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Brilliant blue G

Brilliant blue G is a blue dye commonly used in biological and medical research.
It is a synthetic, water-soluble dye that has been employed for various applications, including staining proteins, visualizing nucleic acids, and labeling cellular structures.
Brilliant blue G's high binding affinity and low toxicity make it a valuable tool for researchers studying cellular processes, protein interactions, and molecular pathways.
This dye has proved useful in a wide range of experimental techniques, from electrophoresis to microscopy.
Researchers can leverage PubCompare.ai's AI-powered platform to optimize thier [sic] experiments with Brilliant blue G, accessing a comprehensive database of protocols and identifying the most effective methods for their studies.

Most cited protocols related to «Brilliant blue G»

Single-Cell mRNA Sequencing of Lung and Blood Cells

Lysis plates for single cell mRNA sequencing were prepared as previous described^{2 (link)}. 96-well lysis plates were used for cells from the blood and mouse samples and contained 4 μL of lysis buffer instead of 0.4 μL.
Following negative selection against immune and endothelial cells by MACS, the remaining human lung cells were incubated with FcR Block (Becton Dickinson (BD) 564219) for 5 minutes and stained with directly conjugated anti-human CD45 (Biolegend 304006) and EPCAM (eBioscience 25–9326-42) antibodies on a Nutator for 30 minutes at the manufacturer’s recommended concentration. Cells were then pelleted (300 x g, 5 minutes, 4°C), washed with FACS buffer three times, then incubated with cell viability marker Sytox blue (1:3000, ThermoFisher S34857) and loaded onto a Sony SH800S cell sorter. Living single cells (Sytox blue-negative) were sorted into lysis plates based on three gates: EPCAM⁺CD45⁻ (designated “epithelial”), EPCAM⁻CD45⁺ (designated “immune”), and EPCAM⁻CD45⁻ (designated “endothelial or stromal”).
Immune cells from subject matched blood were incubated with FcR Block and Brilliant Violet buffer (BD 563794) for 20 minutes and then stained with directly conjugated anti-human CD3 (BD 563548), CD4 (BD 340443), CD8 (BD 340692), CD14 (BD 557831), CD19 (Biolegend 302234), CD47 (BD 563761), CD56 (BD 555516), and CD235a (BD 559944) antibodies for 30 minutes at the manufacturer’s recommended concentration. Cells were pelleted (300 x g, 5 minutes, 4°C), washed with FACS buffer twice, and then incubated with the viability marker propidium iodide and loaded onto a BD FACSAria II cell sorter. Living (propidium iodide-negative) single, non-red blood (CD235a⁻) cells were sorted into lysis plates along with specific immune populations: B cells (CD19⁺CD3⁻), CD8+ T cells (CD8⁺), CD4⁺ T cells (CD4⁺), NK cells (CD19⁻CD3⁻CD56⁺CD14⁻), classical monocytes (CD19⁻ CD3⁻CD56⁻CD14⁺). After sorting, plates were quickly sealed, vortexed, spun down for 1 minute at 1000 x g, snap frozen on dry ice, and stored at −80 until cDNA synthesis.
Mouse cells were incubated with the viability marker DAPI and loaded onto a BD Influx cell sorter. Living (DAPI-negative) single cells were sorted into lysis plates based on presence or absence of the fluorescent lineage label (mEGFP for Axin2-Cre-ERT2, ZsGreen1 for Tbx4-LME-Cre).
Immune cells for bulk mRNA sequencing were incubated with FcR Block for 20 minutes and then stained with one of six panels of directly conjugated antibodies for 30 minutes at the manufacturers recommended concentration: anti-human CD16 (BD 558122), CD123 (BD 560826), CCR3 (R&D FAB155F), ITGB7 (BD 551082), CD3 (BD 555341), CD14 (Invitrogen MHCD1406), CD19 (BD 555414), and CD56 (BD 555517) (“basophils, neutrophils and eosinophils”); anti-human CD16 (BD 558122), CD14 (BD 347497), CD4 (BD 340443), CD3 (BD 555341), CD8 (BD 555368), CD19 (BD 555414), and CD56 (BD 555517) (“classical and nonclassical monocytes”); anti-human CD16 (BD 558122), CD1c (Miltenyi Biotec 130–098-007), CD11c (BD 340544), CCR3 (R&D FAB155F), CD123 (BD 560826), HLA-DR (BD 335796), CD3 (BD 555341), CD4 (BD 555348), CD8 (BD 555368), CD14 (Invitrogen MHCD1406), CD19 (BD 555414), and CD56 (BD 555517) (“pDCs, mDCs, CD16⁺ DCs”); anti-human IgM/IgD (BD 555778), CD19 (BD 557835), CD27 (BD 558664), CD20 (BD 335794), CD3 (BD 555341), CD4 (BD 555348), CD14 (Invitrogen MHCD1406), and CD56 (BD 555517) (“B cells”); anti-human CD16 (BD 558122), CD57 (BD 347393), CD56 (BD 557747), CD3 (BD 555341), CD4 (BD 555348), CD14 (Invitrogen MHCD1406), and CD19 (BD 555414) (“NK cells”); and anti-human CD45RA (Biolegend 304118), CCR7 (R&D FAB197F), CD62L (BD 555544), CD45RO (BD Pharmingen 560608), CD4 (BD 340443), CD8 (BD 340584), CD11b (BD 555389), CD14 (Invitrogen MHCD1406), CD19 (BD 555414), CD56 (BD 555517) (“T cells”). Cells were washed with FACS buffer twice, incubated with the viability marker propidium iodide and loaded onto a BD FACSAria II cell sorter. 40,000 cells from 21 canonical immune populations (Supplementary Table 3) were sorted in duplicate into Trizol LS (Invitrogen 10296010).
After sorting, all plates and samples were quickly sealed, vortexed, spun down for 1 minute at 1000 x g and then snap frozen on dry ice and stored at −80 until cDNA synthesis.

Travaglini K.J., Nabhan A.N., Penland L., Sinha R., Gillich A., Sit R.V., Chang S., Conley S.D., Mori Y., Seita J., Berry G.J., Shrager J.B., Metzger R.J., Kuo C.S., Neff N., Weissman I.L., Quake S.R, & Krasnow M.A. (2020). A molecular cell atlas of the human lung from single cell RNA sequencing. Nature, 587(7835), 619-625.

Publication 2020

Quantitative Proteomics of Trypanosoma Brucei

Two technical replicates were done each using 5 × 10⁶ procyclic cells that were mixed with 5 × 10⁶ LS or SS cells in Laemmli buffer, boiled at 95°C for 5 min and resolved on a 10% acryl amide gel (1,0 mm). Gels were stained with standard Coomassie Brilliant Blue G-250 solution (2.5 g Coomassie Brilliant Blue G-250 from Applichem in 450 ml methanol, 100 ml acetic acid and 400 ml water) and destained in the same solution without Coomassie. Subsequently gels were stored in 20% (v/v) ethanol at 4°C until MS analysis that was done in duplicate on two SDSPAGE lanes (within 2 days). For this, each gel lane was cut into ten bands. Each band was cut into several little cubes that were transferred to a low-binding reagent tube (Sarstedt, Nümbrecht, Germany). Gel slices were washed with 50 mM Tris/HCl pH 8 (Tris buffer) and Tris buffer/acetonitrile (LC-MS grade, Fluka, Buchs, Switzerland) 50/50 before protein reduction with 50 mM DTT (Fluka, Buchs, Switzerland) in Tris buffer for 30 min at 37°C, and alkylation with 50 mM iodoacetamide (Fluka, Buchs, Switzerland) in Tris buffer for 30 min at 37°C in the dark. After washing with Tris buffer and dehydration with acetonitrile the gel cubes were soaked with trypsin solution composed of 10 ng/ml trypsin (Promega) in 20 mM Tris/HCl pH 8, 0.01% ProteaseMax (Promega) for 30 min on ice. Gel cubes were covered by addition of 5–10 ml 20 mM Tris/HCl before digestion for 60 min at 50°C. The supernatant liquid was combined with a single gel extract performed with 20 ml 20% (v/v) formic acid (Merck) in polypropylene HPLC vials. An aliquot of 10 ml from each digest was loaded onto a self-made pre-column (Magic C18, 5 mm, 300 Å, 0.15 mm i.d. x 30 mm length) at a flow rate of ~5 ml/min with solvent A (0.1% formic acid in water/acetonitrile 98:2). After loading, peptides were eluted in back flush mode onto the analytical nano-column (Magic C18, 5 mm, 100 Å, 0.075 mm i.d. × 75 mm length) using an acetonitrile gradient of 5% to 40% solvent B (0.1% formic acid in water/acetonitrile 4.9:95) in 60 min at a flow rate of ~400 nl/min. The column effluent was directly coupled to an LTQ-orbitrap XL mass spectrometer (ThermoFisher, Bremen, Germany) via a nanospray ESI source operated at 1700 V. Data acquisition was made in data dependent mode with precursor ion scans recorded in the Fourier transform detector (FT) with resolution of 60’000 (@ m/z =400) parallel to five fragment spectra of the most intense precursor ions in the linear iontrap. CID mode settings were: Wideband activation on; precursor ion selection between m/z range 360–1400; intensity threshold at 500; precursors excluded for 15 sec. Further tune parameter settings were: Max. injection time LTQ MS2 = 200 ms, orbitrap MS 500 ms; automatic gain control orbitrap = 5 × 10⁵, LTQ MS = 3 × 10⁴, MS2 = 1 × 10⁴.
Mass Spectrometry data and SILAC ratio interpretation was made with MaxQuant version 1.1.1.36 run under Windows7 against a T. brucei sequence database (version available in May 2011) from the Wellcome Trust Sanger Institute Pathogen Sequencing Unit. The default contamination database in Andromeda (MaxQuant) was searched together with the target database. We applied the following MaxQuant default settings: for precursor masses in the first search (+/− 20ppm), in the second search (re-calibrated mass values; +/− 6ppm). For fragment spectra default was set to +/− 0.5 Da and only the top 6 peaks per mass interval of 100 were kept (peak filtering;
[45 (link)]). Other Maxquant parameters were: Peptide and protein FDR set at 1%; carbamidomethyl-cystein set as fixed modification; allowed dynamic modifications were Met oxidation, protein N-terminal acetylation, Phosphorylation on Ser/Thr/Tyr. For SILAC ratio at least two unique or razor peptides without modification were required. A strict trypsin cleavage rule was applied i.e. cleavage c-terminal after K or R, no cleavage if a P follows R or K!. The normalisation was done using the default settings in MaxQuant
[46 (link)].

Gunasekera K., Wüthrich D., Braga-Lagache S., Heller M, & Ochsenreiter T. (2012). Proteome remodelling during development from blood to insect-form Trypanosoma brucei quantified by SILAC and mass spectrometry. BMC Genomics, 13, 556.

Publication 2012

Affinity-Based Protein Purification Across Cell Types

All cell lines/strains utilized in this study are listed in Supplementary Table 5.
Yeast, E. coli and Human cell lines were cultured using
standard procedures and cryomilled and affinity captured essentially as
previously described^{29 (link),30 (link)}, except adapted for 96-well
plates as described in text and elaborated step-wise in the Supplementary Protocol 1. Human
cell lines have not been subjected to mycoplasma testing during the course of
the study. Rabbit IgG used for purifying TAP and SpA tagged proteins was
purchased from Innovative Research. Anti-GFP polyclonal antibodies were prepared
and conjugated as previously described^{30 (link)}, except the concentration of ammonium sulfate used
during the conjugation was 1.5 M. In all cases, proteins were eluted from the
affinity medium by the addition of 1x NuPAGE LDS sample loading solution (Life
Technologies); elution of GFP-tagged proteins included incubation at
70°C for 10 min. Extraction solvent working solutions were mixed from
concentrated stock solutions in 2.5 ml deep-well plates (VWR) manually, using a
Formulator (Formulatrix), or using a Hamilton STAR liquid handling workstation
(program files provided in Supplementary Protocol 2). Supplementary Figure 12 contains
detailed engineering diagram of the powder dispensing manifold. Resuspension of
powders in extraction solvents included sonication with an ice water chilled
microplate horn (yeast) or 8-tip micro-probe (bacteria & human) (Qsonica).
Yeast lysates were also vortexed with steel beads to aid rapid homogenization.
Supplementary Figure
13 displays the bead dispensing manifold utilized in yeast affinity
capture experiments. Custom manufactured filters (Fig. 2, Orochem Technologies) were used to clarify yeast cell
extracts for screens, otherwise extracts were clarified by centrifugation at 14k
RPM and 4°C, for 10 min in a bench top microfuge. To ensure
reproducibility all purifications presented (and processed for MS) were repeated
individually in microfuge tubes using an otherwise comparable procedure except
that extracts were clarified via centrifugation. Polyacrylamide gels were
stained with either a homemade colloidal Coomassie brilliant blue G-250
solution^{79 (link)} or with
Imperial Protein Stain (Thermo Fisher Scientific). Gel images were recorded in
TIFF using a Fujifilm LAS-3000 or an Epson Photo v700. In addition to the cited
publications, detailed protocols for many preparatory procedures utilized in
this study can be obtained at http://www.ncdir.org/public-resources/protocols/.

Hakhverdyan Z., Domanski M., Hough L., Oroskar A.A., Oroskar A.R., Keegan S., Dilworth D.J., Molloy K.R., Sherman V., Aitchison J.D., Fenyö D., Chait B.T., Jensen T.H., Rout M.P, & LaCava J. (2015). Rapid, Optimized Interactomic Screening. Nature methods, 12(6), 553-560.

Publication 2015

Anti-Antibodies Bacteria brilliant blue G Cell Lines Centrifugation Escherichia coli Homo sapiens Horns Ice Mycoplasma polyacrylamide gels Powder Proteins Rabbits Solvents Stains Steel Strains Sulfate, Ammonium Yeast, Dried

Shoot Apex Protein Profiling Analysis

The protein profile quality of shoot apexes was evaluated using 20 μg of protein submitted to SDS-PAGE gels (8 × 10 cm, acrylamide 12,5%) in vertical electrophoresis system (Omniphor).
To the 2D analyses, 500 μg of proteins were applied in immobilized pH gradient (IPG) gel strips of 13 cm with pH range of 3–10 NL (Amersham Biosciences, Immobiline™ Dry-Strip). The isoelectric focusing was carried out in the Ettan IPGphor 3 (GE Healthcare) system, controlled by Ettan IPGphor 3 software. Electrofocusing conditions: rehydration time – 12 h at 20 °C; Running - 500Vh for 1 h, 1000Vh for 1:04 h, 8000Vh for 2:30 h and 8000Vh for 40 min. The strips were reduced using equilibrium buffer (urea 6 mol L^− 1, Tris-HCl pH 8.8 75 mmol L^− 1, glycerol 30%, SDS 2%, bromophenol blue 0.002%) with DTT 10 mg mL^− 1 for 15 min, and alkylated using equilibrium buffer with iodoacetamide 25 mg mL^− 1 for 15 min. Finally, strips were equilibrated with running buffer (Tris 0.25 mol L^− 1, glycine 1.92 mol L^− 1, SDS 1%, pH 8.5) for 15 min. The second dimension was carried out in polyacrylamide gels 12.5% (triplicates) and the electrophoresis running were performed in the HOEFER SE 600 Ruby (GE Healthcare) vertical electrophoresis system under the following parameters: 15cmA/gel for 15 min, 40 mA/gel for 30 min and 50 mA/gel for 3 h, or until complete migration of sample trough the gel. After fixation and coloration with colloidal Comassie Brilliant Blue (CBB) G-250, gels were decolorized with distillated water. The digitalization process was made using ImageScanner III (GE Healthcare), the images were analyzed, and the spot detection was made by matching the gels triplicates in silico using Image Master 2D Platinum software (GE Healthcare).

dos Santos E.C., Pirovani C.P., Correa S.C., Micheli F, & Gramacho K.P. (2020). The pathogen Moniliophthora perniciosa promotes differential proteomic modulation of cacao genotypes with contrasting resistance to witches´ broom disease. BMC Plant Biology, 20, 1.

Publication 2020

Acrylamide brilliant blue G Bromphenol Blue Buffers Electrophoresis Gels Glycerin Glycine Immobiline Iodoacetamide Platinum polyacrylamide gels Proteins Rehydration SDS-PAGE Tromethamine Urea

Extraction and Identification of Cell Wall Proteins

Typically, 0.65 g of lyophilized cell walls was used for one experiment. Proteins were extracted by successive salt solutions in this order: two extractions each time with 6 mL CaCl₂solution (5 mM acetate buffer, pH 4.6, 0.2 M CaCl₂and 10 μL protease inhibitor cocktail), followed by two extractions with 6 mL LiCl solution (5 mM acetate buffer, pH 4.6, 2 M LiCl and 10 μL protease inhibitor cocktail). Cell walls were resuspended by vortexing for 5–10 min at room temperature, and then centrifuged for 15 min at 4000 × g and 4°C. Supernatants were desalted using Econo-Pac^®10 DG columns (Bio-Rad) equilibrated with 0.2 formic acid ammonium salt. The extract were lyophilized and resuspended in sample buffer for separation of proteins by 1D-GE, as previously described [12 (link)].
The next extraction was carried out by SDS and DTT. The cell wall preparation was treated with 12 mL solution containing 62.5 mM Tris, 4% SDS, 50 mM DTT, pH 6.8 (HCl). The mixture was boiled for 5 min and centrifuged for 15 min at 40000 × g and 4°C. The supernatant was dialyzed against 1 L H₂O in Spectra/Por^®membrane 10 kDa MWCO bags (Spectrum Medical Industries) at room temperature, then concentrated by successive centrifugation using the Centriprep^®centrifugal filter devices (YM-10 kDa membrane) (Millipore) at 4000 × g followed by speed vacuum centrifugation.
The protein content of each extract was measured using the Bradford method [27 (link)] with the Coomassie™ protein assay reagent kit (Pierce) using bovine serum albumin (BSA) as standard.
Gels were stained with Coomassie™ Brilliant Blue-based method [28 (link)]. Colored bands were digested with trypsin and MALDI-TOF MS or LC-MS/MS analyses were performed as previously reported [12 (link),13 (link)].
The sequences of the identified proteins were subsequently analyzed with several bioinformatic programs to predict their sub-cellular localization [29 -31 ]. In some cases, predictions were not the same with the three programs. Results are then indicated as "not clear". Data are described in Tables 1–5 (additional data).

Feiz L., Irshad M., Pont-Lezica R.F., Canut H, & Jamet E. (2006). Evaluation of cell wall preparations for proteomics: a new procedure for purifying cell walls from Arabidopsis hypocotyls. Plant Methods, 2, 10.

Publication 2006

Acetate Amino Acid Sequence Biological Assay brilliant blue G Buffers Cells Cell Wall Centrifugation formic acid, ammonium salt Gastrin-Secreting Cells Gels Medical Devices Protease Inhibitors Proteins Serum Albumin, Bovine Sodium Chloride Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Staining Tandem Mass Spectrometry Tissue, Membrane Tromethamine Trypsin Vacuum

Most recents protocols related to «Brilliant blue G»

Coomassie Blue Staining of Sperm Acrosome

The functional integrity of the sperm acrosome was assessed using Coomassie brilliant blue staining as described by Wang [30 (link)]. A Coomassie brilliant blue solution was prepared by first dissolving 0.1 g G-250 in 50 mL of 95% absolute ethanol. Secondly, 100 mL of 85% phosphoric acid was added. Finally, distilled water was added to make the total volume up to 1000 mL. After staining with Coomassie brilliant blue for 30 min at room temperature, each sample was examined under a phase-contrast microscope (OLYMPUS CX31, Tokyo, Japan) at a magnification of 1000× and at least 200 sperm were counted. The head of the intact acrosome sperm was stained blue.

Zhang L., Wang X., Sohail T., Jiang C., Sun Y., Wang J., Sun X, & Li Y. (2024). Punicalagin Protects Ram Sperm from Oxidative Stress by Enhancing Antioxidant Capacity and Mitochondrial Potential during Liquid Storage at 4 °C. Animals : an Open Access Journal from MDPI, 14(2), 318.

Publication 2024

Coomassie Blue Staining for Sperm Acrosome Integrity

Coomassie brilliant blue G-250 staining was used to evaluate the acrosome integrity of sperms. Coomassie brilliant blue G-250 staining solution was prepared by dissolving (0.10 g) of G-250 dye in 50 mL of 95% ethanol. Then, (100 mL) of 85% phosphoric acid was added and the final volume of staining solution was fixed to 1 L. Briefly, a 50 µL semen sample was placed in a test tube. After 1 mL of 4% paraformaldehyde was added to the fixed semen sample for 10 min, the resulting solution was centrifuged at (2000× g) for 5 min to obtain the precipitate of sperm cells. Next, 10 µL of semen sample was spread evenly on a slide with the help of a coverslip to obtain a smear. Finally, coomassie brilliant blue dye (G-250) was used to stain the smear for minimum 30 min. At least 200 sperm heads were evaluated using a 1000× oil immersion lens to determine the percentage of spermatozoa with acrosome integrity and non-integrity.

Sohail T., Zhang L., Wang X., Jiang C., Wang J., Sun X, & Li Y. (2024). Astaxanthin Improved the Quality of Hu Ram Semen by Increasing the Antioxidant Capacity and Mitochondrial Potential and Mitigating Free Radicals-Induced Oxidative Damage. Animals : an Open Access Journal from MDPI, 14(2), 319.

Publication 2024

Soluble Protein Determination in Alfalfa

Not available on PMC !

Soluble protein content was determined using Coomassie brilliant blue G-250 reagent [27] (link). We weighed 1.0 g of alfalfa sprouts, ground them and added 10 mL of distilled water for extraction, and centrifuged it at 4000 r/min for 20 min at 4 • C. We filtered it with a 0.22 µm filter head, aspirated 1 mL of supernatant, added 5 mL of Coomassie Brilliant Blue G-250, and mixed it and let it stand for 2 min, and absorbance values were measured at 595 nm (0-100 mg•L -1 BSA as a standard solution for soluble proteins).

Sun K., Peng Y., Wang M., Li W.H., Li Y., & Chen J. (2024). Effect of Red and Blue Light on the Growth and Antioxidant Activity of Alfalfa Sprouts. Horticulturae, 10(1), 76-76.

Publication 2024

Determining Soluble Protein Content

Not available on PMC !

The soluble protein content was determined using the Coomassie brilliant blue method [24] (link). A 1 g amount of sample was mixed with 5 mL of distilled water, centrifuged at 12,000 rpm at 4 • C for 20 min, and the supernatant was collected. Then, 1 mL of the supernatant was mixed with 5 mL of Coomassie brilliant blue G-250 solution, and the absorbance was measured at 595 nm after 2 min of standing. The soluble protein content in the sample was calculated based on the standard curve of bovine serum albumin (y = 0.0031x + 0.2651) (100-400 µg/mL), and the result was expressed as mg/g of fresh weight.

Guan Y., Lu S., Sun Y., Zhang R., Lu X., Pang L, & Wang L. (2024). Effect of Tea Tree Essential Oil on the Quality, Antioxidant Activity, and Microbiological Safety of Lightly Processed Lily (Lilium brownii var. viridulum) during Storage. Foods (Basel, Switzerland), 13(13).

Publication 2024

Quantifying Protein via Coomassie Staining

Coomassie blue staining method (14 ) was used to determine the protein content in the ROL, RRL and RFL, respectively. The brief process is: take 1 mL of liquid, centrifuge (10,000 g, 10 min) and take the supernatant and dilute it with normal saline at a ratio of 1:3. Dilute the Coomassie Brilliant Blue storage solution with distilled water at a ratio of 1:4. Add 1.5 mL of diluted Coomassie Brilliant Blue working solution to 25 μL of sample supernatant., shake and mix. After standing at room temperature for 10 min, the OD595nm value was measured under a microplate reader.

Tan Z., Liu J, & Wang L. (2024). Factors affecting the rumen fluid foaming performance in goat fed high concentrate diet. Frontiers in Veterinary Science, 11, 1299404.

Publication 2024

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More about "Brilliant blue G"

Brilliant blue G, also known as Coomassie Brilliant Blue G-250, is a versatile synthetic dye commonly used in biological and medical reserach [sic].
This water-soluble dye has a high binding affinity and low toxicity, making it a valuable tool for researchers studying cellular processes, protein interactions, and molecular pathways.
Brilliant blue G has a wide range of applications, including staining proteins, visualizing nucleic acids, and labeling cellular structures.
It is often used in techniques such as electrophoresis, microscopy, and various imaging methods.
The dye's ability to bind to proteins, including bovine serum albumin (BSA), has made it a popular choice for protein quantification and detection.
In addition to its use in staining, Brilliant blue G has also been employed as a labeling agent, allowing researchers to track and visualize various biomolecules and cellular components.
This dye has proved useful in studying trypsin activity, as well as in gelatin and sodium dodecyl sulfate (SDS) gel electrophoresis applications.
Researchers can leverage the power of PubCompare.ai's AI-driven platform to optimize their experiments with Brilliant blue G.
The platform provides access to a comprehensive database of protocols, enabling researchers to identify the most effective methods for their studies and enhance the reproducibility and accuracy of their research.