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Cyan Fluorescent Protein

Cyan Fluorescent Protein (CFP) is a genetically engineered variant of the Green Fluorescent Protein (GFP) that emits light in the cyan region of the visible spectrum.
CFP is widely used as a fluorescent marker in cell biology and molecular biology studies, allowing researchers to visualize protein localization, interactions, and dynamics within living cells.
The blue-shifted emission spectrum of CFP, compared to GFP, makes it useful for multicolor fluorescence applications and FRET (Förster Resonance Energy Transfer) experiments.
Researchers can leverage the PubCompare.ai platform to effeciently discover the best protocols and optimize their Cyan Fluorescent Protein research, enhancing reproducibility and accuracy through the power of AI-driven analysis.

Most cited protocols related to «Cyan Fluorescent Protein»

Simulating Homo-FRET Fluorescence Decay Profiles

Polarisation resolved TCSPC data of fluorophores with a bi-exponential fluorescence decay profile undergoing homo-FRET leading to a bi-exponential anisotropy decay profile was simulated in MATLAB with a time window of 12.5 ns for a simulated pulse repetition rate of 80 MHz. The model, before accounting for incomplete decays and a simulated instrument response function takes the form where is the fractional contribution of the long component of the intensity decay and is the peak intensity. The data was simulated for two detectors polarised parallel and perpendicular to the excitation light, i.e. and . Using Equation 14, and . The model was convolved with a Gaussian IRF with a full width half maximum of 150 ps. The lifetimes of the fluorescence decay components were set to be and with a fractional contribution of the long component . The rotational correlation times were set to and , i.e. of the order expected for a fluorescent protein fusion construct undergoing homo-FRET. The pixel simulated image was split into three regions with initial anisotropy contribution of the short component set to 0.1, 0.2 and 0.3. In all three regions the total initial anisotropy . The initial intensity was set such that there were on average total integrated counts in each pixel and Poissonian noise was added to each decay using the MATLAB function poissrnd. These simulation parameters were chosen to approximate realistic values for cell imaging data, with the lifetimes selected to be similar to those of common cyan fluorescent protein variants such as ECFP and Cerulean [62] (link). In common with Experiment 5, a mean smoothing kernel was applied to each the image representing each time-bin of the data by convolution.

Warren S.C., Margineanu A., Alibhai D., Kelly D.J., Talbot C., Alexandrov Y., Munro I., Katan M., Dunsby C, & French P.M. (2013). Rapid Global Fitting of Large Fluorescence Lifetime Imaging Microscopy Datasets. PLoS ONE, 8(8), e70687.

Publication 2013

Anisotropy Cells Cyan Fluorescent Protein Fluorescence Fluorescence Resonance Energy Transfer Homo Light Pulse Rate Staphylococcal Protein A

Primary B Cell Isolation and Culture

Primary B cells were isolated from spleens of IgH^B1-8/B1-8 Igκ ^−/− transgenic mice (provided by M. Shlomchik, Yale University, New Haven, CT) by negative selection using MACS sorting as described previously (18 (link)). Isolated B cells were cultured overnight with CpG and LPS (Calbiochem, San Diego, CA) and experimented next day. The J558L B cells stably expressing B1-8-γ-cyan fluorescent protein (CFP) and Igα-yellow fluorescent protein (YFP) (γCαY) were established and characterized as previously described (21 (link)). Daudi B cell line stably expressing Lyn16-CFP-YFP fusion protein and CH27 B cell line stably expressing the lipid raft probe Lyn16-CFP, the nonlipid raft probe CFP-Ger, or the full length LynFL-CFP were established and characterized as previously reported (19 (link)). ST486, a human B cell line and A20II1.6, a mouse B cell line, both negative for endogenous FcγRIIB expression, were purchased from the American Type Culture Collection (Manassas, VA). PT67 cell line, a virus packaging cell line, was purchased from BD Clontech (Palo Alto, CA).
Cy3- and Cy5-conjugated Fab goat Abs specific for mouse IgM and IgG were purchased from Jackson ImmunoResearch Laboratories (West Grove, PA). Cy3-conjugated Fab rat mAb specific for mouse IgM (clone no. II/41) was purchased from Rockland (Gilbertsville, PA). Rabbit IgG Abs specific for BSA (rabbit anti-BSA) were purchased from Bethyl Laboratories (Montgomery, TX) and F(ab′)₂ rabbit anti-BSA were prepared as described (20 (link)). PE-conjugated and biotin-conjugated rat mAb specific for mouse FcγRIIB (clone no. 2.4G2) and APC-conjugated mouse mAb specific for human FcγRIIB (clone no. FLI8.26) were purchased from BD Pharmingen (San Diego, CA). Biotin-conjugated mouse mAb specific for human FcγRIIB (clone no. AT10) was purchased from AbD Serotec (Raleigh, NC). Biotin-conjugated F(ab′)₂ goat Abs specific for mouse IgG and IgM, biotin-conjugated F(ab′)₂ rabbit Abs specific for human IgM, and streptavidin were purchased from Jackson ImmunoResearch Laboratories. Rat mAb specific for mouse FcγRIIB (clone no. 190907) was purchased from R&D Systems (Minneapolis, MN) and Fabs mAb 190907 were prepared using an immobilized papain kit (Pierce, Rockford, IL) following the manufacturer’s protocol. Conjugations of Abs with Alexa514, 568, or 647 were performed using Alexa Fluor mAb labeling kits (Molecular Probes, Eugene, OR) following manufacturer’s protocols. BSA conjugated 1:14 with 4-hydroxy-5-iodo-3-nitrophenyl acetyl (NIP) (NIP₁₄-BSA) and BSA conjugated 1:16 with phosphorylcholine (PC₁₆-BSA) were purchased from Biosearch Technologies (Novato, CA). NIP₁₄-BSA and PC₁₆-BSA were conjugated to a Cys-containing peptide terminated with a His₁₂ tag (ASTGTASACTSGASSTGSH₁₂) using succinimidyl-4-(N-maleimidomethyl) cyclohexane-1-carboxylate (Pierce) following manufacturer’s protocols. ICs were formed by mixing 10 nM His₁₂ tagged NIP₁₄-BSA or PC₁₆-BSA with 20 nM rabbit anti-BSA (for IgG-IC) or F (ab′)₂ rabbit anti-BSA [for F(ab′)₂-IC]. Recombinant ICAM-1 with a His₁₂ tag was a gift of J. Huppa (Stanford University, Palo Alto, CA). The mouse ICAM-1/huFc chimera protein with a His₁₂ tag was purchased from R&D Systems. Conjugation of His₁₂-tagged NIP₁₄-BSA and PC₁₆-BSA to Cy5 and His₁₂-tagged ICAM-1 to AlexaFluor488 were performed following manufacturer’s protocols (19 (link)).

Liu W., Sohn H.W., Tolar P., Meckel T, & Pierce S.K. (2010). Antigen-Induced Oligomerization of the B Cell Receptor Is an Early Target of FcγRIIB Inhibition. Journal of immunology (Baltimore, Md. : 1950), 184(4), 1977-1989.

Publication 2010

B-Lymphocytes Biotin biotin 2 Cell Lines Cells Chimera Clone Cells Cyan Fluorescent Protein Cyclohexane Goat Homo sapiens Icam1 protein, mouse Intercellular Adhesion Molecule-1 Iodine Lipids Mice, Transgenic Molecular Probes Mus Papain PC 16 Peptides Phosphorylcholine Proteins Rabbits Streptavidin

Transient and Stable Cell Line Transfection

Transient transfections were carried out using FuGENE™ 6 (Roche). Stable cell lines were produced by selection for G418 resistance. The GPI-GFP construct was from S. Lacey (Southwestern University, TX), GPI-yellow fluorescent protein (YFP) was from M. Edidin (Johns Hopkins University, Baltimore, MD) Plasmids expressing VSV-Gts045-CFP and GalT-CFP were derived, by exchange of GFP for cyan fluorescent protein (CFP), from constructs described previously (Presley et al. 1997; Zaal et al. 1999). The CD59-GFP–expressing plasmid was produced by inserting CD59 cDNA between the EcoRI and BglII sites of plasmid ss-GFP (Nehls et al. 2000). Rab5S34N and Q79L were created by PCR site–directed mutagenesis and cloned KpnI/BamHI into pEGFPc1 and appropriate spectral variants (CLONTECH Laboratories, Inc.). The plasmid expressing dominant negative epsin mutant (just the DPW domain of epsin) was from P. DeCamilli (Yale University, New Haven, CT; Chen et al. 1998). Plasmid-expressing Eps15 mutant (D95/295) was from A. Benmerah (Institut Pasteur, Paris, France; Benmerah et al. 1999)

Nichols B.J., Kenworthy A.K., Polishchuk R.S., Lodge R., Roberts T.H., Hirschberg K., Phair R.D, & Lippincott-Schwartz J. (2001). Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex. The Journal of Cell Biology, 153(3), 529-542.

Publication 2001

antibiotic G 418 CD59 protein, human Cell Lines Cyan Fluorescent Protein Deoxyribonuclease EcoRI DNA, Complementary EPS15 protein, human epsin FuGene Mutagenesis, Site-Directed Plasmids Proteins Transfection Transients

Genetic Engineering of Transcription Factors

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Publication 2018

Cloning Vectors Cyan Fluorescent Protein DNA, Complementary Genes Homo sapiens Internal Ribosome Entry Sites Matrix Attachment Regions Plasmids Repression, Psychology Retroviridae RUNX1 protein, human Vertebral Column

Fluorescent Protein Constructs for Mitochondrial Dynamics

Bax linked to cyan fluorescent protein (CFP-Bax), and the marker of the OMM, 20 amino acids from the COOH terminus of Bax linked to yellow fluorescent protein (YFP-20) were described previously (Nechushtan et al., 1999 (link)). Mfn2-YFP was constructed from the GFP construct described previously (Santel and Fuller, 2001 (link)). Drp1 and Drp1^K38A expression vectors were described previously (Smirnova et al., 1998 (link); Frank et al., 2001 (link)). Drp1 was recloned into pEYFP-C1 to yield pEYFP-Drp1 (YFP-Drp1).
Human homologues of Fis1 (Mozdy et al., 2000 (link)), OMP 25, and synaptojanin 2A (Nemoto and De Camilli, 1999 (link)) were cloned from fetal human brain mRNA (Stratagene) using RT-PCR, and sub-cloned into pEYFP-C1 vectors (BD Biosciences). Mito-YFP (BD Biosciences) and mito-DsRed2 (BD Biosciences) revealed mitochondria.
Cells were transfected using the FuGENE 6 (Roche) and treated as indicated in individual experiments, 12–15 h later.

Karbowski M., Lee Y.J., Gaume B., Jeong S.Y., Frank S., Nechushtan A., Santel A., Fuller M., Smith C.L, & Youle R.J. (2002). Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis. The Journal of Cell Biology, 159(6), 931-938.

Publication 2002

Amino Acids Brain Cells Cloning Vectors Cyan Fluorescent Protein Fetus FuGene Homo sapiens link protein Mitochondria mitofusin 2 protein, human Mitomycin Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger synaptojanin

Most recents protocols related to «Cyan Fluorescent Protein»

Voltage-Sensitive Fluorescence Imaging

Slices were superfused with 95% O₂/5% CO₂-bubbled aCSF containing 4 μm dipicrylamine (DPA; City Chemical, LLC) and 1 μm strychnine for 30 min before experiments. DPA partitions into the cell membrane and its voltage-induced movement modulates a Förster resonance energy transfer interaction with the cerulean fluorescent protein (CeFP) of the hVOS probe to give a voltage-sensitive fluorescent signal (Chanda et al., 2005 (link); Wang et al., 2010 (link)). Bath temperature was measured between the inflow of the chamber and the tissue with a microprobe thermometer. An inline heater warmed the aCSF just before it reached the chamber to keep the temperature between 28°C and 31°C. hVOS imaging was conducted with an Olympus BX51 microscope equipped with a 29-W, 435 nm LED light source (Prizmatix), a standard cyan fluorescent protein filter set, and an Olympus XLUMPlanFl 20× objective (NA 1.0) or LUMPlanFl 60×objective (NA = 0.90). Images were acquired with a CCD-SMQ camera (Redshirt Imaging, now SciMeasure) at 2000 fps with 80 × 80 resolution. A computer program, either Neuroplex (SciMeasure) or an in-house program (Chang, 2006 ), controlled the timing of illumination, stimulation, and data acquisition. hVOS images were acquired as averages of 5–10 trials at 15-s intervals.

Ma Y., Shu W.C., Lin L., Cao X.J., Oertel D., Smith P.H, & Jackson M.B. (2023). Imaging Voltage Globally and in Isofrequency Lamina in Slices of Mouse Ventral Cochlear Nucleus. eNeuro, 10(3), ENEURO.0465-22.2023.

Publication 2023

Bath Cyan Fluorescent Protein dipicrylamine Fluorescence Resonance Energy Transfer Light Microscopy Movement Plasma Membrane Proteins Strychnine Thermometers Tissues

Two-Photon Imaging of Neuronal Areas

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Publication 2023

Alkalies Cyan Fluorescent Protein Fluorescence Hematoporphyrin Derivative Light Microscopy Neurons Proteins Radionuclide Imaging Sapphire Submersion

Genetic Models of Myeloid HDAC7 Regulation

Male and female C57BL/6J mice of 8 to 12 wk of age were obtained from an in-house breeding colony within the QBP animal house (The University of Queensland) or from the animal resources centre (Murdoch, WA). Mac-Hdac7 mice, which overexpress HDAC7 in myeloid cells, have previously been described (11 (link)). Littermate MacBlue mice expressing cyan fluorescent protein (CFP) in myeloid cells (79 (link)) were used as controls for studies using Mac-Hdac7 mice. Myeloid-deleted Hdac7 mice (Hdac7^−/−) (11 (link)) were obtained by crossing Hdac7^flox/flox/LysM^Cre mice with Hdac7^flox/flox mice, with littermate Hdac7^flox/flox (Hdac7^+/+) mice used as controls (80 (link)). As an additional control to ensure that the LysM^Cre allele did not confound data interpretation, functional assays (IL-1β release by ELISA, Escherichia coli-induced ROS production, and intracellular UPEC loads in macrophages) were performed to compare the phenotypes of BMM from LysM^Cre, Hdac7^+/+, and Hdac7^−/− mice (SI Appendix, Fig. S9 A–D). Tlr4^−/− mice (81 (link)) were maintained on a C57BL/6J background at the QBP animal house.

Das Gupta K., Ramnath D., von Pein J.B., Curson J.E., Wang Y., Abrol R., Kakkanat A., Moradi S.V., Gunther K.S., Murthy A.M., Stocks C.J., Kapetanovic R., Reid R.C., Iyer A., Ilka Z.C., Nauseef W.M., Plan M., Luo L., Stow J.L., Schroder K., Karunakaran D., Alexandrov K., Shakespear M.R., Schembri M.A., Fairlie D.P, & Sweet M.J. (2023). HDAC7 is an immunometabolic switch triaging danger signals for engagement of antimicrobial versus inflammatory responses in macrophages. Proceedings of the National Academy of Sciences of the United States of America, 120(4), e2212813120.

Publication 2023

Alleles Animals Biological Assay Cyan Fluorescent Protein Enzyme-Linked Immunosorbent Assay Escherichia coli Females HDAC7 protein, human Interleukin-1 beta Macrophage Males Mice, House Mice, Inbred C57BL Mus Myeloid Cells Phenotype Protoplasm

Chitin-induced FRET analysis of LysM receptors

Leaves of Nicotiana tabacum cv. Xanthi were transformed by agroinfiltration (Norkunas et al., 2018 (link)) with the Agrobacterium tumefaciens strain GV3101 containing an overexpression cassette for VvLYK1-1, VvLYK1-2, VvLYK5-1, or VvLYK5-2 fused with either a C-terminal Cyan Fluorescent Protein (C_ter-CFP in the pH7CWG2 plasmid, Karimi et al., 2005 (link)) or a C-terminal Yellow Fluorescent Protein (C_ter-YFP in the pH7YWG2 plasmid, Karimi et al., 2005 (link)). Five days after (co-)infiltration, the abaxial side of N. tabacum leaves transiently expressing the different constructs was infiltrated with chitin or water (mock treatment). Observations were performed 30 min post-treatments (according to Cheval et al., 2020 (link)) using a Nikon A1-MP multiphoton microscope with an Apo IR x60 objective (NA: 1.27, water immersion, Nikon). Fluorescence lifetime imaging (FLIM) images were collected using a time-correlated single-photon counting (TCSPC) module (Picoquant). CFP excitation (820 nm with two-photon excitation) was provided by an IR laser (Chameleon, Coherent) delivering femtosecond pulses at a repetition rate of 80 MHz. Its resulting fluorescence emission was collected with a single photon avalanche diode (SPAD), using a band-pass emission filter FF01-494/20 (Semrock). TCSPC lifetime recording was performed over 200 temporal channels (final resolution: 0.64 ps). The FLIM analysis was performed on regions of interest (ROIs) drawn on the plasma membrane using the SymPhoTime (PicoQuant) software. Fluorescence lifetime values were calculated by fitting the tail of the CFP fluorescence decay with a bi-exponential model. Among the two generated lifetime constants (τ₁ and τ₂), only τ₁ was reported, as it was the most sensitive to the Förster resonance energy transfer (FRET) (Bègue et al., 2019 (link); Rosnoblet et al., 2021 (link)). The efficiency of the energy transfer was given by the following equation:

E (%) = (1 - \frac{F_{D A}}{F_{D}}) \times 100

, with FDA and FD representing the relative fluorescence lifetime of the donor in the presence or the absence of the acceptor, respectively. Three independent experiments were conducted.

Roudaire T., Marzari T., Landry D., Löffelhardt B., Gust A.A., Jermakow A., Dry I., Winckler P., Héloir M.C, & Poinssot B. (2023). The grapevine LysM receptor-like kinase VvLYK5-1 recognizes chitin oligomers through its association with VvLYK1-1. Frontiers in Plant Science, 14, 1130782.

Publication 2023

Agrobacterium tumefaciens Apolipoprotein A-I Apolipoproteins A Avalanches Chameleons Chitin Cyan Fluorescent Protein Donors Energy Transfer Fluorescence Fluorescence Resonance Energy Transfer Microscopy Plasma Membrane Plasmids Pulse Rate Staphylococcal Protein A Strains Submersion Tail Tobacco Products

Bimolecular Fluorescence Complementation Assay

A bimolecular fluorescence complementation (BiFC) assay was performed by referring to the method described by Kang et al. (85 (link)). A. tumefaciens GV3101 cells containing different paired plasmids (different combinations of pSPYCE and pSPYNE-R or their derivatives) were cultured in Luria-Bertani (LB) liquid medium, collected by centrifugation, resuspended in infiltration buffer, and then mixed, followed by the adjustment to an optical density at 600 nm (OD₆₀₀) of 0.5; they were then used to transform the A. tumefaciens GV3101 (pMP90) strains, respectively. After incubation for 2 to 4 h at room temperature, the A. tumefaciens GV3101 mixture was injected into the leaves of 6-week-old Nicotiana benthamiana plants. Subsequently, the fluorescence was assayed at 3 to 5 days after infiltration using a laser-scanning microscope with cyan fluorescent protein (CFP; excitation wavelength, 405 nm; emission wavelength, 477 nm).

Zeng X., Li D., Lv Y., Lu Y., Mei L., Zhou D., Chen D., Xie F., Lin H, & Li Y. (2023). A Germin-Like Protein GLP1 of Legumes Mediates Symbiotic Nodulation by Interacting with an Outer Membrane Protein of Rhizobia. Microbiology Spectrum, 11(1), e03350-22.

Publication 2023

Buffers Cells Centrifugation Culture Media Cyan Fluorescent Protein derivatives Fluorescence Laser Scanning Microscopy Nicotiana Plants Plasmids Strains

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