Y. and Chai, T. C. (2006) Augmented extracellular ATP signaling in bladder urothelial cells from patients with interstitial cystitis Am J Physiol Cell Physiol 290, C27-34.
7. Stanley, P.E., A review of bioluminescent ATP techniques in rapid microbiology. J. Biolumin. Chemilumin. 4, 375, (1989)
8. Rajgopal, S., and Vijayalakshmi, M.A. Enzyme Microb. Technol. 6, 482-489, (1984)
9. Chappelle, E.W., et al., Determination of bacterial content in fluids,. Meth. Enzymol. 57, 65-72, (1978)
10. Kricka, L.J., Clinical and biochemical applications of luciferases and luciferins. Anal. Biochem. 175, 14-21, (1988)
11. Liu L, Hastings JW. (2006) Two different domains of the luciferase gene in theheterotrophic dinoflagellate Noctiluca scintillans occur as two separate genes in photosynthetic species. Proc Natl Acad Sci U S A. 12. Emamzadeh AR, Hosseinkhani S, Sadeghizadeh M, Nikkhah M, Chaichi MJ, Mortazavi M. (2006) cDNA cloning, expression and homology modeling of a luciferase from the firefly Lampyroidea maculata. J Biochem Mol Biol, 39, 578.
12. Viviani VR, Ohmiya Y. (2006) Bovine serum albumin displays luciferase-like activity in presence of luciferyl adenylate: insights on the origin of protoluciferase activity and bioluminescence colours. Luminescence, 21, 262.
13. Schipper ML, Patel MR, Gambhir SS. (2006) Evaluation of firefly luciferase bioluminescence mediated photodynamic toxicity in cancer cells. Mol Imaging Biol, 8, 218.
14. Oba Y, Sato M, Inouye S. (2006) Cloning and characterization of the homologous genes of firefly luciferase in the mealworm beetle, Tenebrio molitor. Insect Mol Biol, 15, 293.
15. Palomba S, Berovic N, Palmer RE. (2006) Bioluminescence of monolayers of firefly luciferase immobilized on graphite. Langmuir, 22, 5451.
16. Schipper ML, Patel MR, Gambhir SS. (2006) Evaluation of Firefly Luciferase Bioluminescence Mediated Photodynamic Toxicity in Cancer Cells. Mol Imaging Biol.
18. Fraga H, Fernandes D, Novotny J, Fontes R, Esteves da Silva JC. (2006) Firefly luciferase produces hydrogen peroxide as a coproduct in dehydroluciferyl adenylate formation. Chembiochem, 7, 929.