Bio safe coomassie blue

Manufactured by Bio-Rad

Sourced in Italy, United States, Canada

Bio-Safe Coomassie blue is a protein stain used for the detection and quantification of proteins in polyacrylamide gels. It is a ready-to-use solution that provides consistent and reliable results.

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Lab products found in correlation

32p atp, by PerkinElmer (3 mentions) Recombinant kinase, by PerkinElmer (2 mentions) Glutathione sepharose 4b, by Thermo Fisher Scientific (2 mentions) Taq dna polymerase, by New England Biolabs (1 mentions) His spintrap, by GE Healthcare (1 mentions) His gravitrap, by GE Healthcare (1 mentions) Mini protein tetra system, by Bio-Rad (1 mentions) Quikchange lightning, by Agilent Technologies (1 mentions) Tris acetaterunning buffer, by Thermo Fisher Scientific (1 mentions) Hi mark unstained molecular weight ladder, by Thermo Fisher Scientific (1 mentions) Nupage lds sample buffer, by Thermo Fisher Scientific (1 mentions) Pvdf membrane, by Thermo Fisher Scientific (1 mentions) Mini protean gel system, by Bio-Rad (1 mentions) Tris glycine, by Bio-Rad (1 mentions) Criterion tgx gel, by Bio-Rad (1 mentions) Nativemark, by Thermo Fisher Scientific (1 mentions) E coli bl21 cells, by New England Biolabs (1 mentions) Quikchange lightning site directed mutagenesis kit, by Agilent Technologies (1 mentions) Mass spectrometry grade trypsin, by Promega (1 mentions) Criterion xt 4 12 bis tris gel, by Bio-Rad (1 mentions)

15 protocols using bio safe coomassie blue

SDS-PAGE Separation of Wheat Proteins

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Electrophoretic runs were performed according to the study by Ruiz et al. (2016) (link) with minor modifications. Proteins (40 mg lane^–1) were separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) using The Mini Protean TETRA apparatus (Bio-Rad Laboratories, Italy). The molecular mass standard was the Neobiotech (Nanterre, France) Elite Prestained Protein Ladder (6.5–270 kDa). Samples were dried (RapidVap Evaporator Labconco) under vacuum and resuspended in 30 ml MilliQ water, and thus, sample buffer was added [final concentrations 2% SDS, 10% glycerol, 200 mM 2-mercaptoethanol, and 0.01 mg/ml bromophenol blue in 63 mM Tris-HCl (pH 6.8)]. Samples were boiled for 5 min prior to loading. Gels were fixed at room temperature in methanol/glacial acetic acid/water (50/5/45, v/v) for 20 min and then in 50% methanol for 10 min. After fixing, gels were stained with Bio-Safe Coomassie blue (Bio-Rad, Milan, Italy) as described in the instruction protocol.
Gliadins were subdivided into two classes (ω- and α-, γ-) based on their molecular weight, whereas glutenins were subdivided into HMW-GS and LMW-GS (De Santis et al., 2017 (link)). Protein profiles were analyzed using the Azurespot Pro software (Azure Biosystems, Dublin, CA, United States).

Poggi G.M., Aloisi I., Corneti S., Esposito E., Naldi M., Fiori J., Piana S, & Ventura F. (2022). Climate change effects on bread wheat phenology and grain quality: A case study in the north of Italy. Frontiers in Plant Science, 13, 936991.

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Purification of His-tagged Proteins

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Chemicals reagents were from Sigma-Merck. Deoxynucleosides, dNMPs, dNTPs, AMP, ADP and ATP were all of >99% purity. Acetic anhydride and H₃PO₄ (85%) used for the synthesis of acetyl phosphate were ACS grade. Taq DNA polymerase and broad range (10–200 kDa) molecular weight markers were from New England Biolabs (MA, USA). SDS-PAGE gels (15%) were run on a Mini-protein Tetra system and stained with Bio-safe Coomassie Blue (Biorad). His-tagged proteins were purified with His-GraviTrap or His-SpinTrap kits from GE Healthcare.

Loan T.D., Easton C.J, & Alissandratos A. (2019). DNA amplification with in situ nucleoside to dNTP synthesis, using a single recombinant cell lysate of E. coli. Scientific Reports, 9, 15621.

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SDS-PAGE Analysis of Chitosan Protein

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Fifty micrograms of CHT were analysed on 10% SDS-PAGE. Protein bands in the gel were visualized after staining with BioSafe Coomassie Blue (Bio-Rad) and subsequently destained in 9% acetic acid and 5% methanol. Pharmacia low molecular-weight electrophoretic standards were used as molecular weight markers [30 (link)].

Nicolaus B., Poli A., Di Donato P., Romano I., Laezza G., Gioiello A., Ulgiati S., Fratianni F., Nazzaro F., Orlando P, & Dumontet S. (2016). Pb2+ Effects on Growth, Lipids, and Protein and DNA Profiles of the Thermophilic Bacterium Thermus Thermophilus. Microorganisms, 4(4), 45.

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Cpx7A Mutagenesis and Kinase Assay

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QuikChange Lightning (Agilent) was used for site-directed mutagenesis of unedited Cpx7A to generate Cpx7A^I125M,N130S (termed N130S). Recombinant Cpx fused with GST was expressed in E. coli (BL21) and purified using glutathione sepharose 4B (Fisher Scientific). Peak fractions were concentrated and further purified by gel filtration as previously described^{11 (link)}. In vitro kinase assays were performed using purified recombinant Cpx proteins and the catalytic subunit of CK2 (C70–10G, SignalChem). Briefly, 10 mg of purified GST-fusion protein (unedited Cpx7A^I125,N130 or edited Cpx7A^I125M,N130S) was used per reaction and incubated with 2,500 units of recombinant kinase and [³²P]ATP (Perkin Elmer). Reaction products were separated by SDS-PAGE and gels were stained with Bio-Safe Coomassie Blue (Bio-Rad), dried, and exposed to autoradiography film at room temperature. Mean integrated density of each band was quantified using FIJI and relative density of phospho-Cpx (pCpx) was calculated by normalizing to input band intensity determined by Coomassie staining.

Brija E.A., Guan Z., Jetti S.K, & Littleton J.T. (2023). Stochastic RNA editing of the Complexin C-terminus within single neurons regulates neurotransmitter release. bioRxiv.

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Protein Separation and Visualization

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Samples were centrifuged at 16,000g for 5 min to separate the soluble fraction (supernatant) from the insoluble fraction (pellet). Both fractions were dissolved in NuPAGE LDS sample buffer (Life Technologies, Carlsbad, CA) with and without 50 mM DTT (BioRad) and incubated at 80°C for 90 s. Approximately 10 μg of each sample was separated on a 3-8% Tris-Acetate gel using Tris-Acetate running buffer (Life Technologies) for 65 min at 150V. A Hi-Mark unstained molecular weight ladder was used as a reference (Life Technologies). The starting protein concentration for the supernatant of one sample (stir-D3) was low so a maximum of 20 μL was loaded. Protein bands were visualized by staining with Bio-Safe Coomassie blue (BioRad).

Telikepalli S.N., Kumru O.S., Kalonia C., Esfandiary R., Joshi S.B., Middaugh C.R, & Volkin D.B. (2014). Structural Characterization of IgG1 mAb Aggregates and Particles Generated under Various Stress Conditions. Journal of pharmaceutical sciences, 103(3), 796-809.

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Mitrecin A Protein Sequencing

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Purified Mitrecin A was separated by SDS-PAGE using Mini-PROTEAN TGX Any kD polyacrylamide gels (Bio-Rad) and was transferred to a polyvinylidene difluoride (PVDF) membrane (Life Technologies; IB4010-02) using an iBlot gel transfer system. Protein transferred to the membrane was stained with BioSafe Coomassie blue (Bio-Rad), and the bands corresponding to Mitrecin A protein were excised. The membrane-bound protein was washed six times with Type-I water, and ten residues of the N-terminus were sequenced at the Iowa State University Protein Facility by Edman degradation using a 494 Procise protein sequencer and a 140C Analyzer (Life Technologies).

Farris M, & Steinberg A. (2014). Mitrecin A, an endolysin-like bacteriolytic enzyme from a newly isolated soil streptomycete. Letters in Applied Microbiology, 58(5), 493-502.

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Separation and Identification of MHC Isoforms

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We performed separation and identification of MHC isoforms following a previously described method^{28 (link)}. Briefly, muscle blocks were cut into cryosections of 10 μm thickness in a cryostat (Thermo Electronic) cooled to −20°C. Myosin isoforms were separated using 6% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) on a Bio-Rad Mini-PROTEAN gel system (Bio- Rad, Hercules, CA, USA). Electrophoresis was performed at 140 V for 10 h. The gels were subsequently stained with Bio-Safe Coomassie blue (Bio-Rad, Hercules, CA, USA). In the MHC isoform region, three major bands were separated in order of migration to MHC I or IIa and IIx depending on their molecular masses compared with those of marker proteins. Each MHC isoform was expressed as percentage of total densitometry. Densitometry was performed using ImageJ software (National Institutes of Health, MD, USA) (Figure 1).

Oh S.L., Yoon S.H, & Lim J.Y. (2018). Age- and sex-related differences in myosin heavy chain isoforms and muscle strength, function, and quality: a cross sectional study. Journal of Exercise Nutrition & Biochemistry, 22(2), 43-50.

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Native Protein Gel Electrophoresis

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Protein samples
were prepared in Milli-Q water and diluted with native buffer (Biorad)
at a ratio 1:0.8 v/v. An amount of 25 μL of the resulting solution
was loaded per lane in a 4–20% Criterion TGX gel (Biorad).
NativeMark (Life Technologies) was used as marker. Electrophoresis
was run at 125 V constant for 75 min using tris-glycine (Biorad) as
running buffer. Staining of the gels was performed with Bio-Safe Coomassie
blue (Biorad) for 2 h. Gels were left overnight after abundant washing
with demineralized water to further develop the bands before scanning.

Garcia E.S., van Leeuwen J.J., Safi C., Sijtsma L., van den Broek L.A., Eppink M.H., Wijffels R.H, & van den Berg C. (2018). Techno-Functional Properties of Crude Extracts from the Green Microalga Tetraselmis suecica. Journal of Agricultural and Food Chemistry, 66(29), 7831-7838.

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Cpx7A Mutagenesis and Kinase Assay

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QuikChange Lightning Site-Directed Mutagenesis Kit (Agilent) was used for site-directed mutagenesis of unedited Cpx7A to generate Cpx7A^I125M,N130S (termed N130S). Cpx variants were subcloned into a pGEX-2T construct (GE Healthcare Life Sciences) and the recombinant Cpx variants fused with GST were expressed in BL21 E. coli cells (New England BioLabs) and purified using glutathione Sepharose 4B (Thermo Fisher Scientific). Peak fractions were concentrated and further purified by gel filtration as previously described.^{10 (link)}In vitro kinase assays were performed using purified recombinant Cpx proteins and the catalytic subunit of CK2 (C70-10G; SignalChem). Briefly, 10 mg of purified GST-fusion protein (unedited Cpx7A^I125,N130 or edited Cpx7A^I125M,N130S) was used per reaction and incubated with 2,500 units of recombinant kinase and [³²P]ATP (PerkinElmer). Reaction products were separated by SDS-PAGE and gels were stained with Bio-Safe Coomassie Blue (Bio-Rad), dried, and exposed to autoradiography film at room temperature. Mean integrated density of each band was quantified using FIJI and relative density of phospho-Cpx (pCpx) was calculated by normalizing to input band intensity determined by Coomassie staining.

Jalving R., van de Vondervoort P.J., Visser J, & Schaap P.J. (2000). Characterization of the Kexin-Like Maturase of Aspergillus niger. Applied and Environmental Microbiology, 66(1), 363-368.

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Super-SILAC Proteomics Protocol

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Unlabeled primary cell lysates were mixed with the super-SILAC standard in a 1:1 ratio by protein content, as determined by BCA assay. All samples were desalted and buffer exchanged to Tris/HCl buffer using Micro bio-spin 6 columns (Bio-Rad, Hercules, CA). Protein concentration was determined by BCA assay and aliquots containing 80ug of total protein per sample run (up to 240ug for triplicate analysis) were dried by vacuum centrifugation. Protein pellets were resuspended in XT sample buffer containing Criterion XT reducing agent and denatured at 95°C for five minutes. Proteins were resolved by SDS-PAGE on Criterion XT 4-12% Bis-Tris gels (Bio-Rad, Hercules, CA) at 180 volts for 1 hour. The gels were fixed (50:5:45/methanol:aceticacid:water/v:v:v), stained with Bio-Safe Coomassie blue (Bio-Rad, Hercules, CA) and destained in H2O. 32 gel sections were excised from each sample run and the individual bands were processed for in-gel trypsin proteolysis as previously described¹⁰. Trypsin digestion was performed using 12.5ng/ul of mass spectrometry grade Trypsin (Promega, Madison, WI) diluted in 25mM NH₄HCO₃ solution. Peptides recovered from each band were dried by vacuum centrifugation and resuspended in 8ul of 0.1% TFA for mass spectrometry analysis.

Staal J.A., Lau L.S., Zhang H., Ingram W.J., Hallahan A.R., Northcott P.A., Pfister S.M., Wechsler-Reya R.J., Rusert J.M., Taylor M.D., Cho Y.J., Packer R.J., Brown K.J, & Rood B.R. (2015). Proteomic profiling of high risk medulloblastoma reveals functional biology. Oncotarget, 6(16), 14584-14595.

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