Deep purple total protein stain

Manufactured by GE Healthcare

Sourced in United Kingdom

Deep Purple Total Protein Stain is a laboratory product designed for the sensitive detection of proteins in polyacrylamide gels. It provides a reliable and consistent method for visualizing and quantifying proteins separated by electrophoresis.

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Lab products found in correlation

Ne per nuclear and cytoplasmic extraction reagent, by Thermo Fisher Scientific (2 mentions) Decyder software, by GE Healthcare (1 mentions) Typhoon 9400 scanner, by GE Healthcare (1 mentions) Labworks 4, by Analytik Jena (1 mentions) Kaleidoscope prestained standard, by Bio-Rad (1 mentions) Endo hf, by New England Biolabs (1 mentions) Tris hcl ready gel, by Bio-Rad (1 mentions) Epichemi3 darkroom, by Analytik Jena (1 mentions) Amylose resin, by New England Biolabs (1 mentions) Phosphatase inhibitor cocktails 1 and 2, by Merck Group (1 mentions) Recombinant protein g agarose, by Thermo Fisher Scientific (1 mentions) Enhanced chemiluminescence ecl, by GE Healthcare (1 mentions) Horseradish peroxidase hrp conjugated secondary antibody, by Santa Cruz Biotechnology (1 mentions) Chromatin immunoprecipitation chip assay kit, by Merck Group (1 mentions) Sybr green pcr master mix, by Thermo Fisher Scientific (1 mentions) Protease inhibitor mixture, by Roche (1 mentions) Ultraflex 3 tof tof, by Bruker (1 mentions)

6 protocols using deep purple total protein stain

2-DE Gel Proteomic Analysis of E. ictaluri

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Preparative 2-DE gels were prepared exactly as described above, except that the IPG strips were loaded with 500 μg of protein. Resultant gels were stained using Deep Purple Total Protein Stain (GE Healthcare) according to the manufacturer’s protocols. Briefly, gels were fixed overnight in 15% v/v ethanol and 1% w/v citric acid followed by staining for 1 h in 1:200 parts of Deep Purple and 100 mM sodium borate solution at pH 10.5. Gels were then washed for 30 min with 15% v/v ethanol in water, acidified for 30 min using a solution containing 15% v/v ethanol and 1% w/v citric acid. Stained gels were scanned using a Typhoon 9410 imager using a 532 nm laser and a 610 nm BP30 emission filter. In-gel trypsin digestion and MALDI peptide mass fingerprinting (PMF) was performed as previously described [46 (link)] with slight modifications (mass tolerance value was 150 ppm and E. ictaluri protein database was used).

Dumpala P.R., Peterson B.C., Lawrence M.L, & Karsi A. (2015). Identification of Differentially Abundant Proteins of Edwardsiella ictaluri during Iron Restriction. PLoS ONE, 10(7), e0132504.

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Quantitative Protein Extraction and Identification

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Semi-preparative gels, containing 400 ug of total protein extract per strip, were loaded; electrophoretic conditions were the same as for 2-D DIGE, except that gels were stained with a protein fluorescent stain (Deep Purple Total Protein Stain, GE-Healthcare). Image acquisition was performed using the EDI imager. Protein identification was carried out as described previously, and MS data are reported in Supporting Information.

Fania C., Arosio B., Capitanio D., Torretta E., Gussago C., Ferri E., Mari D, & Gelfi C. (2017). Protein signature in cerebrospinal fluid and serum of Alzheimer’s disease patients: The case of apolipoprotein A-1 proteoforms. PLoS ONE, 12(6), e0179280.

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Quantitative Proteomics Analysis of Atrial Fibrillation

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Gel images were acquired on a Typhoon 9400 scanner (GE Healthcare Life Sciences) and analyzed using DeCyder software (version 6.0; GE Healthcare Life Sciences) as previously described (26 (link),27 (link)). Briefly, Cy2-, Cy3- and Cy5-labeled images of each gel were scanned with excitation/emission wavelengths of 488/520, 532/580 and 633/670 nm, respectively. Following CyDye labeling, signals were imaged and the gels were stained using Deep Purple total protein stain (GE Healthcare Life Sciences) according to standard protocols and scanned with excitation/emission wavelengths of 532/560 nm. The 2-D DIGE gel images were subsequently analyzed with DeCyder software. Protein expression patterns for SR-RAA were compared with AF-RAA, and SR-LAA were compared with AF-LAA. Ratios of proteins that increased or decreased >1.5-fold (t-test, P<0.05) were considered significant changes (9 (link)). The corresponding protein spots were also selected in the stained preparative gel for spot picking.

Liu H., Chen G., Zheng H., Qin H., Liang M., Feng K, & Wu Z. (2016). Differences in atrial fibrillation-associated proteins between the left and right atrial appendages from patients with rheumatic mitral valve disease: A comparative proteomic analysis. Molecular Medicine Reports, 14(5), 4232-4242.

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Deglycosylation of Purified PRRSV

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In non-reducing conditions, 2 µg of purified PRRSV was incubated with 100~500 units of peptide-N-glycosidase F (PNGase F, New England Biolabs, Ipswich MA) in 50 mM sodium phosphate, pH 7.5, or 100~400 units of endoglycosidase H_f (Endo H_f, New England Biolabs) in 50 mM sodium citrate, pH 5.5, at 37°C for 1 h. The mixture of virus and endoglycosidase was added to gel loading buffer with 5% β-mercaptoethanol, boiled for 10 min and electrophoresed in 10–20% gradient Tris-HCl Ready Gels (Bio-Rad Laboratories, Hercules CA). For PNGase F samples, CandyCane Glycoprotein Molecular Weight Standards (Invitrogen) were used to estimate protein size and protein bands were visualized with RubyProtein Gel Stain (Invitrogen). For Endo H_f samples, Kaleidoscope Prestained Standards (Bio-Rad) were used to estimate protein size and protein bands were visualized with Deep Purple Total Protein Stain (GE Healthcare, Buckinghamshire, UK). Finally, proteins were analyzed in EpiChemi³ Darkroom (UVP, Upland CA) using LabWorks 4.5 software (UVP).

Li J., Tao S., Orlando R, & Murtaugh M.P. (2015). N-Glycosylation Profiling of Porcine Reproductive and Respiratory Syndrome Virus Envelope Glycoprotein 5. Virology, 478, 86-98.

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Detailed Immunoblotting and ChIP Assay

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Anti-RACK1 (sc-17754), anti-pan actin (sc-1616), anti-GAPDH (sc-25778) antibodies and the horseradish peroxidase (HRP)-conjugated secondary antibodies were purchased from Santa Cruz Biotechnology. Anti-phospho-CREB (#9191), and anti-CREB (#9121) antibodies were from Cell Signaling. Anti-β-actin antibody (#A5316, clone AC-74), forskolin, (FSK) cytochalasin D and phosphatase inhibitor cocktails 1 and 2 were purchased from Sigma-Aldrich. The protease inhibitor mixture was purchased from Roche Applied Science. Nuclear proteins were isolated using the NE-PER Nuclear and Cytoplasmic Extraction Reagents from Thermo Scientific. Trypsin, and the reverse transcription system and 2X PCR Master Mix were purchased from Promega and SYBR® Green PCR Master Mix was from Applied Biosystem. Primers for PCR were synthesized by Sigma-Genosys. Chromatin immunoprecipitation (ChIP) assay kit was from Millipore. Amylose resin was from New England BioLabs. Deep Purple™ Total Protein Stain and Enhanced Chemiluminescence (ECL) were from GE Healthcare. Non-muscle purified actin >99% purity (#APHL99) was purchased from Cytoskeleton. NuPAGE® Bis-Tris pre-casted gels and recombinant protein G-agarose were from Invitrogen.

Neasta J., Fiorenza A., He D.Y., Phamluong K., Kiely P.A, & Ron D. (2016). Activation of the cAMP Pathway Induces RACK1-Dependent Binding of β-Actin to BDNF Promoter. PLoS ONE, 11(8), e0160948.

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Semipreparative Gel Protein Identification

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Semipreparative gels, containing 400 µg of total protein extract per strip, were loaded; electrophoretic conditions were the same as for 2D-DIGE, except that gels were stained with a protein fluorescent stain (Deep Purple Total Protein Stain, GE Healthcare). Image acquisition was performed using the Typhoon 9200 laser scanner. Proteins were identified by PMF utilizing a MALDI-ToF mass spectrometer (Ultraflex III ToF/ToF; Bruker Daltonics, Bremen, Germany), as previously described [26] . In particular, the search was performed by correlation of uninterpreted spectra to Homo sapiens entries in NCBInr database 20100918 (11833178 sequences; 4040378175 residues). Protein identification methods are provided in a MIAPE-MS compliant form [21] in Supporting Information Table 1S. (For further information about protein identification, see Supporting Information Table 2S and Supporting Information Figure 1S).

Moriggi M., Pastorelli L., Torretta E., Tontini G.E., Capitanio D., Bogetto S.F., Vecchi M, & Gelfi C. (2017). Contribution of Extracellular Matrix and Signal Mechanotransduction to Epithelial Cell Damage in Inflammatory Bowel Disease Patients: A Proteomic Study. Proteomics, 17(23-24).

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