英文flag致电:029-68064558
搜索

trFluor Eu 驴抗大鼠IgG(H + L)*交叉吸附*

英文名称:trFluor™ Eu donkey anti-rat IgG (H+L) *Cross Adsorbed*
产品参数
Ex (nm)298Em (nm)617
分子量~150000溶剂Water
存储条件在零下15度以下保存, 避免光照
产品概述

产品基本信息

产品名称:trFluor Eu 驴抗大鼠IgG(H + L)

储存条件:-15℃避光防潮

保质期:24个月

 

产品物理化学光谱特性

分子量:~150000

溶剂:水

激发波长(nm):346

发射波长(nm):617

 

产品介绍

存在于细胞,血清或其他生物流体中的许多生物化合物都是天然荧光的,因此,由于要测定的生物分子的自发荧光引起的高背景,使用常规的快速荧光团会严重限制测定灵敏度。长寿命荧光团与时间分辨检测(激发和发射检测之间的延迟)结合使用,可大程度地减少即时荧光干扰。我们的trFluor Eu探针可用于需要高灵敏度的测定的时间分辨荧光(TRF)。与更传统的荧光团(例如Alexa Fluor或花青染料)相比,trFluor Eu探针具有较大的斯托克斯位移和极长的发射半衰期。与其他TRF化合物相比,我们的trFluor Eu探针具有相对较高的稳定性,高发射率和与生物分子连接的能力。当与一抗结合使用时,这种trFluor Eu驴抗大鼠IgG(H + L)缀合物通常用作间接免疫荧光染色的第二步试剂。百萤生物是AAT Bioquest的中国代理商,为您提供优质的trFluor Eu 驴抗大鼠IgG(H + L)。 

点击查看光谱

 

图示

图1.时间分辨荧光能量转移(TR-FRET)是时间分辨荧光法(TRF)与Förster共振能量转移(FRET)的实际结合,为药物发现研究人员提供了强大的工具。 TR-FRET将TRF的低背景方面与FRET的均相测定形式结合在一起。除更高的通量和更少的假阳性/假阴性结果外,所得测定法还提高了灵活性,可靠性和灵敏性。 FRET涉及两个荧光团,一个供体(例如trFluor Eu和trFluor Tb)和一个受体。如果能量源(例如闪光灯或激光器)对供体的激发,则如果两者在给定的彼此邻近范围内,则将能量转移至受体。受体继而以其特征波长发射光。该技术的FRET方面受多种因素驱动,包括光谱重叠和所涉及的荧光团的邻近性,其中仅当施主与受主之间的距离足够小时才发生能量转移。实际上,FRET系统的特征在于Förster半径(R0):FRET效率为50%时荧光团之间的距离。对于许多FRET配对,R0介于20至90Å之间,具体取决于所使用的受体和检测中荧光团的空间排列。通过测量这种能量转移,可以通过将每个配偶与荧光标记偶联并检测能量转移的水平来评估生物分子之间的相互作用。可以检测受体发射作为能量转移的量度,而无需将结合的与未结合的测定成分分开(例如过滤或洗涤步骤),从而减少了测定时间和成本。

 

 

参考文献

Development of a time-resolved fluorescence resonance energy transfer assay for cyclin-dependent kinase 4 and identification of its ATP-noncompetitive inhibitors
Authors: Lo MC, Ngo R, Dai K, Li C, Liang L, Lee J, Emkey R, Eksterowicz J, Ventura M, Young SW, Xiao SH.
Journal: Anal Biochem (2012): 368

Time-Resolved Fluorescence Resonance Energy Transfer as a Versatile Tool in the Development of Homogeneous Cellular Kinase Assays
Authors: Saville L, Spais C, Mason JL, Albom MS, Murthy S, Meyer SL, Ator MA, Angeles TS, Husten J.
Journal: Assay Drug Dev Technol. (2012)

A homogeneous single-label time-resolved fluorescence cAMP assay
Authors: Martikkala E, Rozw and owicz-Jansen A, Hanninen P, Petaja-Repo U, Harma H.
Journal: J Biomol Screen (2011): 356

Homogeneous time-resolved fluorescence-based assay to screen for ligands targeting the growth hormone secretagogue receptor type 1a
Authors: Leyris JP, Roux T, Trinquet E, Verdie P, Fehrentz JA, Oueslati N, Douzon S, Bourrier E, Lamarque L, Gagne D, Galleyr and JC, M'Kadmi C, Martinez J, Mary S, Baneres JL, Marie J.
Journal: Anal Biochem (2011): 253

Oligomerization of the serotonin(1A) receptor in live cells: a time-resolved fluorescence anisotropy approach
Authors: Paila YD, Kombrabail M, Krishnamoorthy G, Chattopadhyay A.
Journal: J Phys Chem B (2011): 11439

Time-resolved fluorescence resonance energy transfer (TR-FRET) to analyze the disruption of EGFR/HER2 dimers: a new method to evaluate the efficiency of targeted therapy using monoclonal antibodies
Authors: Gaborit N, Larbouret C, Vallaghe J, Peyrusson F, Bascoul-Mollevi C, Crapez E, Azria D, Chardes T, Poul MA, Mathis G, Bazin H, Pelegrin A.
Journal: J Biol Chem (2011): 11337

A time-resolved fluorescence-resonance energy transfer assay for identifying inhibitors of hepatitis C virus core dimerization
Authors: Kota S, Scampavia L, Spicer T, Beeler AB, Takahashi V, Snyder JK, Porco JA, Hodder P, Strosberg AD.
Journal: Assay Drug Dev Technol (2010): 96

Ligand regulation of the quaternary organization of cell surface M3 muscarinic acetylcholine receptors analyzed by fluorescence resonance energy transfer (FRET) imaging and homogeneous time-resolved FRET
Authors: Alvarez-Curto E, Ward RJ, Pediani JD, Milligan G.
Journal: J Biol Chem (2010): 23318

Steady-state and time-resolved fluorescence quenching with transition metal ions as short-distance probes for protein conformation
Authors: Posokhov YO, Kyrychenko A, Ladokhin AS.
Journal: Anal Biochem (2010): 284

Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs
Authors: Visser AJ, Laptenok SP, Visser NV, van Hoek A, Birch DJ, Brochon JC, Borst JW.
Journal: Eur Biophys J (2010): 241