Fluoro hance

Manufactured by Research Products International

Fluoro-Hance is a fluorescence enhancement reagent that increases the intensity of fluorescent signals in biological samples. Its core function is to amplify fluorescence signals, allowing for improved detection and visualization of labeled biomolecules.

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Lab products found in correlation

Bca protein assay, by Thermo Fisher Scientific (2 mentions) Easytag express 35s, by PerkinElmer (1 mentions) Dmem lacking methionine and cysteine, by Merck Group (1 mentions) Penicillin streptomycin, by Thermo Fisher Scientific (1 mentions) Anti ddk flag monoclonal antibody, by OriGene (1 mentions) L methyl 3h methionine, by PerkinElmer (1 mentions) Visionworks ls analysis software, by Analytik Jena (1 mentions)

3 protocols using fluoro hance

Pulse-Chase Analysis of ECM Proteins

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HEK293T cells were grown under the same conditions as above, in individual 35mm plates. Cells were incubated in DMEM lacking methionine and cysteine (Sigma) supplemented with 2 mM glutamine, 5% dialyzed fetal bovine serum (Gemini), and penicillin/streptomycin (Gibco) for 30 minutes (starvation media). Starvation media was removed, and cells were washed once in 37°C PBS containing calcium. Cells were then incubated in starvation media containing 0.1 mCi [³⁵S]-labeled methionine/cysteine (Easy Tag EXPRESS³⁵S, Perkin Elmer) for 20 minutes (pulse). The pulse period was stopped by removal of medium containing radioisotopes, washing, and incubation in DMEM supplemented with 2 mM methionine and cysteine for the indicated chase time. Cells were washed once in ice cold PBS. Cells were removed from the plate by washing 3x with PBS containing 0.1% Triton X-100 followed by 2x washes with PBS to separate cell debris from ECM. ECM proteins were extracted using 90 μl of 2% SDS in PBS, and analyzed by SDS-PAGE as above. No enrichment for CPA6 was performed and no protease inhibitors were used. Gels were fixed in 40% methanol/10% acetic acid/5% glycerol, incubated in Fluoro-Hance (Research Products International) with 5% glycerol, dried, and exposed to x-ray film at -80°C for 5–15 days.

Sapio M.R., Vessaz M., Thomas P., Genton P., Fricker L.D, & Salzmann A. (2015). Novel Carboxypeptidase A6 (CPA6) Mutations Identified in Patients with Juvenile Myoclonic and Generalized Epilepsy. PLoS ONE, 10(4), e0123180.

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Metabolic Labeling of NHE1 Protein

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PSN cells were metabolically labeled with [9,10-³H]palmitic acid (0.5 mCi/ml) for 1–6 h at 37 °C in N-MEM, containing 1 mM sodium pyruvate to inhibit palmitate metabolism through fatty acid -oxidation ^{28 ,29 (link)}. After labeling, cells were washed with SP buffer and lysed in radioimmunoprecipitation assay buffer (RIPA; 10 mM sodium phosphate, 150 mM NaCl, 2 mM EDTA, 50 mM sodium fluoride, 1% Triton X-100, 1% sodium deoxycholate, 0.1% SDS, pH 7.2). Lysates were then immunoblotted with anti-DDK (FLAG) monoclonal antibody (Clone OTI4C5, Origene) to determine NHE1 levels and volumes containing equal amounts of NHE1 (verified by a second immunoblot) were immunoprecipitated with anti-DDK (FLAG) monoclonal antibody (Clone OTI4C5, Origene) bound to protein A beads. Precipitated NHE1 was resolved on 4–20% SDS-polyacrylamide gels, treated with Fluoro-Hance (Research Products International) fluorographic reagent for 30 min, dried, and exposed to x-ray film for ~ 60 days at −80°C.

Hovde M.J., Bolland D.E., Armand A., Pitsch E., Bakker C., Kooiker A.J., Provost J.J., Vaughan R.A., Wallert M.A, & Foster J.D. (2021). Sodium hydrogen exchanger (NHE1) palmitoylation and potential functional regulation. Life sciences, 288, 120142.

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Methylation Assays of Bacterial Cultures

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Methylation assays were performed as previously described (Watts et al., 2011 (link)). Briefly, cultures were induced with 200 μM IPTG, centrifuged, washed and resuspended in chemotaxis buffer [0.1 mM K⁺EDTA, 10 mM KPO₄ pH 7.4, 10 mM Na-lactate, 1 mM MgSO₄, and 1 mM (NH₄)₂SO₄]. Then, 200 μg ml⁻¹ chloramphenicol was added to inhibit protein synthesis, and methylation was initiated by adding 9.7 μCi ml⁻¹ L-(methyl-³H) methionine (PerkinElmer, Waltham, MA). Reactions were stopped with 2 μl formaldehyde (per 1.02 ml reaction). After SDS-PAGE, gels were soaked for 30 min in Fluorohance™ (Research Products International, Mount Prospect, IL), then dried and exposed to autoradiography film at −80 °C for 2–4 days. Bands were quantified in the linear range using VisionWorks®LS Analysis Software (Analytik Jena, Upland, CA). Band densities were normalized by dividing by the concentration of protein in the formaldehyde-treated samples as determined in a BCA™ Protein Assay (Thermo Scientific). Statistical analyses were carried out using a two-tailed Student’s t-test. A value of P <0.05 was considered statistically significant.

Orillard E, & Watts K.J. (2020). DECIPHERING THE CHE2 CHEMOSENSORY PATHWAY AND THE ROLES OF INDIVIDUAL CHE2 PROTEINS FROM PSEUDOMONAS AERUGINOSA. Molecular microbiology, 115(2), 222-237.

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