Brilliant green is a synthetic dye used as a bacteriostatic agent and biological stain.
It is effective against gram-positive bacteria, and has applications in microbiology, histology, and topical antiseptic preparations.
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For each transcript a standard curve was constructed using the purified PCR product generated for each specific primer pair. Single reactions were prepared for each cDNA along with each serial of dilution using the Brilliant® SYBR® Green Master Mix (Stratagene). Each PCR reaction also included a reverse transcription negative control (without reverse transcriptase) to confirm the absence of genomic DNA, a non template negative control to check for primer-dimer and a porcine genomic DNA control to verify no specific amplification with the primers. Each reaction consisted of 20 μl containing 2 μl of cDNA and 5 pmol of each primer. The real time qPCR was run on MX3000p (Stratagene). The cycling conditions were 1 cycle of denaturation at 95°C/10 min, followed by 40 three-segment cycles of amplification (95°C/30 sec, 58°C–63°C (gene depending, see table 2)/1 min, 72°C/30 sec) where the fluorescence was automatically measured during PCR and one three-segment cycle of product melting (95°C/1 min, 55°C/30 sec, 95°C/30 sec). The baseline adjustment method of the Mx3000 (Stratagene) software was used to determine the Ct in each reaction. A melting curve was constructed for each primer pair to verify the presence of one gene-specific peak and the absence of primer dimmer. All samples were amplified in duplicates and the mean was used for further analysis.
Nygard A.B., Jørgensen C.B., Cirera S, & Fredholm M. (2007). Selection of reference genes for gene expression studies in pig tissues using SYBR green qPCR. BMC Molecular Biology, 8, 67.
For paired-end RNA-Seq experiments, 400 ng of total RNA was prepared after FACS purification of 500,000 GFP+ or GFP− cells. The RNA samples were then amplified using a NuGEN RNA kit for genomic sample amplification, and sequenced to a depth of 21 (S+P) and 35 (SHH) million paired-end reads on an Illumina HiSeq instrument at the HudsonAlpha Institute of Biotechnology. The reads were aligned to the reference transcriptome as well as a library of exon junctions using Bowtie (Version 1) (Langmead et al., 2009 (link)). Data was analyzed using Expression Plot (Friedman and Maniatis, 2011 (link)) using a P value of 0.001 and a 2 fold change threshold. Gene ontology was performed using DAVID (Huang et al., 2008 , 2009 (link)) with enrichment sets from Expression Plot. The RNA-seq data is available in the Gene Expression Omnibus (GEO) database (http://www.ncbi.nlm.nih.gov/geo/) under the accession number GSE41795. All quantitative data was analyzed using Sigma Plot 11 or Microsoft Excel. Sample groups were subject to Student’s t-test or where appropriate a One-Way ANOVA with Holm-Sidak post hoc pair-wise comparisons was performed. All experimental data passed an equal variance and normality test (Shapiro-Wilk).
Amoroso M.W., Croft G.F., Williams D.J., O'Keeffe S., Carrasco M.A., Davis A.R., Roybon L., Oakley D.H., Maniatis T., Henderson C.E, & Wichterle H. (2013). Accelerated High-Yield Generation of Limb-Innervating Motor Neurons from Human Stem Cells. The Journal of Neuroscience, 33(2), 574-586.
An aliquot of 0.5 μg total RNA was treated with 1 unit DNAse (Fermentas, St. Leon-Rot, Germany) 30 min at 37°C. Reverse transcription of RNA (0.5 μg) was performed with oligo (dT)12–18 primer and 200 units of SUPERSCRIPT II (Invitrogen, Karlsruhe, Germany) and 24 units of Ribo LockTM RNAse inhibitor (Fermentas) for 1 h at 42°C. The cDNA was used for PCR analysis. All cDNA probes were analyzed for: ACTA1, (NM_001100), amplicon length 85 bp; MYOG, (NM_002479), amplicon length 113 bp; MYH3, (NM_002470), amplicon length 84 bp and the RG: ACTB (NM_001101), amplicon length 104 bp; B2M, (NM_004048), amplicon length 98 bp; GAPDH, (NM_002046), amplicon length 119 bp; cyclophilin A/PPIA, (NM_203430), amplicon length 121 bp; RPLPO, (NM_001002), amplicon length 170 bp; TBP, (NM_003194), amplicon length 132 bp. The QuantiTect/PrimerAssays were purchased from QIAGEN GmbH (Hilden, Germany). cDNAs were amplified with Brilliant® II SYBR® Green QRT-PCR Master Mix (Stratagene-Agilent Technologies, Waldbronn, Germany). The thermal profile consisted of 1 cycle at 50°C for 2 minutes followed by 1 cycle at 95°C (2 min), 45 cycles at 95°C (15 sec), 60°C (1 min). Amplification was performed using the Mx3005P™ QPCR System (Stratagene). For relative quantification, a standard curve was generated in every individual run. Shortly, total RNA was pooled from muscle biopsies of healthy human volunteers, reverse transcription was performed and a serial dilution of the cDNA was used to perform the calibration curve. The data were analyzed using the relative standard curve method. For each unknown sample, the relative amount is calculated using linear regression analysis from their respective standard curves. Data were analyzed using the Mx3005P analysis software (Stratagene-Agilent Technologies, Waldbronn, Germany). The efficiencies of all GOI and RG were calculated in every individual run (Table 1).
Stern-Straeter J., Bonaterra G.A., Hörmann K., Kinscherf R, & Goessler U.R. (2009). Identification of valid reference genes during the differentiation of human myoblasts. BMC Molecular Biology, 10, 66.
Biopsy Cyclophilin A Deoxyribonuclease I DNA, Complementary Endoribonucleases GAPDH protein, human Healthy Volunteers Homo sapiens Muscle Tissue Oligonucleotide Primers Oligonucleotides Reverse Transcription SYBR Green II Technique, Dilution
Stable RNAi was achieved by viral shRNA. For Sec10 knockdown, cells were transfected with siRNA oligonucleotides as described6 (link). In all instances knockdown was verified by standard western blot or Q-RT PCR procedures (Brilliant-II SYBR Green Kit, Agilent, Santa Clara, CA), normalizing to GAPDH expression. Q-RT PCR Primers are presented in Supplementary Table 1. RNAi target sequences are presented in Supplementary Table 2. Rab8a_1, Rab10, Rab11a_1, Rab11b, in pRVH1-puro or –hygro retroviruses were previously published44 (link). All other shRNAs were generated in pLKO.1-puro45 (link), or pLKO.1-blast, which was constructed by exchanging the puromycin resistance gene for blasticidin. Cdc42, Par3 and Tuba shRNAs were adapted for pLKO.1 from published sequences21 (link), 46 (link). pLKO.1 lentiviruses were constructed according to the Addgene pLKO.1 protocol (www.addgene.org) using iRNAi (www.mekentosj.com), and target sequences were based on an (AA)N19 algorithm. RNAi sequences were submitted to BLAST (NCBI) to verify target specificity. For isoform-specific RNAi to Rabin8, shRNAs predicted to target the α isoform (Rabin8_4, Rabin8_5) or to both α and β (Rabin8_2) isoforms of canine Rabin8 were extrapolated from sequence alignment with human Rabin8 splice forms (mined from NCBI). For knockdown and rescue experiments, GFP-tagged plasmids of transcripts from human or rat, which are not targeted by anti-canine shRNAs, were used.
Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peränen J., Martin-Belmonte F, & Mostov K.E. (2010). A molecular network for de novo generation of the apical surface and lumen. Nature cell biology, 12(11), 1035-1045.
alpha-Tubulin brilliant green Canis familiaris CDC42 protein, human Cells GAPDH protein, human Genes Homo sapiens Lentivirus Oligonucleotide Primers Oligonucleotides Plasmids Protein Isoforms Puromycin RAB8A protein, human Retroviridae Reverse Transcriptase Polymerase Chain Reaction RNA, Small Interfering RNA Interference Sequence Alignment Short Hairpin RNA Western Blotting
Expression Constructs—The pGW1H-Irga6cTag1 construct was generated by amplification of the Irga6cTag1 sequence from pGEX-4T-2-Irga6cTag1 (former pGEX-4T-2-IIGP-m) (16 (link)) by using Irga6cTag1 forward (5′-cccccccccgtcgaccaccatgggtcagctgttctcttcacctaag-3′) and reverse (5′-cccccccccgtcgactcagtcacgatgcggccgctcgagtcggcctag-3′) primers and cloned into pGW1H vector (British Biotech) by SalI digestion. Mutations were introduced into the coding region of pGW1H-Irga6wt (15 (link)), pGW1H-Irga6cTag1, and pGEX-4T2-Irga6wt (16 (link)) according to the QuikChange site-directed mutagenesis kit (Stratagene) using the following forward and corresponding reverse primers: G2A, 5′-gagtcgaccaccatggctcagctgttctcttca-3′; Δ7-12, 5′-gggtcagctgttctctaataatgatttgccc-3′; Δ7-25, 5′-ccaccatgggtcagctgttctctaaatttaatacggg-3′; Δ20-25, 5′-gaataatgatttgccctccagcaaatttaatacgggaag-3′; F20A, 5′-gagaataatgatttgccctccagcgctactggttattttaag-3′; T21A, 5′-gaataatgatttgccctccagctttgctggttattttaag-3′; G22A, 5′-gccctccagctttactgcttattttaagaaatttaatacggg-3′; Y23A, 5′-gccctccagctttactggtgcttttaagaaatttaatacggg-3′; F24A, 5′-gccctccagctttactggttatgctaagaaatttaatacgggaag-3′; K25A, 5′-gccctccagctttactggttattttgcgaaatttaatacgggaag-3′; K82A, 5′-gggagacgggatcaggggcgtccagcttcatcaataccc-3′; S83N, 5′-ggagacgggatcagggaagaacagcttcatcaataccctg-3′; E106A, 5′-gctaaaactggggtggtggcggtaaccatggaaag-3′. Cell Culture and Serological Reagents—L929 (CCL-1) and gs3T3 (Invitrogen) mouse fibroblasts were cultured in IMDM or Dulbecco's modified Eagle's medium (both GIBCO) supplemented with 10% fetal calf serum (Biochrom). Hybridoma 10D7 and 10E7 cells were grown in IMDM, supplemented with 5% fetal calf serum. Cells were induced with 200 units/ml IFNγ (Cell Concepts) for 24 h and transfected using FUGENE6 transfection reagent according to the manufacturer's protocol (Roche Applied Science). Propagation of T. gondii strain ME49 was done as described previously (8 ). gs3T3 cells were infected for 2 h with T. gondii ME49 strain at a multiplicity of infection of 8 24 h after IFNγ stimulation. The following serological reagents were used: anti-Irga6 mouse monoclonal antibodies 10D7 and 10E7, anti-Irga6 rabbit polyclonal serum 165, anti-cTag1 rabbit polyclonal serum 2600 (8 ), donkey-anti-mouse Alexa 546, donkey anti-rabbit Alexa 488 (all from Molecular Probes), goat anti-mouse κ light chain (Bethyl), goat anti-mouse κ light chain horseradish peroxidase (Bethyl), goat anti-mouse κ light chain-fluorescein isothiocyanate (Southern Biotech), 4′,6-diamidino-2-phenylindole (Roche Applied Science), and donkey anti-rabbit, donkey anti-goat, and goat anti-mouse horseradish peroxidase (all from Amersham Biosciences). Antibody Purification and Papain Digestion—10D7 and 10E7 antibodies were purified from corresponding hybridoma supernatants over a Protein A-Sepharose column (Amersham Biosciences). Antibody was eluted with 50 mm sodium acetate, pH 3.5, 150 mm NaCl and pH-neutralized to 7.5 with 1 m Tris, pH 11. Buffer was exchanged five times subsequently by dilution of antibody-containing sample in papain buffer (75 mm phosphate buffer, pH 7.0, 75 mm NaCl, 2 mm EDTA) and concentrated in a centrifugal concentrator (Vivaspin20; Sartorius) with a 10 kDa cut-off filter at 2000 × g at 4 °C. The concentration of the antibodies was determined by using formula, concentration of antibody (mg/ml) = 0.8 × A280. Papain digestion was done according to Ref. 20 (link). The papain-digested antibodies were further purified on a HiLoad 26/60 Superdex 75 preparation grade column (Amersham Biosciences) in papain buffer. Samples were incubated in SDS-PAGE sample buffer under nonreducing conditions and subjected to SDS-PAGE. Proteins were detected by colloidal Coomassie staining. Treatment with Aluminum Fluoride—AlCl3 (Sigma) was added to 10 ml of IMDM containing no fetal calf serum to a final concentration of 300 μm and mixed by vigorous shaking. Subsequently, NaF (Sigma) was added to a final concentration of 10 mm and mixed, and the final solution was applied to confluent L929 cells previously induced with IFNγ or transfected for 24 h. Cells were incubated in aluminum fluoride complex (AlFx) solution for 30 min at 37 °C and then washed with cold PBS and collected by scraping. Cell pellets were lysed in 0.1% Thesit/PBS containing 300 μm AlCl3 and 10 mm NaF in the presence or absence of 0.5 mm GTP for 1 h at 4 °C. Immunoprecipitation and Immunofluorescence—Immunoprecipitation was modified from Ref. 21 . 1 × 106 L929 fibroblasts/sample were induced with IFNγ and/or transfected for 24 h (or left untreated) and harvested by scraping. Cells were lysed in 0.1% Thesit, 3 mm MgCl2, PBS, Complete Mini protease inhibitor mixture without EDTA (Roche Applied Science) for 1 h at 4 °C in the absence of nucleotide or in the presence of 0.5 mm GDP, GTP, GTPγS, or 300 μm AlCl3 and 10 mm NaF in the presence or absence of 0.5 mm GTP (all from Sigma). Protein A-Sepharose™ CL-4B beads (Amersham Biosciences) were incubated with 10D7 monoclonal mouse anti-Irga6 antibody or 2600 (anti-cTag1) polyclonal rabbit serum for 1 h at 4 °C. Bound proteins were eluted by boiling for 10 min in elution buffer (100 mm Tris/HCl, pH 8.5, 0.5% SDS) with SDS-PAGE sample buffer (50 mm Tris/HCl, pH 6.1, 1% SDS, 5% glycerol, 0.0025% bromphenol blue (w/v), 0.7% β-mercaptoethanol). Immunofluorescence was preformed as previously described (15 (link)).
10D7 antibody detects Irga6 at the PVM but not at the ER. gs3T3 fibroblasts were induced with IFNγ for 24 h prior to 2-h infection with T. gondii ME49 strain with a multiplicity of infection of 8. Irga6 protein was labeled with rabbit anti-Irga6 polyclonal serum 165 (red) and with mouse monoclonal anti-Irga6 antibodies 10E7 (A) or 10D7 (B) (green). PC, phase-contrast images. Parasitophorous vacuoles are indicated by the arrowheads. 10D7 detected Irga6 on the PVM efficiently but the cytoplasmic, ER membrane-associated Irga6 at a barely detectable level.
Colloidal Coomassie Staining—Gels were washed 30 min with H2O and subsequently placed in incubation solution (17% ammonium sulfate (w/v), 20% MeOH, 2% phosphoric acid). After a 60-min incubation, solid Coomassie Brilliant Blue G-250 (Serva) was added to the solution to a concentration of 330 mg/500 ml and incubated 1-2 days. The gels were destained by incubation in 20% MeOH for 1 min and stored in 5% acetic acid. All was done at room temperature and while shaking. Expression and Purification of Irga6 Proteins from E. coli—pGEX-4T-2-Irga6 constructs were transformed into BL-21 E. coli strain. Cells were grown at 37 °C to an A600 of 0.8 when the expression of glutathione S-transferase-fused Irga6 proteins was induced by 0.1 mm isopropyl-β-d-thiogalactoside at 18 °C overnight. Cells were harvested (5000 × g, 15 min, 4 °C); resuspended in PBS, 2 mm DTT, Complete Mini protease inhibitor mixture without EDTA (Roche Applied Science) and lysed using a microfluidizer (EmulsiFlex-C5; Avestin) at a pressure of 150 megapascals. The lysates were cleared by centrifugation at 50,000 × g for 60 min at 4 °C. The soluble fraction was purified on a glutathione-Sepharose affinity column (GSTrap FF 5 ml; Amersham Biosciences) equilibrated with PBS, 2 mm dithiothreitol. The glutathione S-transferase domain was cleaved off by overnight incubation with thrombin (20 units/ml; Serva) on the resin at 4 °C. Free Irga6 was eluted with PBS, 2 mm dithiothreitol, and the protein content in fractions was analyzed by SDS-PAGE and visualized by Coomassie staining (22 (link)). The protein-containing fractions were concentrated in a centrifugal concentrator (Vivaspin20; Sartorius). Aliquots were shock-frozen in liquid nitrogen and stored at -80 °C. The concentration of protein was determined by UV spectrophotometry at 280 nm.
Papic N., Hunn J.P., Pawlowski N., Zerrahn J, & Howard J.C. (2008). Inactive and Active States of the Interferon-inducible Resistance GTPase, Irga6, in Vivo. The Journal of Biological Chemistry, 283(46), 32143-32151.
Photocatalytic degradation of BG dye and 4-NP using Gd(OH)3 and 4, 8, and 12% Ni-Gd(OH)3 NRs under UV light irradiation were investigated. In brief, 10 mg of Gd(OH)3 and 4, 8, and 12% Ni-Gd(OH)3 NRs were mixed with 50 mL of the respective pollutants: 10 ppm of BG dye or 4-NP solutions. The sample mixture was sonicated for 3 min and stirred in the dark for another 3 min. Then, the reaction solutions were continuously stirred and irradiated with UV light (300 W) for 5 h. The absorbance of the BG or 4-NP solution at λmax of 620 and 316 nm, respectively, was taken every 1 h to observe the photocatalysis progress for a total of five hours. The percentage of photocatalytic BG dye or 4-NP degradation was obtained using the following equation (Eq. 1): where Ablank is the absorbance of BG or 4-NP only and Asample is the absorbance of BG or 4-NP after photocatalytic degradation reaction with the respective catalyst.
Matussin S.N., Khan F., Harunsani M.H., Kim Y.M, & Khan M.M. (2024). Photocatalytic degradation of brilliant green and 4-nitrophenol using Ni-doped Gd(OH)3 nanorods. Scientific Reports, 14, 8269.
Gadolinium nitrate hexahydrate (Gd(NO3)3·6H2O, 99%) and nickel nitrate hexahydrate (Ni(NO3)2·6H2O, 99%) were obtained from Sigma-Aldrich. Sodium hydroxide (NaOH, 99.9%) was obtained from Merck. Water was purified using aquatron (England) and used throughout the experiments. For photocatalysis experiments, brilliant green (C27H34N2O4S, 90%) and 4-nitrophenol (C6H5NO3, 99%) were used and obtained from Merck and Sigma-Aldrich, respectively.
Matussin S.N., Khan F., Harunsani M.H., Kim Y.M, & Khan M.M. (2024). Photocatalytic degradation of brilliant green and 4-nitrophenol using Ni-doped Gd(OH)3 nanorods. Scientific Reports, 14, 8269.
The sera (1:400) of Fcgr2b-deficient mice were diluted at 8 months, and wild-type mice were tested for ANA as described11 (link). In short, diluted serum (30 µL) was added to the Hep-2 cell-coated slide, and phosphate-buffered saline (PBS) was used as a negative control, followed by incubation for 30 min. Then, the cells were washed with PBS 2 times and incubated with 30 µL of goat anti-mouse IgG–Alexa (1:500) (Abcam, Cambridge, MA, USA; cat. FA 1512-1010-1) for 30 min and washed with PBS. Finally, the slides were fixed and analyzed under a fluorescence microscope. The researcher will be blinded and grade the intensity as 4 = maximal fluorescence (brilliant yellow-green), 3 = less brilliant (yellow-green fluorescence), 2 = definite (dull yellow-green), and 1 = very dim (subdued fluorescence).
Alee I., Chantawichitwong P., Leelahavanichkul A., Paludan S.R., Pisitkun T, & Pisitkun P. (2024). The STING inhibitor (ISD-017) reduces glomerulonephritis in 129.B6.Fcgr2b-deficient mice. Scientific Reports, 14, 11020.
For the photocatalytic degradation study, three dyes were selected such as Orange G, Acid Blue 161, and Brillant Green. To eliminate the maximum dye level, a Pen‐Ray UV (ColeParmer) lamp with a wavelength of 254 nm and a light intensity of 44 W m−2 was used. The saturated oxygen concentration in the solution medium was achieved with the help of a pump. Experiments were made by adding 100 mg of photocatalyst to a 20 mg L−1 dye solution with a volume of 400 mL. Before starting the experiments, they were mixed for 30 min in the dark for the adsorption and desorption of dye molecules on the surface of the photocatalysis. Samples taken at different time intervals were centrifuged to determine the concentration. The concentration of the samples was measured at wavelengths of 578, 624, and 475 nm using a UV spectrophotometer (Optizen α). Table1 shows the molecular properties of Brilliant Green, Acid Blue 161, and Orange G dyes. Decomposition percentages of Acid Blue 161, Brilliant Green, and Orange G dyestuffs before and after photocatalytic degradation were calculated using Equation 1.
C0 and Cs represent the initial and final dye concentrations in the aqueous phase, respectively.
Tekin D., Birhan D., Tekin T, & Kiziltas H. (2024). Degradation of Orange G, Acid Blue 161, and Brillant Green Dyes Using UV Light‐Activated GA–TiO2–Cd Composite. Global Challenges, 8(5), 2300271.
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The Brilliant III Ultra-Fast SYBR Green QPCR Master Mix is a reagent designed for real-time quantitative PCR (qPCR) applications. It contains SYBR Green I, a fluorescent dye that binds to double-stranded DNA, enabling the detection and quantification of target DNA sequences.
Brilliant II SYBR Green QPCR Master Mix is a ready-to-use solution for quantitative PCR (qPCR) analysis. It contains SYBR Green I dye, enabling real-time detection of DNA amplification.
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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
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The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.
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TRIzol is a monophasic solution of phenol and guanidine isothiocyanate that is used for the isolation of total RNA from various biological samples. It is a reagent designed to facilitate the disruption of cells and the subsequent isolation of RNA.
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The RNeasy kit is a laboratory equipment product that is designed for the extraction and purification of ribonucleic acid (RNA) from various biological samples. It utilizes a silica-membrane-based technology to efficiently capture and isolate RNA molecules.
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The High-Capacity cDNA Reverse Transcription Kit is a laboratory tool used to convert RNA into complementary DNA (cDNA) molecules. It provides a reliable and efficient method for performing reverse transcription, a fundamental step in various molecular biology applications.
Brilliant III SYBR Green QPCR Master Mix is a pre-formulated solution designed for quantitative real-time PCR (qPCR) analysis. It contains all the necessary components, including SYBR Green I dye, for the amplification and detection of DNA targets.
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The IScript cDNA Synthesis Kit is a reagent kit used for the reverse transcription of RNA into complementary DNA (cDNA). The kit contains all the necessary components to perform this reaction, including a reverse transcriptase enzyme, reaction buffer, and oligo(dT) primers.
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The QuantiTect Reverse Transcription Kit is a laboratory tool designed for the reverse transcription of RNA into complementary DNA (cDNA). It enables the conversion of RNA samples into cDNA, which can then be used for various downstream applications, such as real-time PCR or gene expression analysis.
Brilliant green is a synthetic dye that has several applications in the field of microbiology, histology, and topical antiseptic preparations. It is primarily used as a bacteriostatic agent, effectively inhibiting the growth of gram-positive bacteria. Brilliant green is also utilized as a biological stain in various laboratory techniques, such as microscopy and histological sample preparation.
Brilliant green is a widely used reagent in research, particularly in studies involving microbiology and cell biology. However, researchers may face challenges in identifying the most effective and reproducible protocols related to Brilliant green. Factors such as concentration, incubation time, and compatibility with other reagents can vary across different studies, making it difficult to compare and optimize protocols.
Brilliant green is available in various forms, including powder, solution, and pre-made staining kits. The specific form and concentration of Brilliant green can affect its performance and suitability for different applications. Researchers should carefuly select the appropriate Brilliant green product based on their experimental requirements and the desired outcomes.
PubCompare.ai is a powerful tool that can assist researchers in optimizing their Brilliant green studies. The platform allows you to efficiently screen protocol literature, leveraging AI to pinpoit critical insights. PubCompare.ai can help researchers identify the most effective protocols related to Brilliant green for their specific research goals. The platform's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accruacy.
Brilliant green has a range of applications in both research and clinical settings. In microbiology, it is used as a selective growth medium for gram-positive bacteria, allowing for the identification and isolation of specific bacterial strains. In histology, Brilliant green is employed as a counterstain, enhancing the visualization of cellular structures and tissue samples. Additionally, Brilliant green has been used in topical antiseptic preparations, leveraging its bacteriostatic properties to prevent infection in wound care and other clinical applications.
