Coomassie brilliant blue cbb

Manufactured by Nacalai Tesque

Sourced in Japan

Coomassie brilliant blue (CBB) is a synthetic dye commonly used in biochemistry and molecular biology for the staining of proteins in gel electrophoresis and other analytical techniques. It is a versatile and widely-used staining agent that binds non-specifically to proteins, allowing for the visualization and quantification of protein samples.

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Lab products found in correlation

Mal peg 2000, by NOF corporation (3 mentions) Creatinine colorimetric assay kit, by Cayman Chemical (2 mentions) Las 4000 image analyzer system, by Fujifilm (1 mentions) Immobilon p transfer membrane, by Merck Group (1 mentions) Supersignal west femto substrate, by Thermo Fisher Scientific (1 mentions) Pd 10 column, by GE Healthcare (1 mentions) Chemidoc touch imaging system, by Bio-Rad (1 mentions) Skim milk, by BD (1 mentions) Ecl prime, by Bio-Rad (1 mentions) Chemi lumi one ultra, by Nacalai Tesque (1 mentions) Chemidoc, by Bio-Rad (1 mentions)

6 protocols using coomassie brilliant blue cbb

Quantification of Urinary Albumin in Mice

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Urine samples were collected from 8-week-old mice by gentle manual compression of the
abdomen. To measure albumin, urine samples were diluted with sample buffer containing 2%
sodium dodecyl sulfate (SDS), 5% 2-mercaptoethanol, 10% glycerol, 60 mM Tris-HCL (pH 6.8)
and bromophenol blue, and heated at 95°C for 5 min. Samples containing 1
µl of urine were applied to 10% SDS-polyacrylamide gel electrophoresis.
As a positive control, 5 µg of bovine serum albumin was loaded
simultaneously. The gel was fixed and stained with Coomassie brilliant blue (CBB; Nacalai
Tesque, Kyoto, Japan) according to manufacturer’s instructions, and scanned using a
standard commercial scanner. CBB-stained band corresponding to urinary albumin was
quantified using the ImageJ gel analysis program (http://imagej.net/). Urinary creatinine
was measured using a creatinine colorimetric assay kit (Cayman chemical, Ann Arbor, MI,
USA) according to manufacturer’s instructions. The urinary albumin excretion was
normalized against the urinary creatinine. Urine collection was performed twice over a
three-day period, and the measured urinary albumin excretion was averaged for each
mouse.

Sasaki H., Takahashi Y., Ogawa T., Hiura K., Nakano K., Sugiyama M., Okamura T, & Sasaki N. (2019). Deletion of the Tensin2 SH2-PTB domain, but not the loss of its PTPase activity, induces podocyte injury in FVB/N mouse strain. Experimental Animals, 69(2), 135-143.

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Gelatin Zymography for Aorta Proteases

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Lysed human aorta samples were mixed with 5x non-reducing sample buffer (312.5 mmol/L Tris-HCl [pH 6.8], 11.5% SDS, 40% glycerol), and loaded onto a 7.5% SDS-PAGE gel containing 4 mg/mL gelatin. After SDS-PAGE, the gel was washed twice with washing buffer (50 mmol/L Tris-HCl [pH 7.5], 2.5% Triton X-100, 5 mmol/L CaCl₂, 1 µmol/L ZnCl₂) at 37 °C for 30 min each time, and then incubated in incubation buffer (50 mmol/L Tris-HCl [pH 7.5], 1% Triton X-100, 5 mmol/L CaCl₂, 1 µmol/L ZnCl₂) for 10 min with gentle agitation, followed by replacement with fresh incubation buffer and incubation for 24 h at 37 °C. After Coomassie Brilliant Blue (CBB; Nacalai Tesque) staining, areas of gelatin degradation were visible as clear and sharp bands against a blue background of the non-degraded substrate. Band densities were analyzed using ImageJ software (National Institute of Health, Bethesda, MD, USA).

Molla M.R., Shimizu A., Komeno M., Rahman N.I., Soh J.E., Nguyen L.K., Khan M.R., Tesega W.W., Chen S., Pang X., Tanaka-Okamoto M., Takashima N., Sato A., Suzuki T, & Ogita H. (2022). Vascular smooth muscle RhoA counteracts abdominal aortic aneurysm formation by modulating MAP4K4 activity. Communications Biology, 5, 1071.

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SDS-PAGE and Immunoblotting Protocol

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The protein samples were subjected to 10–20% gradient sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The proteins were stained by Coomassie Brilliant Blue (CBB; Nacalai Tesque, Kyoto, Japan) or transferred to an Immobilon-P Transfer Membrane (Merck Millipore) and reacted with the appropriate antibodies. The immune complexes were visualized with the SuperSignal West Femto substrate (Thermo Scientific, Rockford, IL) and detected by an LAS-4000 image analyzer system (Fujifilm, Tokyo, Japan).

Shima R., Li T.C., Sendai Y., Kataoka C., Mori Y., Abe T., Takeda N., Okamoto T, & Matsuura Y. (2016). Production of hepatitis E virus-like particles presenting multiple foreign epitopes by co-infection of recombinant baculoviruses. Scientific Reports, 6, 21638.

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Quantifying Urinary Albumin in Mice

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Urine samples were collected from 8-week-old mice by gentle manual compression of the abdomen. To measure albumin, urine samples were diluted with sample buffer containing 2% sodium dodecyl sulfate (SDS), 5% ß-mercaptoethanol, 10% glycerol, 60 mM Tris-HCL (pH 6.8) and bromophenol blue, and heated at 95 °C for 5 min. Samples containing 1 μL of urine were applied to 10% SDS-polyacrylamide gel electrophoresis. As a positive control, 5 μg of bovine serum albumin was loaded simultaneously. The gel was fixed and stained with Coomassie brilliant blue (CBB; Nacalai Tesque, Kyoto, Japan) according to manufacturer’s instructions, and scanned using a standard commercial scanner. CBB-stained urinary albumin was quantified by the ImageJ gel analysis program (http://imagej.net/). Urinary creatinine was measured using a creatinine colorimetric assay kit (Cayman chemical, Michigan, USA) according to manufacturer’s instructions. The urinary albumin excretion was normalized against the urinary creatinine. Urine collection was performed twice over a three-day period, and the measured urinary albumin excretion was averaged for each mouse.

Takahashi Y., Sasaki H., Okawara S, & Sasaki N. (2018). Genetic loci for resistance to podocyte injury caused by the tensin2 gene deficiency in mice. BMC Genetics, 19, 24.

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Redox regulation of GPx7 and GPx8

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Purified GPx7, the luminal domain of GPx8, PDIs and their mutants were separately reduced with 10 mM DTT for 10 min at 30ºC followed by DTT removal through a PD-10 column (GE Healthcare) pre-equilibrated with 50 mM Tris/HCl (pH 7.4) buffer containing 300 mM NaCl. To analyze the redox status of GPx7, GPx8 and their mutants, different concentrations (10, 50 and 200 μM) of H2O2 was mixed with 1 μM reduced GPx7, GPx8 or their mutants in degassed buffer containing 50 mM Tris/HCl (pH 7.4) and 300 mM NaCl at 30C. For PDI oxidation assays, 10 μM reduced PDI was incubated with 1 μM GPx7, GPx8 or their mutants, and reactions were initiated by adding 10, 50 or 200 μM of H2O2. At indicated time points, samples were quenched using 1 mM mal-PEG 2000 (NOF Corporation). The reaction mixture was boiled for 3 min after an addition of an equal volume of 2  Laemmli buffer. All samples were run through non-reducing SDS-PAGE followed by staining with Coomassie Brilliant Blue (CBB) (Nacalai Tesque). The gel images were captured by using ChemiDoc Touch Imaging System (Bio-Rad).

Kanemura S., Sofia E.F., Hirai N., Okumura M., Kadokura H., & Inaba K. (2020). Biochemical characterizations of ER-resident peroxidases, GPx7 and GPx8, reveal their distinct and regulated oxidative activities.

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SDS-PAGE and Western Blot Analysis

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Before SDS-PAGE, samples were mixed with sample buffer containing βmercaptoethanol 38 , and boiled at 98°C for 5 minutes. For mouse samples, the polyvinylidene difluoride (PVDF) membrane was treated with Tris-buffered saline (TBS)-0.1% Tween20 (Nacalai Tesque) containing 10% skim milk (Becton Dickinson and Company) for 1 hour, followed by the primary antibody [IZUMO1, SLC2A3, HA, and FLAG (1:1,000), 1D4 (1:5,000)] for 3 hours or overnight. After washing with TBST, the membrane was treated with secondary antibodies (1:1,000). For zebrafish samples, after wet transfer onto nitrocellulose, total protein was visualized by Ponceau staining before blocking with 5% milk powder in TBST. The primary antibody [mouse antizebrafish-Dcst2 (1:50 in blocking buffer)] was incubated overnight at 4°C. The membrane was washed with TBST before secondary antibody incubation for 1 hour. The HRP activity was visualized with ECL prime (BioRad) and Chemi-Lumi One Ultra (Nacalai Tesque) (for mouse) or ChemiDoc (BioRad) (for zebrafish). Then, the total proteins on the membrane were visualized with Coomassie Brilliant Blue (CBB) (Nacalai Tesque).

Noda T., Blaha A., Fujihara Y., Gert K.R., Emori C., Deneke V.E., Oura S., Berent S., Kodani M., Panser K., Cabrera-Quio L.E., Pauli A., & Ikawa M. (2021). Sperm membrane proteins DCST1 and DCST2 are required for the sperm-egg fusion process in mice and fish.

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