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Amido Black

Amido Black is a versatile dye used in various biomedical applications, including protein staining and blotting.
It provides a sensitive and reliable method for detecting and visualizing proteins separated by gel electrophoresis.
The PubCompare.ai platform leverages AI-driven comparisons to help researchers identify the best protocols and products for their research workflow, enhancing reproducibility and accuracy.
With Amido Black, researchers can locate relevant protocols from the literature, preprints, and patents, optimizing their research protocols and streamlining their research process.

Most cited protocols related to «Amido Black»

1
SDS-PAGE Protein Separation and Western Blot Analysis
Cited 8 times
Separation of proteins under denaturing conditions was conducted by SDS-PAGE using 15% acrylamide gels [66] (link), [67] . The amount of total protein loaded per lane was 6 µg, 12 µg, and 50 µg for HapR, Dns, and TfoX detection, respectively. For western blot analysis, the proteins were transferred onto PVDF western blotting membranes (Roche), stained with amido black to verify transfer efficiency, incubated in blocking buffer, and reacted with primary antibodies directed against HapR (1∶5000), Dns (1∶1000), or TfoX (1∶2000). Detection of the primary antibody was performed using a secondary goat anti-rabbit IgG antibody conjugated to peroxidase (Sigma A9169; used at a 1∶20,000 dilution). Signals were revealed using Lumi-LightPLUS Western Blotting substrate (Roche, Switzerland) and were recorded by exposure to chemiluminescence-detecting films (Amersham Hyperfilm ECL, GE Healthcare).
Lo Scrudato M, & Blokesch M. (2012). The Regulatory Network of Natural Competence and Transformation of Vibrio cholerae. PLoS Genetics, 8(6), e1002778.
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Publication 2012
Acrylamide Amido Black anti-IgG Antibodies Buffers Chemiluminescence Gels Goat Immunoglobulins Peroxidase polyvinylidene fluoride Proteins Rabbits SDS-PAGE Technique, Dilution Tissue, Membrane Western Blot
2
Quantification of Phospholipids, Proteins, and Q10 in Samples
Cited 4 times
Total phospholipid contents were determined using an assay for the quantification of phosphate described previously.28 Total protein contents were determined using the amido black method to minimize interference by phospholipids.62 (link),63 Total Q10 content was measured using a previously published method with modifications.35 (link) 1−2 μL of PL sample was added to 100 μL of HPLC-grade ethanol, vortexed for ~30 s, and then the Q10 was reduced by addition of 1 mM KBH4 from a 1 M aqueous stock solution. After 10 min, the precipitated protein was removed by a 2 min spin at 16,300 × g, and samples placed on dry ice until required. For analysis, 50 μL was injected onto a Nucleosil 100−5C18 column attached to an Agilent 1100 series HPLC system equipped with a Thermo Scientific Dionex Ultimate 3000RS Electrochemical Detector (ECD) and eluted in a mobile phase of 70% ethanol, 30% methanol, 0.7% NaClO4, and 0.07% HClO4 flowing at 800 μL min−1. Standard ECD potentials of +1000, −500, and +300 mV were used to detect the Q10H2. The first cell (+1000 mV) conditions the buffer, while the second and third cells allow quantification of Q10 and Q10H2. Because no Q10 is present (it has been reduced chemically prior to injection), we observe only the Q10H2 peak detected using the third cell. Mito-CI content and orientation were determined using the NADH:A-PAD+ oxidoreduction assay and by comparison to standard samples as described previously,28 in the presence and absence of 20 μg mL−1 alamethicin. Ec-F1F0 orientation was determined by measuring ATP hydrolysis as described previously,28 in the presence and absence of 20 μg mL−1 alamethicin. Ec-F1F0 contents were calculated by subtracting the mito-CI content from the total protein content.
Biner O., Fedor J.G., Yin Z, & Hirst J. (2020). Bottom-Up Construction of a Minimal System for Cellular Respiration and Energy Regeneration. ACS synthetic biology, 9(6), 1450-1459.
Publication 2020
Alamethicin Amido Black Biological Assay Buffers Cells Dry Ice Ethanol Germ Cells High-Performance Liquid Chromatographies Hydrolysis Methanol Mitomycin NADH Oxidation-Reduction Phosphates Phospholipids potassium borohydride Proteins
3
SDS-PAGE and Western Blot Analysis of Cell Signaling Proteins
Cited 4 times
SDS-PAGE and Western blot analysis were performed as described previously (Saxon et al. 1994; Frey et al. 1997), using either 10% (PKC isozymes, pRb, p107, and p130) or 20% (cdks, cyclins, and CKIs) SDS-polyacrylamide minigels. 30 μg of protein, assayed in quadruplicate by the bicinchoninic acid (BCA) method (Pierce Chemical Co.), was loaded per lane, and blots were routinely stained with either 0.1% Fast green (Sigma-Aldrich) or 1% Amido black (Sigma-Aldrich) immediately after transfer to ensure equal loading and even transfer. Primary antibody dilutions were as follows: 1:500 for anti-Rb, –cyclin D1, and -p27kip1; 1:1,000 for anti-p15, -p16, -p21waf1/cip1, -p107, -p130, -cdk2, -cdk4, -PKCδ, -GFP, and –cyclin A; and 1:2,000 for anti–cyclin E, –cyclin D (pan), -PKCα, and -PKCε. Secondary antibodies were used at 1:2,000.
Frey M.R., Clark J.A., Leontieva O., Uronis J.M., Black A.R, & Black J.D. (2000). Protein Kinase C Signaling Mediates a Program of Cell Cycle Withdrawal in the Intestinal Epithelium. The Journal of Cell Biology, 151(4), 763-778.
Publication 2000
Amido Black Antibodies bicinchoninic acid CCND1 protein, human CDK2 protein, human CDKN1B protein, human CHKA protein, human Cyclin-Dependent Kinases Cyclin A Cyclin E Cyclins Fast Green Immunoglobulins Isoenzymes polyacrylamide PRKCA protein, human Protein Kinase C-epsilon Proteins RBL1 protein, human SDS-PAGE Technique, Dilution Western Blot
4
Exosome Isolation and Characterization from NSC-34 Cells
Cited 3 times
Exosomes were isolated from the extracellular media of wt and mSOD1 NSC-34 cells, as currently in use in our lab (Cunha et al., 2016 (link)). Briefly, the culture media (20 ml) of the NSC-34 cells differentiated for 4 DIVs was centrifuged at 1,000 g for 10 min to remove cell debris. Then, the supernatant was transferred to another tube and centrifuged again at 16,000 g for 60 min, to separate microvesicles (size ~1,000 nm). The recovered supernatant was subsequently filtered in a 0.22 μm pore filter, and further centrifuged in the Ultra L-XP100 centrifuge (Beckman Coulter Inc., California, USA) at 100,000 g for 120 min to pellet exosomes (size ~100 nm). The pellet of exosomes was then resuspended in phosphate-buffered saline (PBS) and centrifuged one last time at 100,000 g for 120 min, in order to wash the pellet. All centrifugations were performed at 4°C. Characterization of exosomes in terms of size and concentration was performed by Nanoparticle tracking analysis (NTA) using the Nanosight, model LM10-HSBF (Malvern, UK) and the NTA software version 3.1. Transmission electron microscopy (TEM) technique used the Jeol JEM 1400 Transmission Electron Microscope (Peabody, MA, USA). Western blot analysis was performed as usual in our lab (Vaz et al., 2015 (link)) to evaluate the expression of alix, flotillin-1 and CD63 by using 20 μg of total protein and specific antibodies (mouse anti-Alix, Cell Signaling, #2171; mouse anti-flotillin-1, BD Biosciences, #6108; goat anti-CD63, Santa Cruz Biotechnology, #sc-31214). Normalization was made by using Amido Black staining as loading control. To evaluate total RNA and microRNA, the final pellet containing exosomes was resuspended in lysis buffer, and exosomal RNA extracted with the miRCURY Isolation Kit-Cell (Exiqon), as described below.
Pinto S., Cunha C., Barbosa M., Vaz A.R, & Brites D. (2017). Exosomes from NSC-34 Cells Transfected with hSOD1-G93A Are Enriched in miR-124 and Drive Alterations in Microglia Phenotype. Frontiers in Neuroscience, 11, 273.
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Publication 2017
Amido Black Antibodies Buffers Cell-Derived Microparticles Cells Cell Separation Centrifugation Culture Media Exosomes FLOT1 protein, human Goat MicroRNAs Mus Phosphates Proteins Saline Solution TDO inhibitor LM10 Transmission Electron Microscopy Western Blot
5
Western Blot Analysis of Phosphorylation
Cited 3 times
For Western blot analyses using anti-phosphothreonine (α-pThr), anti-StkP, and anti-PhpP antibodies, bacteria were grown exponentially in 5 mL BHI broth to OD620 ≈ 0.1 to 0.2–0.5. Aliquots of 1.0 to 1.5 mL were centrifuged (5 min, 13,000×g at 25 °C), and cell pellets were put on dry ice. Frozen pellets were resuspended in 20 µL SEDS lysis buffer (0.1% deoxycholate (vol/vol), 150 mM NaCl, 0.2% SDS (vol/vol), 15 mM EDTA pH 8.0) for samples with OD620 ≈ 0.1–0.2 and 40–80 µL for samples with OD620 ≈ 0.4. Samples were incubated at 37°C for 15 min until cells visibly lysed as determined via phase microscopy. The Bio-Rad DC™ protein assay kit I was used to determine total protein concentrations of samples using a standard curve of 0.1 to 3.0 mg/mL of BSA. Absorbance (750 nm) were determined in a 96-well plate reader (Synergy H1 Hybrid Reader, BioTek). Samples were diluted with 2× Laemlli SDS loading buffer (Bio-Rad) and incubated at 95°C for 10 min. 12.5 µg of total protein was loaded per sample onto a 4–15% precast gradient SDS-PAGE gel (Bio-Rad) and subjected to electrophoresis. Proteins were transferred to a nitrocellulose membrane. StkP proteins, PhpP proteins, and threonine-phosphorylated proteins were detected respectively with anti-StkP (1:50,000), anti-PhpP (1:20,000), or α-pThr (1:2000) (Novakova et al., 2010 (link)) as primary antibodies, and ECL anti-rabbit IgG horseradish peroxidase linked whole antibody as secondary (1:10,000). Chemiluminescent signals in protein bands were detected with 1–3 min exposures and quantified using an IVIS imaging system as described in previously (Wayne et al., 2010 (link)). To determine relative amounts of threonine-phosphorylated proteins and the PhpP and StkP proteins, luminescence values for each band were subtracted by the value of the background (defined as a box enclosing the same area of the blot with no detectable signal or from a Δ[phpP-stkP]). Background-subtracted amounts are expressed relative to amounts in wild-type or bacteria that were not depleted for GpsB. After blotting, membranes were stained with amido black solution to confirm that protein loading was similar between samples.
Rued B.E., Zheng J.J., Mura A., Tsui H.C., Boersma M.J., Mazny J.L., Corona F., Perez A.J., Fadda D., Doubravová L., Buriánková K., Branny P., Massidda O, & Winkler M.E. (2017). Suppression and Synthetic-Lethal Genetic Relationships of ΔgpsB Mutations Indicate That GpsB Mediates Protein Phosphorylation and Penicillin-Binding Protein Interactions in Streptococcus pneumoniae D39. Molecular microbiology, 103(6), 931-957.
Publication 2017
6-(beta-pyridyl)-3-hydroxy-pyrazol(3,4b)pyridine Amido Black Anti-Antibodies Antibodies Bacteria Biological Assay Buffers Cells Deoxycholate Dry Ice Edetic Acid Electrophoresis Freezing Hybrids IGG-horseradish peroxidase Immunoglobulins Luminescence Microscopy Nitrocellulose Pellets, Drug Phosphothreonine Proteins Rabbits SDS-PAGE Sodium Chloride Synapsin I Threonine Tissue, Membrane Western Blot

Most recents protocols related to «Amido Black»

1
Protein Quantification and Western Blotting
Whole cell extracts from 5 × 105 cells (6–8 µ-slides) were obtained at 3 h and 6 h post treatment and lysed using cell lysis RIPA buffer (Sigma Aldrich, Schnelldorf, Germany) supplemented with complete mini EDTA free protease cocktail inhibitor (Roche, Germany) and PhosSTOP (Roche, Munich, Germany). The lysates were centrifuged at 10,000× g for 30 min at 4 °C. Protein concentrations were determined using Amido black assay and 20 µg of protein in sample buffer was subjected to 7.5–15% SDS-PAGE and transferred onto polyvinylidene difluoride membrane (Immobilon-P, Millipore, Burlington, MA, USA). For immunoblotting, membranes were incubated with primary antibodies as mentioned above (refer to antibodies section). Subsequently, membranes were incubated with horseradish peroxidase conjugated secondary antibodies prior to detection with a lumisensor chemiluminescent HRP substrate using LAS 3000 reader (Fujifilm, Kleve, Germany). Band densities were measured by densitometry (ImageJ software Version 1.51, NIH, Bethesda, MD, USA). Density values are expressed as a ratio normalized to loading control and the fold change is compared to control samples.
Bola S., Subramanian P., Calzia D., Dahl A., Panfoli I., Funk R.H, & Roehlecke C. (2023). Analysis of Electric Field Stimulation in Blue Light Stressed 661W Cells. International Journal of Molecular Sciences, 24(4), 3433.
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Publication 2023
Amido Black Antibodies Biological Assay Buffers Cell Extracts Cells Densitometry Edetic Acid Immobilon P polyvinylidene fluoride Protease Inhibitors Proteins Radioimmunoprecipitation Assay SDS-PAGE Tissue, Membrane
2
Chromatin Fractionation for Protein Analysis
Chromatin fractionation was performed as described63 (link). Briefly, cells were washed in PBS and resuspended in 1 ml buffer A (10 mM HEPES pH 7.9, 10 mM KCl, 1.5 mM MgCl2, 0.34 M sucrose, 10% glycerol, 1 mM DTT and 1X protease inhibitor cocktail). Triton X-100 was added to 0.1% and the cells are incubated on ice for 10 min. Nuclei were collected by centrifugation at 4000 rpm at 4 °C. The supernatant was taken as the cytosolic fraction. Nuclei were washed once with buffer A and then lysed for 30 min in ‘No Salt’ buffer (3 mM EDTA, 0.2 mM EGTA, 1 mM DTT, and 1X protease inhibitor cocktail) on ice. Chromatin was pelleted by centrifugation at 4000 rpm at 4 °C and supernatant was enriched in soluble nuclear proteins. For western blotting, equal amounts of isolated chromatin, estimated by amido black (Sigma) staining, were run on an 8%, 15% or 4-15% SDS-PAGE gel, then transferred to PVDF membranes (Millipore). After blocking with Intercept® (PBS) Blocking Buffer (LI-COR) for 1 h at room temperature, the membrane was incubated with primary antibodies at 4 °C overnight. The membrane was then washed three times with PBST for 10 min and then incubated for 1 h at room temperature with appropriate secondary antibodies conjugated with Dylight (Invitrogen). After extensive washing, fluorescent detection was performed using the Odyssey® Fc imaging system (Li-Cor Biosciences). Alternatively, immunoblotting was performed as described63 (link). For the quantification of the bands obtained by Western blot experiments, the relative density of the band obtained from the Odyssey® Fc imaging system after blotting with antibodies of interest was normalized to the relative density of the bands obtained by blotting with antibodies against housekeeping proteins (H3 or H4). This ratio was used to compare expressions between conditions.
Mohammed Ismail W., Mazzone A., Ghiraldini F.G., Kaur J., Bains M., Munankarmy A., Bagwell M.S., Safgren S.L., Moore-Weiss J., Buciuc M., Shimp L., Leach K.A., Duarte L.F., Nagi C.S., Carcamo S., Chung C.Y., Hasson D., Dadgar N., Zhong J., Lee J.H., Couch F.J., Revzin A., Ordog T., Bernstein E, & Gaspar-Maia A. (2023). MacroH2A histone variants modulate enhancer activity to repress oncogenic programs and cellular reprogramming. Communications Biology, 6, 215.
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Publication 2023
Amido Black Antibodies Cardiac Arrest Cell Nucleus Cells Centrifugation Chromatin Cytosol Edetic Acid Egtazic Acid Fractionation, Chemical Glycerin HEPES Magnesium Chloride Nuclear Proteins polyvinylidene fluoride Protease Inhibitors Proteins SDS-PAGE Sodium Chloride Sucrose Tissue, Membrane Triton X-100 Western Blotting
3
Circadian Regulation of Microglia
Western blotting was used to investigate the oscillation of PER2 and BMAL1 clock proteins, and for quantification of phosphorylated-p47phox levels in BV2 microglia. Time course samples were collected from synchronized BV2 cells as described above. For measurement of phospho-p47phox levels, BV2 cells were plated in 6-well plates at a density of 105 cells/mL and allowed to reach 90% confluence. At confluence, cells were treated with LPS (1 μg/mL), or LPS (1 μg/mL) + apocynin (100 μM), or LPS (1 μg/mL) + GSK2795039 (25 μM) for 24 h. BV2 cells with no additives were used as a control. For all samples, cells were washed with ice-cold PBS and lysed with RIPA lysis buffer (Millipore Sigma, Burlington, MA) containing the Halt Protease Inhibitor Cocktail (ThermoFischer Scientific). Protein concentrations were measured using the Pierce BCA Protein Assay Kit (Pierce, Waltham, MA). Samples were loaded at 25 μg of total protein per lane, resolved by SDS-PAGE (BioRad, Hercules, CA), and transferred onto nitrocellulose membranes (Bio-Rad). Following blocking with 5% skim milk in PBST (137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, pH 7.4, 0.2% Tween-20) for 2 h at room temperature, the membranes were incubated with primary antibodies against PER2 (1:1000, Invitrogen, Waltham, MA), BMAL1 (1:1000, Invitrogen), and phospho-p47phox (Ser 370) (1:1000, Invitrogen) at 40C in 1% skim milk in PBST overnight. Post-overnight incubation, the membranes were washed six times with PBST and incubated with secondary antibody (1:10,000) for 1 h. The membranes were then washed with PBST, and the protein bands were detected using SuperSignal West Pico Chemiluminescent Substrate (Pierce). Amido black staining (see below) was used to normalize protein loading. Protein bands were detected using the BioRad ChemiDoc XRS+ Imager (BioRad). Quantification of detected protein bands was performed with the ImageLab 6.0.1 software (Life Science, Waltham, MA).
Muthukumarasamy I., Buel S.M., Hurley J.M, & Dordick J.S. (2023). NOX2 inhibition enables retention of the circadian clock in BV2 microglia and primary macrophages. Frontiers in Immunology, 14, 1106515.
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Publication 2023
acetovanillone Amido Black Antibodies Biological Assay Buffers Cells CLOCK Proteins Cold Temperature GSK2795039 Immunoglobulins Microglia Milk, Cow's NCF1 protein, human Nitrocellulose Protease Inhibitors Proteins Radioimmunoprecipitation Assay SDS-PAGE Sodium Chloride Tissue, Membrane Tween 20
4
Amido Black Protein Quantification
Amido Black staining was used to measure total protein loaded in a lane as the internal loading-control for Western blots. Following detection of protein bands, membranes were washed three times in DI water. The membranes were then stained for 1 min using a staining solution containing 0.1% amido black reagent in 10% acetic acid solution. The membranes were then washed twice for 1 min with a de-staining solution containing 5% acetic acid. Post de-staining, the membranes were washed two times for 10 min each in DI water. The membranes were then air-dried and visualized using a Bio-Rad ChemiDoc XRS+ Imager. Quantification of amido black stained membranes was done using the ImageLab 6.0.1 software.
Muthukumarasamy I., Buel S.M., Hurley J.M, & Dordick J.S. (2023). NOX2 inhibition enables retention of the circadian clock in BV2 microglia and primary macrophages. Frontiers in Immunology, 14, 1106515.
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Publication 2023
Acetic Acid Amido Black Proteins Tissue, Membrane Western Blot
5
Microglial Cell Line BV2 Inflammatory Assay
The BV2 mouse microglial cell line was obtained from Banca Cellule ICLC, Genova, Italy. Lipopolysaccharide (LPS) 500X was obtained from Invitrogen (Waltham, MA). Murine IL-4 was obtained from Peprotech Inc. (Rocky Hill, NJ). NOX2 inhibitors apocynin and GSK2795039 (GSK) were purchased from Millipore Sigma (Burlington, MA) and MedChemExpress (Monmouth Junction, NJ), respectively. Primary antibodies against phospho-p47phox (Ser 370), PER2, and BMAL1, and goat anti-rabbit secondary antibody were obtained from Invitrogen. Phosphate buffered saline (PBS) and trypsin-EDTA for cell culture were obtained from Gibco, ThermoFisher Scientific (Waltham, MA). The Amido Black stain was obtained from ThermoFisher Scientific.
Muthukumarasamy I., Buel S.M., Hurley J.M, & Dordick J.S. (2023). NOX2 inhibition enables retention of the circadian clock in BV2 microglia and primary macrophages. Frontiers in Immunology, 14, 1106515.
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Publication 2023
acetovanillone Amido Black Antibodies Antibodies, Anti-Idiotypic Cell Culture Techniques Cell Lines Edetic Acid Goat GSK2795039 inhibitors Lipopolysaccharides Microglia Mus NCF1 protein, human Phosphates Rabbits Saline Solution Stains Trypsin

Top products related to «Amido Black»

1
Amido black by Merck Group
Sourced in United States, Germany
Amido Black is a type of lab equipment used for the detection and quantification of proteins. It is a staining dye that binds to proteins and can be used to visualize and analyze protein samples in various laboratory techniques, such as gel electrophoresis and Western blotting.
2
Technovit 7100 by Kulzer
Sourced in Germany, United Kingdom, United States
Technovit 7100 is a two-component resin system designed for embedding and preparing samples for microscopic analysis. It is a cold-curing resin that allows for the preservation of the original structure and morphology of the embedded samples.
3
Clarity western ecl substrate by Bio-Rad
Sourced in United States, Germany, United Kingdom, Italy, France, Japan, Canada, China, Spain, Australia, Denmark, Belgium, Sweden, Finland, Netherlands, Panama
Clarity Western ECL Substrate is a chemiluminescent detection reagent used in Western blotting applications. It is designed to provide a sensitive and reliable method for detecting and quantifying target proteins.
4
Image lab software by Bio-Rad
Sourced in United States, China, Germany, United Kingdom, Italy, France, Canada, Australia, Belgium, Japan, Portugal, Sweden, Czechia, Switzerland, Spain
Image Lab software is a data analysis tool designed for use with Bio-Rad's gel and blot imaging systems. The software provides a user-friendly interface for capturing, analyzing, and processing images of gels, blots, and other samples.
5
Amido black 10b by Merck Group
Sourced in Germany
Amido black 10B is a protein staining dye used in biochemical applications. It is a black, water-soluble powder that binds to proteins, allowing their visualization and quantification.
6
Chemidoc instrument by Bio-Rad
Sourced in United States
The ChemiDoc instrument is a compact and versatile imaging system designed for capturing and analyzing images of chemiluminescent, fluorescent, and colorimetric samples. It provides high-quality imaging capabilities for a wide range of applications in the life sciences and analytical chemistry fields.
7
Pvdf membrane by Bio-Rad
Sourced in United States, Germany, China, United Kingdom, Japan, France, Canada, Spain, Italy, Australia, Switzerland, Austria, Belgium
PVDF membranes are a type of laboratory equipment used for protein transfer and detection in Western blot analysis. They provide a stable and durable surface for the immobilization of proteins, enabling effective identification and quantification of target proteins in complex biological samples.
8
Axioskop 2 by Zeiss
Sourced in Germany, United States, Japan, United Kingdom, Canada, Italy
The Axioskop 2 is a laboratory microscope designed for a variety of applications. It features a robust optical system and advanced illumination options to support high-quality imaging. The core function of the Axioskop 2 is to provide a versatile platform for microscopic observation and analysis.
9
Chemidoc mp imaging system by Bio-Rad
Sourced in United States, United Kingdom, China, Germany, Canada, France, Australia, Italy, Spain, Japan, Denmark, Austria, Israel, Sweden, Portugal, Belgium, Singapore, United Arab Emirates
The ChemiDoc MP Imaging System is a versatile laboratory instrument designed for the detection and analysis of various biomolecules, including proteins, nucleic acids, and chemiluminescent samples. It utilizes advanced imaging technology to capture high-quality images and data for applications such as Western blotting, gel documentation, and DNA/RNA visualization.
10
Dc protein assay kit by Bio-Rad
Sourced in United States, United Kingdom, Germany, Italy, Australia, Spain, China, Japan, France, Canada, Belgium, Czechia, Sweden
The DC protein assay kit is a colorimetric-based protein quantification method developed by Bio-Rad. It allows for the determination of protein concentration in aqueous solutions.

More about "Amido Black"

Amido Black, also known as naphthol blue-black or Naphthol blue-black B, is a versatile and widely-used dye in various biomedical applications.
It is particularly renowned for its ability to stain and visualize proteins separated by gel electrophoresis, providing a sensitive and reliable method for protein detection and analysis.
Beyond its use in protein staining, Amido Black finds applications in diverse areas, including Western blotting, immunohistochemistry, and even in the detection of DNA and RNA.
Its adaptability and effectiveness have made it an indispensable tool for researchers across numerous fields, from biochemistry and molecular biology to clinical diagnostics.
To optimize the research workflow and enhance reproducibility, the PubCompare.ai platform leverages AI-driven comparisons to help researchers identify the best protocols and products for their specific needs.
This includes not only Amido Black, but also related techniques and reagents such as Technovit 7100 for embedding samples, Clarity Western ECL Substrate for chemiluminescent protein detection, and the Image Lab software for image analysis.
Amido Black 10B, a specific variant of the dye, is often utilized for its sensitivity and versatility, allowing researchers to detect even minute amounts of proteins.
The ChemiDoc instrument, a popular imaging system, is frequently employed in conjunction with Amido Black for the visualization and quantification of protein bands.
Additionally, PVDF membranes and the Axioskop 2 microscope can be seamlessly integrated into the research workflow, providing a comprehensive suite of tools for protein analysis and visualization.
The ChemiDoc MP Imaging System, with its advanced features and capabilities, further enhances the research process by enabling high-quality imaging and data analysis.
To complement these techniques, the DC protein assay kit offers a reliable method for determining the concentration of proteins, ensuring accurate quantification and standardization of experiments.
By leveraging the insights and capabilities provided by these tools and technologies, researchers can streamline their workflows, improve reproducibility, and gain deeper insights into their biological systems of interest.