单比色皿样本室
Overview of ChronosDFD
ChronosDFD用于测量少于1秒的复衰减寿命,通过Vinci完成全自动化。Vinci是一个易于使用,基于Windows的软件包。
ChronosDFD的关键特征
频域测量
最大的灵敏度
全自动的
与外部设备集成
可升级的
- 拥有灵活的仪器构造和各种光源 (激光二极管、LED和钛-蓝宝石激光器)
- 占地面积紧凑,为了使光在样本内能够高效地耦合并且将灵敏度最大化而设计了较短的光学路径长度
- 下至皮秒上至秒的寿命测定性能
- 全自动化的仪器部件包括了:比色皿支架、偏振板、滤光轮、单色器和搅拌器
- 由PC操控将恒温浴、滴定仪、停流仪器和压力泵集成
- 可升级使其成为全稳态仪器
- 用于快速且精确偏振测定的T式样图形和平行光束光学设计
- 由Vinci多维荧光光谱仪供电
通过频域和ChronosDFD实现的数据采集的关键特征
- 荧光寿命时从两个可测量的参数计算的:相位角和调制
- 速度更快并且更不容易出现伪影
- 能够一步测量各向异性衰减 (旋转相关时)
- 可以更好地分辨短寿命部分
- 由于毫秒量级的高采样率,这是基于寿命传感和实时测量的首选方案
数据相当清晰!
丙二醇中的荧光素
在ChronosDFD上用470 nm激发波长 (氙弧灯) 测量的丙二醇内荧光素频域各向异性衰减 (微分极化相位角和振幅比)。发射通过530长通滤波器收集。θ = 5.3 ns、R0 = 0.40和τ = 4 ns, T = 27-28°C的计算数值。水中的BodipyFL
在ChronosDFD上用471 nm激光二极管测量水中BodipyFL频域各向异性衰减 (微分极化相位角和振幅比)。发射通过520长通滤波器收集。数据由衰减时5.87 ns的单指数衰减拟合 (χ2 = 0.97)。Product Specifications for ChronosDFD
光源
- 激光二极管 (nm): 370, 405, 436, 473, 635, 690, 780, 830
- LED (nm): 280, 300, 335, 345, 460, 500, 520
- 脉冲二极管:超连续谱、钛蓝宝石、脉冲激光二极管
聚焦和收集几何排列
- 平行光束设计,用于精准偏振测量
偏振器
- UV级别格兰-汤普逊偏振器,L/A=2.0
探测器
- 快速PMT
- 混合型PMT
- APD
探测器模块
- 光子计数电子元件
波长范围
- 200 nm至1700 nm (取决于探测器)
最大计数范围
- 上至8000万次/秒 (使用混合型探测器)
寿命测量范围
- 10-12 s至1 s
操作系统
- Windows 11
电源要求
- 通用电源输入:110 - 240 V, 50/60 Hz, 400 VAC
大小 (mm)
- 540 (长) x 425 (宽) x 235 (高)
重量 (kg)
- 25
ChronosDFD的配置示例
ChronosDFD的产品配件
产品资源
-
“Degradation Kinetics of Indocyanine Green in Aqueous Solution.” Saxena, V., Sadoqi, M. & Shao, J. Journal of Pharmaceutical Sciences, 92(10), pp. 2090–2097, 2003, Oct. doi: 10.1002/jps.10470.
-
“Characterization of Fluorinated Catansomes: A Promising Vector in Drug-Delivery.” Rosholm, K.R., Arouri, A., Hansen, P.L., González-Pérez, A. & Mouritsen, O.G. Langmuir, 28(5), pp. 2773–2781, 2012, Jan. doi: 10.1021/la2039834.
-
“Indocyanine green-loaded biodegradable nanoparticles: preparation, physicochemical characterization and in vitro release.” Saxena, V., Sadoqi, M. & Shao, J. International Journal of Pharmaceutics, 278(2), pp. 293–301, 2004, Jul. doi: 10.1016/j.ijpharm.2004.03.032.
-
“Enhanced photo-stability, thermal-stability and aqueous-stability of indocyanine green in polymeric nanoparticulate systems.” Saxena, V., Sadoqi, M. & Shao, J. Journal of Photochemistry and Photobiology B: Biology, 74(1), pp. 29–38, 2004, Mar. doi: 10.1016/j.jphotobiol.2004.01.002.
-
“Water-soluble norsquaraine dyes for protein labeling and pH-sensing applications.” Hovor, I.V., Kolosova, O.S., Sanin, E.V., Obukhova, O.M., Tatarets, A.L., Terpetschnig, E.A. & Patsenker, L.D. Dyes and Pigments, 170(10), p. 107567, 2019, Nov. doi: 10.1016/j.dyepig.2019.107567.
-
“Electronic absorption spectra and fluorescent properties of non-associated 16,17-bis(alkoxy)violanthrone dyes and their dependence on the nature of substituent and solvent's parameters.” Ponomarev, O., Sanin, E., Chepeleva, L. & Roshal, A. Dyes and Pigments, 156(10), pp. 45–52, 2018, Sep. doi: 10.1016/j.dyepig.2018.03.068.
-
“Development and Characterization of a Fluorescent Tracer for the Free Fatty Acid Receptor 2 (FFA2/GPR43).” Hansen, A.H., Sergeev, E., Pandey, S.K., Hudson, B.D., Christiansen, E., Milligan, G. & Ulven, T. Journal of Medicinal Chemistry, 60(13), pp. 5638–5645, 2017, Jun. doi: 10.1021/acs.jmedchem.7b00338.
-
“Development and Characterization of a Potent Free Fatty Acid Receptor 1 (FFA1) Fluorescent Tracer.” Christiansen, E., Hudson, B.D., Hansen, A.H., Milligan, G. & Ulven, T. Journal of Medicinal Chemistry, 59(10), pp. 4849–4858, 2016, May. doi: 10.1021/acs.jmedchem.6b00202.
-
“Characterization of the Photophysical, Thermodynamic, and Structural Properties of the Terbium(III)–DREAM Complex.” Gonzalez, W.G., Ramos, V., Diaz, M., Garabedian, A., Molano-Arevalo, J.C., Fernandez-Lima, F. & Miksovska, J. Biochemistry, 55(12), pp. 1873–1886, 2016, Mar. doi: 10.1021/acs.biochem.6b00067.
-
“Tetraaryl-, Pentaaryl-, and Hexaaryl-1,4-dihydropyrrolo[3,2-b]pyrroles: Synthesis and Optical Properties.” Krzeszewski, M., Thorsted, B., Brewer, J. & Gryko, D.T. The Journal of Organic Chemistry, 79(7), pp. 3119–3128, 2014, Mar. doi: 10.1021/jo5002643.
-
“Graphene Oxide as a Quencher for Fluorescent Assay of Amino Acids, Peptides, and Proteins.” Li, S., Aphale, A.N., Macwan, I.G., Patra, P.K., Gonzalez, W.G., Miksovska, J. & Leblanc, R.M. ACS Applied Materials & Interfaces, 4(12), pp. 7069–7075, 2012, Dec. doi: 10.1021/am302704a.
-
“Developing Red-Emissive Ruthenium(II) Complex-Based Luminescent Probes for Cellular Imaging.” Zhang, R., Ye, Z., Yin, Y., Wang, G., Jin, D., Yuan, J. & Piper, J.A. Bioconjugate Chemistry, 23(4), pp. 725–733, 2012, Mar. doi: 10.1021/bc200506w.
-
“Ground- and Excited-State Properties of Zn(II) Tetrakis(4-tetramethylpyridyl) Pophyrin Specifically Encapsulated within a Zn(II) HKUST Metal–Organic Framework.” Larsen, R.W., Miksovska, J., Musselman, R.L. & Wojtas, L. The Journal of Physical Chemistry A, 115(42), pp. 11519–11524, 2011, Sep. doi: 10.1021/jp2064408.
-
“Seta-633 - A NIR Fluorescence Lifetime Label for Low-Molecular-Weight Analytes.” Povrozin, Y.A., Kolosova, O.S., Obukhova, O.M., Tatarets, A.L., Sidorov, V.I., Terpetschnig, E.A. & Patsenker, L.D. Bioconjugate Chemistry, 20(9), pp. 1807–1812, 2009, Aug. doi: 10.1021/bc9002458.
-
“Noncovalent Assembly of a Metalloporphyrin and an Iron Hydrogenase Active-Site Model: Photo-Induced Electron Transfer and Hydrogen Generation.” Li, X., Wang, M., Zhang, S., Pan, J., Na, Y., Liu, J., {\Aa}Kermark, B. & Sun, L. The Journal of Physical Chemistry B, 112(27), pp. 8198–8202, 2008, Jun. doi: 10.1021/jp710498v.
-
“Flavin Adenine Dinucleotide Structural Motifs: From Solution to Gas Phase.” Molano-Arevalo, J.C., Hernandez, D.R., Gonzalez, W.G., Miksovska, J., Ridgeway, M.E., Park, M.A. & Fernandez-Lima, F. Analytical Chemistry, 86(20), pp. 10223–10230, 2014, Sep. doi: 10.1021/ac5023666.
-
“Water soluble indodicarbocyanine dyes based on 2,3-dimethyl-3-(4-sulfobutyl)-3H-indole-5-sulfonic acid.” Markova, L.I., Fedyunyayeva, I.A., Povrozin, Y.A., Semenova, O.M., Khabuseva, S.U., Terpetschnig, E.A. & Patsenker, L.D. Dyes and Pigments, 96(2), pp. 535–546, 2013, Feb. doi: 10.1016/j.dyepig.2012.09.007.
-
“Seta-633 - A NIR Fluorescence Lifetime Label for Low-Molecular-Weight Analytes.” Povrozin, Y.A., Kolosova, O.S., Obukhova, O.M., Tatarets, A.L., Sidorov, V.I., Terpetschnig, E.A. & Patsenker, L.D. Bioconjugate Chemistry, 20(9), pp. 1807–1812, 2009, Aug. doi: 10.1021/bc9002458.
-
“Near-infrared, dual-ratiometric fluorescent label for measurement of pH.” Povrozin, Y.A., Markova, L.I., Tatarets, A.L., Sidorov, V.I., Terpetschnig, E.A. & Patsenker, L.D. Analytical Biochemistry, 390(2), pp. 136–140, 2009, Jul. doi: 10.1016/j.ab.2009.03.047.
-
“Synthesis of water-soluble, ring-substituted squaraine dyes and their evaluation as fluorescent probes and labels.” Tatarets, A.L., Fedyunyayeva, I.A., Dyubko, T.S., Povrozin, Y.A., Doroshenko, A.O., Terpetschnig, E.A. & Patsenker, L.D. Analytica Chimica Acta, 570(2), pp. 214–223, 2006, Jun. doi: 10.1016/j.aca.2006.04.019.
-
“Fatty acid sensor for low-cost lifetime-assisted ratiometric sensing using a fluorescent fatty acid binding protein.” Bartolome, A., Bardliving, C., Rao, G. & Tolosa, L. Analytical Biochemistry, 345(1), pp. 133–139, 2005, Oct. doi: 10.1016/j.ab.2005.07.030.
-
“Dual-Labeled Glucose Binding Protein for Ratiometric Measurements of Glucose.” Ge, X., Tolosa, L. & Rao, G. Analytical Chemistry, 76(5), pp. 1403–1410, 2004, Jan. doi: 10.1021/ac035063p.
-
“Reagentless optical sensing of glutamine using a dual-emitting glutamine-binding protein.” Tolosa, L., Ge, X. & Rao, G. Analytical Biochemistry, 314(2), pp. 199–205, 2003, Mar. doi: 10.1016/s0003-2697(02)00586-9.
-
“Human cytochrome C natural variants: Studying the membrane binding properties of G41S and Y48H by fluorescence energy transfer and molecular dynamics.” Muroni, A., Minicozzi, V., Piro, M.C., Sinibaldi, F., Mei, G. & Di V.A. International Journal of Biological Macromolecules, 274, p. 133371, 2024, Aug. doi: 10.1016/j.ijbiomac.2024.133371.
-
“Molecular and cellular evidence of a direct interaction between the TRAF2 C-terminal domain and ganglioside GM1.” De L.A., Faienza, F., Fulci, C., Nicolai, E., Calligari, P., Palumbo, C. & Caccuri, A.M. The International Journal of Biochemistry & Cell Biology, 167, p. 106508, 2024, Feb. doi: 10.1016/j.biocel.2023.106508.
-
“One for All, All for One: The Peculiar Dynamics of TNF-Receptor-Associated Factor (TRAF2) Subunits.” Minicozzi, V., Di V.A., Caccuri, A.M., Mei, G. & Di P.L. Symmetry, 14(4), p. 720, 2022, Apr. doi: 10.3390/sym14040720.
-
“The Odd Faces of Oligomers: The Case of TRAF2-C, A Trimeric C-Terminal Domain of TNF Receptor-Associated Factor.” Di V.A., Nicolai, E., Minicozzi, V., Caccuri, A.M., Di P.L. & Mei, G. International Journal of Molecular Sciences, 22(11), p. 5871, 2021, May. doi: 10.3390/ijms22115871.
-
“Polymorphism on human aromatase affects protein dynamics and substrate binding: spectroscopic evidence.” Di N.G., Di V.A., Zhang, C., Nicolai, E., Castrignanò, S., Di P.L., Gilardi, G. & Mei, G. Biology Direct, 16(1), 2021, Apr. doi: 10.1186/s13062-021-00292-9.
-
“The Puzzling Problem of Cardiolipin Membrane-Cytochrome c Interactions: A Combined Infrared and Fluorescence Study.” Ripanti, F., Di V.A., Cestelli G.M., Romani, M., Filabozzi, A., Carbonaro, M., Piro, M.C., Sinibaldi, F., Nucara, A. & Mei, G. International Journal of Molecular Sciences, 22(3), p. 1334, 2021, Jan. doi: 10.3390/ijms22031334.
-
“Solution-Binding and Molecular Docking Approaches Combine to Provide an Expanded View of Multidrug Recognition in the MDR Gene Regulator BmrR.” Gunio, D., Froehlig, J., Pappas, K., Ferguson, U. & Wade, H. Journal of Chemical Information and Modeling, 56(2), pp. 377–389, 2016, Feb. doi: 10.1021/acs.jcim.5b00704.
-
“Strain Promoted Click Chemistry of 2- or 8-Azidopurine and 5-Azidopyrimidine Nucleosides and 8-Azidoadenosine Triphosphate with Cyclooctynes. Application to Living Cell Fluorescent Imaging.” Zayas, J., Annoual, M., Das, J.K., Felty, Q., Gonzalez, W.G., Miksovska, J., Sharifai, N., Chiba, A. & Wnuk, S.F. Bioconjugate Chemistry, 26(8), pp. 1519–1532, 2015, Jul. doi: 10.1021/acs.bioconjchem.5b00300.
-
“Amphiphilic Residues 29–44 of DREAM N-Termini Mediate Calmodulin:DREAM Complex Formation.” Gonzalez, W.G., Arango, A.S. & Miksovska, J. Biochemistry, 54(28), pp. 4391–4403, 2015, Jul. doi: 10.1021/acs.biochem.5b00251.
-
“The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity.” Chang, C.-k., Wu, T.-H., Wu, C.-Y., Chiang, M.-h., Toh, E.K.-W., Hsu, Y.-C., Lin, K.-F., Liao, Y.-h., Huang, T.-h. & Huang, J.J.-T. Biochemical and Biophysical Research Communications, 425(2), pp. 219–224, 2012, Aug. doi: 10.1016/j.bbrc.2012.07.071.
-
“Cotranslational Protein Folding within the Ribosome Tunnel Influences Trigger-Factor Recruitment.” Lin, K.-F., Sun, C.-S., Huang, Y.-C., Chan, S., Koubek, J., Wu, T.-H. & Huang, J.J.-T. Biophysical Journal, 102(12), pp. 2818–2827, 2012, Jun. doi: 10.1016/j.bpj.2012.04.048.
-
“Efficient Isolation of Pseudomonas aeruginosa Type III Secretion Translocators and Assembly of Heteromeric Transmembrane Pores in Model Membranes.” Romano, F.B., Rossi, K.C., Savva, C.G., Holzenburg, A., Clerico, E.M. & Heuck, A.P. Biochemistry, 50(33), pp. 7117–7131, 2011, Jul. doi: 10.1021/bi200905x.
-
“Production of Ribosome-Released Nascent Proteins with Optimal Physical Properties.” Ziehr, D.R., Ellis, J.P., Culviner, P.H. & Cavagnero, S. Analytical Chemistry, 82(11), pp. 4637–4643, 2010, Apr. doi: 10.1021/ac902952b.
-
“Excited-state lifetime studies of the three tryptophan residues in the N-lobe of human serum transferrin.” James, N.G., Ross, J.A., Mason, A.B. & Jameson, D.M. Protein Science, 19(1), pp. 99–110, 2009, Nov. doi: 10.1002/pro.287.
-
“Chain Dynamics of Nascent Polypeptides Emerging from the Ribosome.” Ellis, J.P., Bakke, C.K., Kirchdoerfer, R.N., Jungbauer, L.M. & Cavagnero, S. ACS Chemical Biology, 3(9), pp. 555–566, 2008, Aug. doi: 10.1021/cb800059u.
-
“Fructose-1,6-bisphosphate Acts Both as an Inducer and as a Structural Cofactor of the Central Glycolytic Genes Repressor (CggR).” Zorrilla, S., Chaix, D., Ortega, A., Alfonso, C., Doan, T., Margeat, E., Rivas, G., Aymerich, S., Declerck, N. & Royer, C.A. Biochemistry, 46(51), pp. 14996–15008, 2007, Dec. doi: 10.1021/bi701805e.
-
“Inducer-Modulated Cooperative Binding of the Tetrameric CggR Repressor to Operator DNA.” Zorrilla, S., Doan, T., Alfonso, C., Margeat, E., Ortega, A., Rivas, G., Aymerich, S., Royer, C.A. & Declerck, N. Biophysical Journal, 92(9), pp. 3215–3227, 2007, May. doi: 10.1529/biophysj.106.095109.
-
“Hydration of the Folding Transition State Ensemble of a Protein.” Brun, L., Isom, D.G., Velu, P., García-Moreno, B. & Royer, C.A. Biochemistry, 45(11), pp. 3473–3480, 2006, Feb. doi: 10.1021/bi052638z.
-
“Confined dynamics of a ribosome-bound nascent globin: Cone angle analysis of fluorescence depolarization decays in the presence of two local motions.” Ellis, J.P., Culviner, P.H. & Cavagnero, S. Protein Science, 18(10), pp. 2003–2015, 2009, Jun. doi: 10.1002/pro.196.
-
“Reorientational Dynamics of Enzymes Adsorbed on Quartz: A Temperature-Dependent Time-Resolved TIRF Anisotropy Study.” Czeslik, C., Royer, C., Hazlett, T. & Mantulin, W. Biophysical Journal, 84(4), pp. 2533–2541, 2003, Apr. doi: 10.1016/s0006-3495(03)75058-9.
-
“Time-resolved fluorescence anisotropy studies show domain-specific interactions of calmodulin with IQ target sequences of myosin V.” Bayley, P., Martin, S., Browne, P. & Royer, C. European Biophysics Journal, 32(2), pp. 122–127, 2003, Jan. doi: 10.1007/s00249-002-0274-7.
-
“Equilibrium Binding of Estrogen Receptor with DNA Using Fluorescence Anisotropy.” Ozers, M.S., Hill, J.J., Ervin, K., Wood, J.R., Nardulli, A.M., Royer, C.A. & Gorski, J. Journal of Biological Chemistry, 272(48), pp. 30405–30411, 1997, Nov. doi: 10.1074/jbc.272.48.30405.
-
“Structural and Thermodynamic Characterization of T4 Lysozyme Mutants and the Contribution of Internal Cavities to Pressure Denaturation.” Ando, N., Barstow, B., Baase, W.A., Fields, A., Matthews, B.W. & Gruner, S.M. Biochemistry, 47(42), pp. 11097–11109, 2008, Sep. doi: 10.1021/bi801287m.
-
“Glutathione-Activated Emission of Ultrasmall Gold Nanoparticles in the Second Near-Infrared Window for Imaging of Early Kidney Injury.” Zhao, Z., Chen, H., He, K., Lin, J., Cai, W., Sun, Y. & Liu, J. Analytical Chemistry, 95(11), pp. 5061–5068, 2023, Mar. doi: 10.1021/acs.analchem.2c05612.
-
“Amphiphilic Block Copolymer-Guided in Situ Fabrication of Stable and Highly Controlled Luminescent Copper Nanoassemblies.” Zhou, T., Zhu, J., Gong, L., Nong, L. & Liu, J. Journal of the American Chemical Society, 141(7), p. 2852–2856, 2019, Feb. doi: 10.1021/jacs.8b12026.
-
“Liberating Researchers from the Glovebox: A Universal Thermal Radiation Protocol Toward Efficient Fully Air-Processed Perovskite Solar Cells.” Wang, G., Liu, C., Kong, W., Chen, H., Li, D., Amini, A., Xu, B. & Cheng, C. Solar RRL, 3(5), p. 1800324, 2019, Jan. doi: 10.1002/solr.201800324.