Flamingo fluorescent gel stain

Manufactured by Bio-Rad

Sourced in United States

Flamingo fluorescent gel stain is a fluorescent dye used to visualize nucleic acids, such as DNA and RNA, in agarose or polyacrylamide gels. It binds to nucleic acids and emits a bright, pink fluorescent signal when exposed to ultraviolet (UV) light.

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Lab products found in correlation

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Close spelling variants of this product

Flamingo fluorescent stain (6 citations) Flamingo Fluorescent Protein Gel Stain (5 citations) Flamingo Stain (2 citations)

16 protocols using flamingo fluorescent gel stain

2D Gel Electrophoresis Protein Profiling

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Protein extracts were separated by two-dimensional gel electrophoresis as previously described [53 (link)]. Gels were then labeled with Flamingo Fluorescent Gel Stain (Bio-Rad, Hercules, CA, USA), scanned in a Typhoon 9400 (GE Healthcare, Chicago, IL, USA), and analyzed for spot variations using PD-Quest 8.0 (Bio-Rad, Hercules, CA, USA). Three animals from each group were analyzed. Spots of interest were then excised and identified by matrix-assisted laser desorption/ionization-time-of-flight using an AutoFlex III Smartbeam MALDI-ToF/ToF (Bruker Daltonics, Billerica, MA, USA).

Gallinat A., Vilahur G., Padró T, & Badimon L. (2022). Network-Assisted Systems Biology Analysis of the Mitochondrial Proteome in a Pre-Clinical Model of Ischemia, Revascularization and Post-Conditioning. International Journal of Molecular Sciences, 23(4), 2087.

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Mitochondrial Proteome Profiling by 2DE

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Each mitochondrial protein was loaded onto Immobiline^™ Drystrip immobilised pH gradient (IPG) strips (13 cm, pH 3–10 NL, GE healthcare^®) using the passive rehydration method for 12 h. Isoelectric focussing was performed using Ettan IPGphor (GE healthcare^®) at 20 °C, and the gel strips were equilibrated with the equilibration buffer twice for 15 min each, as described previously^{51 (link)}. The second dimension run was performed as follows. Each equilibrated gel strip was loaded onto a 12.5% sodium dodecyl sulphate polyacrylamide gel, sealed with the agarose sealing solution and supplied with current, using a vertical slab gel electrophoresis unit (SE 600 Chroma Hoefer^®), of 15 mA/gel for 30 min and then with a current of 30 mA/gel until the bromophenol blue reached the bottom of the gels. Gels were fixed with 10% acetic acid in 40% ethanol for 2 h, stained with the Flamingo^™ Fluorescent gel stain (Bio-Rad^®) for 18 h and washed with distilled water. 2DE was performed in triplicate.

Ampawong S., Isarangkul D., Reamtong O, & Aramwit P. (2018). Adaptive effect of sericin on hepatic mitochondrial conformation through its regulation of apoptosis, autophagy and energy maintenance: a proteomics approach. Scientific Reports, 8, 14943.

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2D Protein Separation and Visualization

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The 2D protein separation was carried out as described earlier30 (link). The 2-DE gels were stained with Flamingo fluorescent gel stain (Bio-Rad, Hercules, CA, USA) following the manufacturer instructions. After staining, gels were scanned at 50 μm resolution on a Fuji FLA-5100 scanner. The digitalized images were analyzed using Delta 2D 3.4 (Decodon, Brunswick, Germany). For protein visualization, the 2-DE gels were additionally stained overnight with colloidal Coomassie blue, Roti-Blue (Roth, Karlsruhe, Germany).

Dihazi G.H., Jahn O., Tampe B., Zeisberg M., Müller C., Müller G.A, & Dihazi H. (2015). Proteomic analysis of embryonic kidney development: Heterochromatin proteins as epigenetic regulators of nephrogenesis. Scientific Reports, 5, 13951.

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Two-Dimensional Gel Electrophoresis Workflow

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The dried culture supernatant was dissolved in sample buffer (8 M urea, 2%CHAPS, 50 mM dithiothreitol [DTT], 0.2% Bio‐Lyte 3/10 carrier ampholyte, 0.001%BPB, #1632108 Bio‐Rad Laboratories, Inc., Hercules, CA, USA) and adjusted to 0.4 mg/ml. A total of 125 μl (50 μg) of the prepared samples was applied to immobilized pH gradient (IPG) strips (ReadyStrip, pH 3‐10 non‐linear, # 1632002, Bio‐Rad Laboratories, Inc.), and isoelectric focusing (IEF) was performed using the PROTEAN® i12 IEF System (Bio‐Rad Laboratories, Inc.) according to the manufacturer's instructions. Later, the IPG strips were reduced with DTT, carbamidemethylated with iodoacetamide, applied to precast gels (Any kD Mini‐PROTEAN TGX Precast Gel # 4569031, Bio‐Rad Laboratories, Inc.), and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) was performed. The electrophoresed gels were stained with Flamingo Fluorescent Gel Stain (# 1610491, Bio‐Rad Laboratories, Inc.) or Coomassie Brilliant Blue (CBB) (Expedeon, Cambridge, UK). Image analyses of the stained gels were performed using a Gel Imaging system (Gel Doc EZ system, Bio‐Rad Laboratories, Inc.) and PDQuest 2‐D analysis software (Bio‐Rad Laboratories, Inc.).

Miyazaki Y., Goto T., Li X., Nakayama K., Okasho K., Takeda M., Mizuno K., Kimura H., Uegaki M., Sumiyoshi T., Teramoto Y., Akamatsu S., Kobayashi T., Ogawa O, & Inoue T. (2022). Up‐regulation of secretory leukocyte protease inhibitor in human samples might have a potential role of predicting prostate cancer recurrence and progression after surgery and hormonal therapy. Cancer Medicine, 12(3), 3328-3342.

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Proteomic Analysis of Cell Lysates

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Cell lysates were prepared with M-PER Mammalian Protein Extraction Reagent (Thermo Scientific) and centrifuged for 10 min at 10000 g. The cleared supernatant was then precipitated with DOC/TCA [21] (link). The resulting pellet was dissolved in rehydration buffer (8 M Urea, 2 M Thiourea, 2% w/v CHAPS, 0.002% w/v bromphenol blue, 1% Ampholytes, IPG buffer pH 3–11, 20 mM DTT) and 100 µg protein was applied to IPG strips (ReadyStrip 24 cm, 3–10 NL, BioRad). The IEF run was performed in a Protean IEF cell (BioRad) according to manufactures' instructions. The second dimension separation was carried out on a 12% SDS-PAGE gel according to Laemmli (Ettan Daltsix electrophoresis system). Proteins were visualized with Flamingo Fluorescent Gel Stain (BioRad) and visualized on a FLA-7000 Phosphoimager (Fujifilm). Gel overlays and subsequent analyses were performed with the Delta2D Software Package (Decodon).

Murmann T., Carrillo-García C., Veit N., Courts C., Glassmann A., Janzen V., Madea B., Reinartz M., Harzen A., Nowak M., Perner S., Winter J, & Probstmeier R. (2014). Staurosporine and Extracellular Matrix Proteins Mediate the Conversion of Small Cell Lung Carcinoma Cells into a Neuron-Like Phenotype. PLoS ONE, 9(2), e86910.

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Characterization of Released MUC4β Protein

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MUC4β protein released after 8 hr in PBS was analyzed using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in denaturing condition. Briefly, released MUC4β protein was dried by lyophilization and redissolved into 25 μl loading buffer. The solution was boiled for 10 min prior to SDS-PAGE analysis. Approximately 10 μg of released MUC4β was loaded into Mini-Protean TGX gels (Bio-Rad) and electrophoresed (150 V, 60 min, 4°C). Gels were then incubated in fixative (40% ethanol, 10% acetic acid, 3 hr) and stained overnight with Flamingo fluorescent gel stain (Bio-Rad). The resulting gels were imaged using a Typhoon 9400 flatbed scanner (GE Healthcare).
For protein tertiary structure, the fluorescence emission levels associated with the tyrosine and tryptophan residues of the protein were measured as an indicator for the folding state. The fluorescence of the released protein (40 μg/ml) at 280 nm wavelength excitation was analyzed over the range of 300–400 nm using a SpectraMax 190 plate reader (Molecular Devices, Sunnyvale, CA). The fluorescence of both released MUC4β and unencapsulated MUC4β protein were measured and the relative peak maxima and positions were compared to assess the tertiary structure.

Liu L., Kshirsagar P., Christiansen J., Gautam S.K., Aithal A., Gulati M., Kumar S., Solheim J.C., Batra S.K., Jain M., Wannemuehler M.J, & Narasimhan B. (2020). Polyanhydride nanoparticles stabilize pancreatic cancer antigen MUC4β. Journal of biomedical materials research. Part A, 109(6), 893-902.

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Fluorescent Protein Gel Analysis

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For image analysis, 2-DE gels were fixed in a solution containing 50% methanol and 12% acetic acid overnight and fluorescent stained with Flamingo fluorescent gel stain (Bio-Rad, Hercules, CA, USA) for minimum 5 h. Thereafter, gels were scanned at 50 μm resolution on a Fuji FLA-5100 scanner using the Image Reader Software (Fuji). The digitalized images were analyzed using Delta 2D 4.3 (Decodon, Braunschweig, Germany). For protein identification, 2-DE gels were additionally stained with colloidal Coomassie blue, Roti-Blue (Roth, Karlsruhe, Germany) overnight.

Dihazi G.H., Mueller G.A., Asif A.R., Eltoweissy M., Wessels J.T, & Dihazi H. (2015). Proteomic characterization of adrenal gland embryonic development reveals early initiation of steroid metabolism and reduction of the retinoic acid pathway. Proteome Science, 13, 6.

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Fluorescent Gel Staining for 2-DE Image Analysis

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For image analysis, 2-DE gels were fixed in a solution containing 50% methanol and 12% acetic acid overnight and stained with Flamingo® fluorescent gel stain (Bio-Rad) for 5 hours. Gels were then scanned at 50 μm resolution on a Fuji FLA-5100 scanner (Fuji Photo, Kanagawa, Japan). Digitalized images were analyzed using Delta 2D 3.4 (Decodon, Greifswald, Germany). 2-DE gels were post-stained with colloidal Coomassie® (Roti-Blue; Roth, Karlsruhe, Germany) overnight to enable manual spot picking for protein identification.

Blaschke S., Rinke K., Maring M., Flad T., Patschan S., Jahn O., Mueller C.A., Mueller G.A, & Dihazi H. (2015). Haptoglobin-α1, -α2, vitamin D-binding protein and apolipoprotein C-III as predictors of etanercept drug response in rheumatoid arthritis. Arthritis Research & Therapy, 17(1), 45.

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NF1 Protein Interactome Analysis

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NF1 full-length or truncated proteins pulled down by KIPA beads were loaded to SDS-PAGE gel and separated by electrophoresis. The gel was then strained by Flamingo Fluorescent Gel Stain (Bio-Rad). Cell/tumor lysates were prepared and analyzed by Western blots as described previously (9 (link)). The antibodies target NF1 and GAPDH were from MilliporeSigma (MABN2557, Clone NF1-A376G3) and Santa Cruz Biotechnology, respectively. The antibodies against ERα (D8H8), ERK1/2, Phospho-ERK1/2 (T202/Y204), and β-tubulin (9F3) were all from Cell Signaling Technology.

Kim B.J., Zheng Z.Y., Lei J.T., Holt M.V., Chen A., Peng J., Fandino D., Singh P., Kennedy H., Dou Y., Chica-Parrado M.D., Bikorimana E., Ye D., Wang Y., Hanker A.B., Mohamed N., Hilsenbeck S.G., Lim B., Asirvatham J.R., Sreekumar A., Zhang B., Miles G., Anurag M., Ellis M.J, & Chang E.C. (2023). Proteogenomic Approaches for the Identification of NF1/Neurofibromin-depleted Estrogen Receptor–positive Breast Cancers for Targeted Treatment. Cancer Research Communications, 3(7), 1366-1377.

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Characterization of Viral Protein Structures

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Post-fusion F protein and G protein encapsulated particles were left to release overnight (18 h) in 300 µL of PBS. Protein structure and stability was analyzed by SDS-PAGE. Each well of a Mini-Protean TGX gel was loaded with 1.5 µg of released proteins. The gel was electrophoresed at 100V for 10 min and then at 140V for 1 h. The gel was incubated in fixative (10% acetic acid and 40% ethanol) for two hours at 4°C then stained overnight with Flamingo fluorescent gel stain (BioRad). The gel was imaged with the use of an iBright™ CL1500 System Imager (ThermoFisher, Waltham, MA).

Maina T.W., Grego E.A., Broderick S., Sacco R.E., Narasimhan B, & McGill J.L. (2023). Immunization with a mucosal, post-fusion F/G protein-based polyanhydride nanovaccine protects neonatal calves against BRSV infection. Frontiers in Immunology, 14, 1186184.

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