Gross E, Bedlack RS, Loew LM. 1994. Dual-wavelength ratiometric fluorescence measurement of the membrane dipole potential. Biophys J 67:208–216.

Churchich JE. 1986. Fluorescence properties of free and bound pyri-doxal phosphate and derivatives. Pyridoxal Phosphate: Chem Biochem Med Asp A, 1A:545–567.

Eriksson S, Kim SK, Kubista M, Norden B. 1993. Binding of 4′,6-diamidino-2-phenylindole (DAPI) to AT regions of DNA: evidence for an allosteric conformational change. Biochemistry 32:2987–2998.

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Bowen CM, Katzenellenbogen JA. 1997. Synthesis and spectroscop-ic characterization of two aza-tetrahydrochrysenes as potential fluorescent ligands for the estrogen receptor. J Org Chem 62:7650–7657.

Oi VT, Glazer AN, Stryer L. 1982. Fluorescent phycobiliprotein conjugates for analyses of cells and molecules. J Cell Biol 93:981–986.

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Buschmann V, Weston KD, Sauer M. 2003. Spectroscopic study and evaluation of red-absorbing fluorescent dyes. Bioconjugate Chem 14:195–204.

Wang Q, Scheigetz J, Gilbert M, Snider J, Ramachandran C. 1999. Fluorescein monophosphates as fluorogenic substrates for protein tyrosine phosphatases. Biochim Biophys Acta 1431:14–23.

Douglass PM, Salins LLE, Dikici E, Daunert S. 2002. Class-selective drug detection: fluorescently labeled calmodulin as the biorecogni-tion element for phenothiazines and tricyclic antidepressants. Bioconjugate Chem 13:1186–1192.

How dofluorophoreswork

Adir N, Lerner N. 2003. The crystal structure of a novel unmethylat-ed form of C-phycocyanin, a possible connector between cores and rods in phycobilisomes. J Biol Chem 278(28):25926–25932.

Telford WG, Moss MW, Morseman JP, Allnutt FCT. 2001. Cyanobacterial stabilized phycobilisomes as fluorochromes for extracellular antigen detection by flow cytometry. J Immunol Methods 254:13–30.

Cacciatore TW, Brodfuehrer PD, Gonzalez JE, Jiang T, Adams SR, Tsien RY, Kristan Jr WB, Kleinfield D. 1999. Identification of neural circuits by imaging coherent electrical activity with FRET-based dyes. Neuron 23:449–459.

Poenie M, Chen C-S. 1993. New fluorescent probes for cell biology. In Optical microscopy, pp. 1–25. Ed B Herman, JJ Lemasters. Academic Press, New York.

Wagnieres GA, Star WM, Wilson BC. 1998. In vivo fluorescence spectroscopy and imaging for oncological applications. Photochem Photobiol 68(5):603–632.

Shapovalov VL, Kotova EA, Rokitskaya TI, Antonenko YN. 1999. Effect of Gramicidin A on the dipole potential of phospholipid membranes. Biophys J 77:299–305.

Prendergast FG, Haugland RP, Callahan PJ. 1981. 1-[4-(trimethy-lamino)phenyl]-6-phenylhexa-1,3,5 triene: synthesis, fluorescence properties, and use as a fluorescence probe of lipid bilayers. Biochemistry 20:7333–7338.

Lin Y, Weissleder R, Tung CH. 2003. Synthesis and properties of sulfhydryl-reactive near-infrared cyanine fluorochromes for fluorescence imaging. Mol Imaging 2(2):87–92.

Gonzalez JE, Tsien RY. 1995. Voltage sensing by fluorescence resonance energy transfer in single cells. Biophys J 69:1272–1280.

When an optical bandpass filter is used with non-collimated light such as convergent or divergent rays, the wavelength shift will appear somewhat less than that of collimated light at the same angle. In a cone of light only the central ray is normal to the surface and all others are increasingly off-angle. The resultant shift could be given by integrating the wavelength shift over the range of angles but this is a rather lengthy process. A good approximation of the shift can be made by using the previous formula and dividing the calculated shift by two. This will work in systems where the full cone angle is a maximum of 20°.

Huang S, Heikal AA, Webb WW. 2002. Two-photon fluorescence spectroscopy and microscopy of NAD(P)H and flavoprotein. Biophys J 82:2811–2825.

Haq I, Ladbury JE, Chowdhry BZ, Jenkins TC, Chaires JB. 1997. Specific binding of Hoechst 33258 to the d(CGCAAATTTGCG)2 duplex: calorimetric and spectroscopic studies. J Mol Biol 271:244–257.

Prendergast FG, Meyer M, Carlson GL, Iida S, Potter JD. 1983. Synthesis, spectral properties, and use of 6-acryloyl-2-dimethy-laminonaphthalene (Acrylodan). J Biol Chem 258(12):7541–7544.

Rettig W, Lapouyade R. 1994. Fluorescence probes based on twisted intramolecular charge transfer (TICT) states and other adiabatic pho-toreactions. In Topics in fluorescence spectroscopy, Vol. 4: Probe design and chemical sensing, pp. 109–149. Ed JR Lakowicz. Plenum Press, New York.

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Fluorophoresexamples

Czarnik AW. 1994. Fluorescent chemosensors for cations, anions, and neutral analytes. In Topics in fluorescence spectroscopy, Vol. 4: probe design and chemical sensing, pp. 49–70. Ed JR Lakowicz. Plenum Press, New York.

Lövgren T, Pettersson K. 1990. Time-resolved fluoroimmunoassay, advantages and limitations. In Luminescence immunoassay and molecular applications, pp. 233–253. Ed K Van Dyke, R Van Dyke. CRC Press, Boca Raton, FL.

Xiao G-S, Zhou J-M. 1996. Conformational changes at the active site of bovine pancreatic RNase A at low concentrations of guanidine hydrochloride probed by pyridoxal 5′-phosphate. Biochim Biophys Acta 1294:1–7.

Gershkovich AA, Kholodovych VV. 1996. Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IFETS). J Biochem Biophys Methods 33:135–162.

Bevis BJ, Glick BS. 2002. Rapidly maturing variants of the discosoma red fluorescent protein (DsRed). Nature Biol 20:83–87.

Campbell RE, Tour O, Palmer AE, Steinbach PA, Baird GS, Zacharias DA, Tsien RY. 2002. A monomeric red fluorescent protein. Proc Natl Acad Sci USA 99(12):7877–7882.

Heim R, Tsien RY. 1996. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr Biol 6:178–182.

Horrocks WDeW, Sudnick DR. 1981. Lanthanide ion luminescence probes of the structure of biological macromolecules. Acc Chem Res 14:384–392.

Gafni A, Brand L. 1976. Fluorescence decay studies of reduced nicotinamide adenine dinucleotide in solution and bound to liver alcohol dehydrogenase. Biochemistry 15(15):3165–3171.

Telford WG, Moss MW, Morseman JP, Allnutt FCT. 2001. Cryptomonad algal phycobiliproteins as fluorochromes for extracellular and intracellular antigen detection by flow cytometry. Cytometry 44:16–23.

Hull RV, Conger PS, Hoobler RJ. 2001. Conformation of NADH studied by fluorescence excitation transfer spectroscopy. Biophys Chem 90:9–16.

Mataga N, Chosrowjan H, Taniguchi S, Tanaka F, Kido N, Kitamura M. 2002. Femtosecond fluorescence dynamcis of flavoproteins: comparative studies on flavodoxin, its site-directed mutants, and riboflavin binding protein regarding ultrafast electron transfer in protein nanospaces. J Phys Chem B 106:8917–8920.

Nordlund TM, Wu P, Anderson S, Nilsson L, Rigler R, Graslund A, McLaughlin LW, Gildea B. 1990. Structural dynamics of DNA sensed by fluorescence from chemically modified bases. SPIE Proc 1204:344–353.

Cubitt AB, Heim R, Adams SR, Boyd AE, Gross LA, Tsien RY. 1995. Understanding, improving and using green fluorescent proteins. Trends Biochem Sci 20:448–455.

Biologicalfluorophores

Bruno J, Horrocks WDeW, Zauhar RJ. 1992. Europium(III) luminescence and tyrosine to terbium(III) energy transfer studies of invertebrate (octopus) calmodulin. Biochemistry 31:7016–7026.

Baird GS, Zacharias DA, Tsien RY. 2000. Biochemistry, mutagene-sis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc Natl Acad Sci USA 97(22):11984–11989.

Usually functions as a pair of plane mirrors that send the light through the objective to the eyepiece. May consist of a more complex optical system when the ...

Flanagan JH, Romero SE, Legendre BL, Hammer RP, Soper A. 1997. Heavy-atom modified near-IR fluorescent dyes for DNA sequencing applications: synthesis and photophysical characterization. SPIE Proc 2980:328–337.

Kao WY, Davis CE, Kim YI, Beach JM. 2001. Fluorescence emission spectral shift measurements of membrane potential in single cells. Biophys J 81:1163–1170.

Slavik J. 1982. Anilinonaphthalene sulfonate as a probe of membrane composition and function. Biochim Biophys Acta 694:1–25.

Nakanishi J, Nakajima T, Sato M, Ozawa T, Tohda K, Umezawa Y. 2001. Imaging of conformational changes of proteins with a new environment-sensitive fluorescent probe designed for site-specific labeling of recombinant proteins in live cells. Anal Chem 73:2920–2928.

Fluorophoreslist

Arden-Jacob J, Frantzeskos J, Kemnitzer NU, Zilles A, Drexhage KH. 2001. New fluorescent markers for the red region. Spectrochim Acta A 57:2271–2283.

Kung CE, Reed JK. 1986. Microviscosity measurements of phospho-lipid bilayers using fluorescent dyes that undergo torsional relaxation. Biochemistry 25:6114–6121. See also Biochemistry (1989) 28:6678–6686.

Walkup GK, Imperiali B. 1996. Design and evaluation of a peptidyl fluorescent chemosensor for divalent zinc. J Am Chem Soc 118:3053–3054.

Andresen M, Schmitz-Salue R, Jakobs S. 2004. Short tetracysteine tags to β-tubulin demonstrate the significance of small labels for live cell imaging. Mol Biol Cell 15:5616–5622.

Fluorescence probes represent the most important area of fluorescence spectroscopy. The wavelength and time resolution required of the instruments is determined by the spectral properties of the fluorophores. Furthermore, the information available from the experiments is determined by the properties of the probes. Only probes with non-zero anisotropies can be used to measure rotational diffusion, and the lifetime of the fluorophore must be comparable to the timescale of interest in the experiment. Only probes that are sensitive to pH can be used to measure pH. And only probes with reasonably long excitation and emission wavelengths can be used in tissues, which display autofluorescence at short excitation wavelengths.

Sabbatini N, Guardigli M. 1993. Luminescent lanthanide complexes as photochemical supramolecular devices. Coord Chem Rev 123:201–228.

Johnson ID, Kang HC, Haugland RP. 1991. Fluorescent membrane probes incorporating dipyrrometheneboron difluoride fluorophores. Anal Biochem 198:228–237.

Kwon O-S, Blazquez M, Churchich JE. 1994. Luminescence spec-troscopy of pyridoxic acid and pyridoxic acid bound to proteins. Eur J Biochem 219:807–812.

Klonis N, Wang H, Quazi NH, Casey JL, Neumann GM, Hewish DR, Hughes AB, Deady LW, Tilley L. 2001. Characterization of a series of far red absorbing perylene diones: a new class of fluorescent probes for biological applications. J Fluoresc 11(1):1–11.

Niwa H, Inouye S, Hirano T, Matsuno T, Kojima S, Kubota M, Ohashi M, Tsuji FI. 1996. Chemical nature of the light emitter of the Aequorea green fluorescent protein. Proc Natl Acad Sci USA 93:13617–13622.

Schroeder F, Barenholz Y, Gratton E, Thompson TE. 1987. A fluorescence study of dehydroergosterol in phosphatidylcholine bilayer vesicles. Biochemistry 26:2441–2448.

Kawai M, Lee MJ, Evans KO, Nordlund TM. 2001. Temperature and base sequence dependence of 2-aminopurine fluorescence bands in single- and double-stranded oligodeoxynucleotides. J Fluoresc 11(1):23–32.

Lumture JB, Wensel TG. 1993. A novel reagent for labelling macro-molecules with intensity luminescent lanthanide complexes. Tetrahedron Lett 34(26):4141–4144.

Loontiens FG, McLaughlin LW, Diekmann S, Clegg RM. 1991. Binding of Hoechst 33258 and 4′,6-diamidino-2-phenylindole to self-complementary decadeoxynucleotides with modified exocyclic base substitutents. Biochemistry 30:182–189.

Geoghegan KF. 1996. Improved method for converting an unmodified peptide to an energy-transfer substrate for a proteinase. Bioconjugate Chem 7(3):385–391.

Tjioe I, Legerton T, Wegstein J, Herzenberg LA, Roederer M. 2001. Phycoerythrin-allophycocyanin: a resonance energy transfer fluo-rochrome for immunofluorescence. Cytometry 44:24–29.

Smiley ST, Reers M, Mottola-Hartshorn C, Lin M, Chen A, Smith TW, Steele GD, Chen LB. 1991. Intracellular heterogeneity in mito-chondrial membrane potentials revealed by a J-aggregate-forming lipophilic cation JC-1. Proc Natl Acad Sci USA 88:3671–3675.

Daniel E, Weber G. 1966. Cooperative effects in binding by bovine serum albumin, I: the binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations. Coop Effects Binding Albumin 5:1893–1900.

Berlier JE, Rothe A, Buller G, Bradford J, Gray DR, Filanoski BJ, Telford WG, Yue S, Liu J, Cheung C-Y, Chang W, Hirsch JD, Beechem JM, Haugland RP, Haugland RP. 2003. Quantitative comparison of long-wavelength Alexa fluor dyes to Cy dyes: fluorescence of the dyes and their bioconjugates. J Histochem Cytochem 51(12):1699–1712.

Loura LMS, Prieto M. 1997. Aggregation state of dehydroergosterol in water and in a model system of membranes. J Fluoresc 7(1):173S–175S.

Valeur B. 1994. Principles of fluorescent probe design for ion recognition. In Topics in fluorescence spectroscopy, Vol. 4: Probe design and chemical sensing, pp. 21–48. Ed JR Lakowicz. Plenum Press, New York.

Weber G, Farris FJ. 1979. Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-propionyl-2-(dimethylamino)-naphthalene. Biochemistry 18:3075–3078.

Illsley NP, Verkman AS. 1987. Membrane chloride transport measured using a chloride-sensitive fluorescent probe. Biochemistry 26:1215–1219.

To reduce the chance of damage due to thermal shock, we recommend a maximum operating temperature of 70°C, and a maximum temperature change of 5°C per minute.

Davenport L, Targowski P. 1996. Submicrosecond phospholipid dynamics using a long lived fluorescence emission anisotropy probe. Biophys J 71:1837–1852.

Rye HS, Yue S, Wemmer DE, Quesada MA, Haugland RP, Mathies RA, Glazer AN. 1992. Stable fluorescent complexes of double-stranded DNA with bis-intercalating asymmetric cyanine dyes: properties and applications. Nucleic Acids Res 20(11):2803–2812.

Plásek J, Sigler K. 1996. Slow fluorescent indicators of membrane potential: a survey of different approaches to probe response analysis. J Photochem Photobiol B: Biol 33:101–124.

Holzwarth AR, Wendler J, Suter GW. 1987. Studies on chromophore coupling in isolated phycobiliproteins. Biophys J 51:1–12.

Use our free Gaussian elimination calculator to solve matrix equations, systems of linear equations, and perform Gauss-Jordan elimination.

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Jean JM, Hall KB. 2002. 2-aminopurine electronic structure and fluorescence properties in DNA. Biochemistry 41:13152–13161.

The metal-dielectric type is similar to the all-dielectric type except that it utilizes a metal spacer layer instead of a dielectric layer. Although this type of filter has excellent out-of-band blocking and high passband transmission, it lacks the sharp cut-on and cut-off slopes of the typical two and three cavity filters. The metal-dielectric type is mainly used for bandpass filters in the ultraviolet. However one version, the induced transmission type, is used as an additional blocking component when rejection is required to the far infrared.

Wolfbeis OS. 1985. The fluorescence of organic natural products. In Molecular luminescence spectroscopy, Part 1, pp. 167–370. Ed SG Schulman. John Wiley & Sons, New York.

Clarke RJ, Kane DJ. 1997. Optical detection of membrane dipole potential: avoidance of fluidity and dye-induced effects. Biochim Biophys Acta 1323:223–239.

Karasawa S, Araki T, Yamamoto-Hino M, Miyawaki A. 2003. A green-emitting fluorescent protein from Galaxeidae coral and its monomeric version for use in fluorescent labeling. J Biol Chem 278(36):34167–34171.

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Visser AJWG. 1984. Kinetics of stacking interactions in flavin adenine dinucleotide from time-resolved flavin fluorescence. Photochem Photobiol 40(6):703–706.

Demas JN, DeGraff BA. 1992. Applications of highly luminescent transition metal complexes in polymer systems. Macromol Chem Macromol Symp 59:35–51.

Diegelman S, Fiala A, Leibold C, Spall T, Buchner E. 2002. Transgenic flies expressing the fluorescence calcium sensor cameleon 2.1 under UAS control. Genesis 34:95–98.

All of our optical bandpass filters are stabilized to prevent drift of peak wavelength with age and are hermetically sealed for maximum humidity protection. Each filter is mounted in a black anodized aluminum ring which affords increased protection against damage resulting from rough handling and moisture penetration. However, even with this construction, it is advisable to avoid prolonged exposure to environments in which high humidity and large temperature variations are concurrent.

Kinnunen PKJ, Koiv A, Mustonen P. 1993. Pyrene-labeled lipids as fluorescent probes in studies on biomembranes and membrane models. In Fluorescence spectroscopy: new methods and applications, pp. 159–171. Ed OS Wolfbeis. Springer-Verlag, New York.

Palmer GM, Keely PJ, Breslin TM, Ramanujam N. 2003. Autfluorescence spectroscopy of normal and malignant human breast cell lines. Photochem Photobiol 78(5):462–469.

Madhuri S, Vengadesan N, Aruna P, Koteeswaran D, Venkatesan P, Ganesan S. 2003. Native fluorescence spectroscopy of blood plasma in the characterization of oral malignancy. Photochem Photobiol 78(2):197–204.

Balzani V, Ballardini R. 1990. New trends in the design of luminescent metal complexes. Photochem Photobiol 52(2):409–416.

Brochon J-C, Wahl P, Monneuse-Doublet M-O, Olomucki A. 1977. Pulse fluorimetry study of octopine dehydrogenase-reduced nicoti-namide adenine dinucleotide complexes. Biochemistry 16(21):4594–4599.

Wiedenmann J, Schenk A, Rocker C, Girod A, Spindler KD. 2002. A far-red fluorescent protein with fast maturation and reduced oligomerization tendency from Entacmaea quadricolor (anthozoa, actinaria). Proc Natl Acad Sci USA 99(18):11646–11651.

Lippincott-Schwartz J, Patterson GH. 2003. Development and use of fluorescent protein markers in living cells. Science 300:87–91.

Gambetta GA, Lagarias JC. 2001. Genetic engineering of phy-tochrome biosynthesis in bacteria. Proc Natl Acad Sci USA 98(19):10566–10571.

Zimmer M. 2002. Green fluorescent protein (GFP): applications, structure, and related photophysical behavior. Chem Rev 102:759–781.

Glazer AN, Peck K, Matheis RA. 1990. A stable double-stranded DNA ethidium homodimer complex: application to picogram fluorescence detection of DNA in agarose gels. Proc Natl Acad Sci USA 87:3851–3855.

Graefe KA, Tang Z, Karnes HT. 2000. High-performance liquid chromatography with on-line post-column immunoreaction detection of digoxin and its metabolites based on fluorescence energy transfer in the far-red spectral region. J Chromatogr B 745:305–314.

Li L, Murphy JT, Lagarias JC. 1995. Continuous fluorescence assay of phytochrome assembly in vitro. Biochemistry 34:7923–7930.

Hemmila I. 1993. Progress in delayed fluorescence immunoassay. In Fluorescence spectroscopy, new methods and applications, pp. 259–266. Ed OS Wolfbeis. Springer-Verlag, New York.

Steiner RF, Kubota Y. 1983. Fluorescent dye-nucleic acid complexes. In Excited states of biopolymers. Ed RF Steiner. Plenum Press, New York.

Southwick PL, Ernst LA, Tauriello EW, Parker SR, Mujumdar RB, Mujumdar SW, Clever HA, Waggoner AS. 1990. Cyanine dye labeling reagents-carboxymethylindocyanine succinimidyl esters. Cytometry 11:418–430.

Geddes CD, Lakowicz JR, eds. 2005. Advanced concepts in fluorescence sensing: small molecule sensing. Top Fluoresc Spectrosc 9, forthcoming.

Nakanishi J, Maeda M, Umezawa Y. 2004. A new protein conformation indicator based on biarsenical fluorescein with an extended ben-zoic acid moiety. Anal Sci 20:273–278.

DaCosta RS, Andersson H, Wilson BC. 2003. Molecular fluorescence excitation-emission matrices relevant to tissue spectroscopy. Photochem Photobiol 78(4):384–392.

Wu P, Li H, Nordlund TM, Rigler R. 1990. Multistate modeling of the time and temperature dependence of fluorescence from 2-aminopurine in a DNA decamer. SPIE Proc 204:262–269.

Another very important factor to note is that due to matching the different cavities within a filter construction, we cannot add an infinite amount of cavities. Please refer to the standard and custom interference filter section of this site for the appropriate information.

Albani JR, Sillen A, Engelborghs Y, Gervais M. 1999. Dynamics of flavin in flavocytochrome b2: a fluorescence study. Photochem Photobiol 69(1):22–26.

Due to the fact that the Fabry-Perot filter is essentially Lorentzian in shape, the cut-on and cut-off slopes are very shallow and the rate of attenuation in the out-of-band blocking range is very slow. To improve the slopes and increase the attenuation in the blocking band, we introduce more cavities into the construction. Please refer to the band shape charts for a comparison of one to four cavity filters. Please note that this data is only applicable to dielectric bandpass filters.

Churchich JE. 1976. Fluorescent probe studies of binding sites in proteins and enzymes. Mod Fluoresc Spectrosc 2:217–237.

Mizuno H, Sawano A, Eli P, Hama H, Miyawaki A. 2001. Red fluorescent protein from discosoma as a fusion tag and a partner for fluorescence resonance energy transfer. Biochemistry 40:2502–2510.

Fradkov AF, Chen Y, Ding L, Barsova EV, Matz MV, Lukyanov SA. 2000. Novel fluorescent protein from discosoma coral and its mutants possesses a unique far-red fluorescence. FEBS Lett 479:127–130.

Leenders R, Kooijman M, van Hoek A, Veeger C, Visser AJWG. 1993. Flavin dynamics in reduced flavodoxins. Eur J Biochem 211:37–45.

Chang PY, Jackson MB. 2003. Interpretation and optimization of absorbance and fluorescence signals from voltage-sensitive dyes. J Membr Biol 196:105–116.

Szmacinski H, Lakowicz JR. 1994. Lifetime-based sensing. In Topics in fluorescence spectroscopy, Vol. 4: Probe design and chemical sensing, pp. 295–334. Ed JR Lakowicz. Plenum Press, New York.

Davenport L, Shen B, Joseph TW, Straher MP. 2001. A novel fluorescent coronenyl-phospholipid analogue for investigations of sub-microsecond lipid fluctuations. Chem Phys Lipids 109:145–156.

Fluorophoresin fluorescence microscopy

Vaccari S, Benci S, Peracchi A, Mozzarelli A. 1996. Time-resolved fluorescence of tryptophan synthase. Biophys Chem 61:9–22.

Kwon MS, Koo BC, Choi BR, Lee HT, Kim YH, Ryu WS, Shim H, Kim JH, Kim NH, Kim T. 2004. Development of transgenic chickens expressing enhanced green fluorescent protein. Biochem Biophys Res Commun 320:442–448.

Lukyanov KA, Fradkov AF, Gurskaya NG, Matz MV, Labas YA, Savitsky AP, Markelov ML, Zaraisky AG, Zhao X, Fang Y, Tan W, Lukyanov SA. 2000. Natural animal coloration can be determined by a nonfluorescent green fluorescent protein homolog. J Biol Chem 275(34):25879–25882.

Rahavendran SV, Karnes HT. 1996. An oxazine reagent for derivati-zation of carboxylic acid analytes suitable for liquid chromatograph-ic detection using visible diode laser-induced fluorescence. J Pharmacol Biomed Anal 15:83–98.

Fluorophore structure

Terpetschnig E, Szmacinski H, Lakowicz JR. 1997. Long lifetime metal—ligand complexes as probes in biophysics and clinical chemistry. Methods Enzymol 278:295–321.

Jean JM, Hall KB. 2001. 2-aminopurine fluorescence quenching and lifetimes: role of base stacking. Proc Natl Acad Sci USA 98(1):37–41.

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Chalfie M, Tu Y, Euskirchen G, Ward WW, Prasher DC. 1994. Green fluorescent protein as a marker for gene expression. Science 263:802–805.

Adachi M, Nagao Y. 2001. Design of near-infrared dyes based on A-conjugation system extension, 2: theoretical elucidation of framework extended derivatives of perylene chromophore. Chem Mater 13:662–669.

Zhang J, Davidson RM, Wei M, Loew LM. 1998. Membrane electric properties by combined patch clamp and fluorescence ratio imaging in single neurons. Biophys J 74:48–53.

Martin RB, Richardson FS. 1979. Lanthanides as probes for calcium in biological systems. Quart Rev Biophys 12(2):181–209.

Thousands of fluorescent probes are known, and it is not practical to describe them all. This chapter contains an overview of the various types of fluorophores, their spectral properties, and applications. Fluorophores can be broadly divided into two main classes—intrinsic and extrinsic. Intrinsic fluorophores are those that occur naturally. These include the aromatic amino acids, NADH, flavins, derivatives of pyridoxyl, and chlorophyll. Extrinsic fluorophores are added to the sample to provide fluorescence when none exists, or to change the spectral properties of the sample. Extrinsic fluorophores include dansyl, fluorescein, rho-damine, and numerous other substances.

Richardson FS. 1982. Terbium(III) and europium(III) ions as luminescent probes and stains for biomolecular systems. Chem Rev 82:541–552.

Vaccari S, Benci S, Peracchi A, Mozzarelli A. 1997. Time-resolved fluorescence of pyridoxal 5′-phosphate-containing enzymes: trypto-phan synthetase and O-acetylserine sulfhydrylase. J Fluoresc 7(1):135S–137S.

Mizeret J. 1998. Cancer detection by endoscopic frequency-domain fluorescence lifetime imaging. Thesis presented at École Polytechnique Federale de Lausanne, 177 pp.

Griffin BA, Adams SR, Tsien RY. 1998. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281:269–272.

Hammer RP, Owens CV, Hwang SH, Sayes CM, Soper SA. 2002. Asymmetrical, water-soluble phthalocyanine dyes for covalent labeling of oligonucleotides. Bioconjugate Chem 13:1244–1252.

Li B, Lin S-X. 1996. Fluorescence-energy transfer in human estradi-ol 17β-dehydrogenase–NADH complex and studies on the coenzyme binding. Eur J Biochem 235:180–186.

Hawkins ME, Pfleiderer W, Mazumder A, Pommier YG, Balis FM. 1995. Incorporation of a fluorescent guanosine analog into oligonu-cleotides and its application to a real time assay for the HIV-1 integrase 3′-processing reaction. Nucleic Acids Res 23(15):2872–2880.

Trinquet E, Maurin F, Préaudat M, Mathis G. 2001. Allphycocyanin 1 as a near-infrared fluorescent tracer: isolation, characterization, chemical modification, and use in a homogeneous fluorescence resonance energy transfer system. Anal Biochem 296:232–244.

Matz MV, Fradkov AF, Labas YA, Savitsky AP, Zaraisky AG, Markelov ML, Lukyanov SA. 1999. Fluorescent proteins from non-bioluminescent Anthozoa species. Nature Biotechnol 17:969–973.

Klymchenko AS, Duportail G, Mély Y, Demchenko AP. 2003. Ultrasensitive two-color fluorescence probes for dipole potential in phospholipid membranes. Proc Natl Acad Sci USA 100(20):11219–11224.

The all-dielectric type consists of two highly reflecting mirrors separated by a dielectric spacer layer. These reflecting mirrors are constructed of alternating high and low refractive index materials and the reflectance of the stack is sometimes in excess of 99.99%. By varying the thickness of the spacer layer and or the number of reflecting layers, one can alter the central wavelength and bandwidth of the filter. This type of filter displays very high transmission in the passband, but, has a limited range of out-of-band blocking. To compensate for this deficiency, an additional blocking component is added, which is either all-dielectric or metal-dielectric depending upon the required blocking range. This additional blocking component will eliminate any unwanted out-of-band radiation but it will also reduce the overall throughput of the filter.

Bandpass filters are one of the simplest and most economical ways to transmit a well-defined band of light, and to reject all other unwanted radiation. Their design is essentially a thin film Fabry-Perot Interferometer formed by vacuum deposition techniques, and consists of two reflecting stacks, separated by an even-order spacer layer. Each one of these structures is referred to as a cavity, and some filters may contain as many as eight cavities. There are many different variations of the Fabry-Perot type bandpass filter, but for this discussion, we will only consider the all-dielectric and metal-dielectric type.

Matayoshi ED, Wang GT, Krafft GA, Erickson J. 1990. Novel fluo-rogenic substrates for assaying retroviral proteases by resonance energy transfer. Science 247:954–957.

Murphys JT, Lagarias JC. 1997. Purification and characterization of recombinant affinity peptide-tagged oat phytochrome A. Photochem Photobiol 65(4):750–758.

Thompson RB. 1994. Red and near-infrared fluorometry. In Topics in fluorescence spectroscopy, Vol 4: Probe design and chemical sensing, pp. 151–152. Ed JR Lakowicz. Plenum Press, New York.

Kao JPY. 1994. Practical aspects of measuring [Ca2+] with fluorescent indicators. In Methods in Cell Biology, Vol. 40, pp. 155–181. Ed R Nuccitelli. Academic Press, New York.

Fluorochrome vs fluorophore

By the original definition, a macro photograph is one in which the size of the subject on the negative or image sensor is life-size or greater. ... In some senses ...

Fischer AJ, Lagarias JC. 2004. Harnessing phytochrome’s glowing potential. Proc Natl Acad Sci USA (Early Ed.) 101:17334–17339.

Ignatova Z, Gierasch LM. 2004. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc Natl Acad Sci USA 101:523–528.

As a general rule, the highly reflective side of the filter should always face the source of radiation. This minimizes the thermal load on the absorbing glass blocking components and epoxies, thereby extending the lifetime of the filter. Apart from reduction of thermal effects, filter orientation is without influence on the spectral characteristics.

The effects of temperature, optical path geometry and environmental conditions must be considered when selecting or specifying optical bandpass filters. All of our filters are designed to operate at 23°C in normal incidence collimated beams. Please consult with one of our  before specifying any off-normal conditions so that a filter best suited for your application can be designed.

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Is GFP a fluorophore

Loos D, Cotlet M, De Schryver F, Habuchi S, Jofkens J. 2004. Single-molecule spectroscopy selectively probes donor and acceptor chromophore in the phycobiliprotein allophycocyanin. Biophys J 87:2598–2608.

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Sep 12, 2022 — Polarizing filters are composed of long molecules aligned in one direction. If we think of the molecules as many slits, analogous to those for ...

The central wavelength of the all-dielectric Fabry-Perot filter will shift lower in wavelength with an increase in the incident angle. The amount of wavelength shift is dependent upon the incident angle and the effective index (N*) of the filter. This feature can be very useful in tuning a narrowband filter to the desired central wavelength. The following formula may be used to determine the wavelength shift of a filter in collimated light with incident angles up to 15 degrees:

(2006). Fluorophores. In: Lakowicz, J.R. (eds) Principles of Fluorescence Spectroscopy. Springer, Boston, MA. https://doi.org/10.1007/978-0-387-46312-4_3

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The center wavelength of an interference filter will shift linearly with changes in ambient temperature, therefore it is very important to specify the operating temperature when ordering. The wavelength shifts in the direction of the temperature change, up with a positive change and down with a negative change. This shift factor will vary depending upon the filter's initial center wavelength. Please refer to the following chart for the proper temperature coefficient.

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Adams SR, Campbell RE, Gross LA, Martin BR, Walkup GK, Yao Y, Llopis J, Tsien RY. 2002. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J Am Chem Soc 124:6063–6076.