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Proteosilver plus

Manufactured by Merck Group
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ProteoSilver Plus is a silver-based protein staining kit for the detection of proteins in polyacrylamide gels. It provides a sensitive and reliable method for visualizing proteins separated by SDS-PAGE.

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Lab products found in correlation

Imagemaster 2d platinum v7, by GE Healthcare (1 mentions) Ltq orbitrap mass spectrometer, by Thermo Fisher Scientific (1 mentions) Mascot search engine 2, by Matrix Science (1 mentions) Protein assay kit, by Bio-Rad (1 mentions)

Close spelling variants of this product

ProteoSilver Plus kit ProteoSilver Plus Silver Staining Kit ProteoSilver Plus Silver Stain Kit ProteoSilver

5 protocols using proteosilver plus

1

Characterization of IgG Hexamers

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The IgG-hexamers prepared from patients’ sera were separated by SDS-PAGE and silver stained (with ProteoSilver™ plus, Sigma). The heavy (γ) and light chains were identified by their molecular mass and high abundance. All other protein bands were excised from the gels and subjected to mass spectrometry at the Smoler Protein Research Center (Technion – Israel Institute of Technology, Haifa, Israel).
Naseraldeen N., Michelis R., Barhoum M., Chezar J., Tadmor T., Aviv A., Shvidel L., Litmanovich A., Shehadeh M., Stemer G., Shaoul E, & Braester A. (2021). The Role of Alpha 2 Macroglobulin in IgG-Aggregation and Chronic Activation of the Complement System in Patients With Chronic Lymphocytic Leukemia. Frontiers in Immunology, 11, 603569.
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2

Comparative Proteomic Analysis of Gels

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Two different stains, one with CoomassieBrillant Blue (CBB) for one-dimensional gels, and the second silver nitrate for two-dimensional gels, were used (this was prepared on the same gel after the first staining with CBB). In the case of CBB staining gels, they were incubated for 30 min in a dye solution containing 0.1% (w/v) Coomassie Blue - G250, 10% (v/v) acetic acid, and 25% (v/v) isopropanol and finally the gels were transferred to a bleaching solution of 10% (v/v) acetic acid and 10% (v/v) isopropanol. For silver nitrate staining, the suggested kit protocol was followed (ProteoSilver™ Plus, Sigma).
The image acquisition was performed by gel scanning III Image Scanner (GE Healthcare Life Sciences). Image Master 2D Platinum v 7.0 (GE Healthcare Life Sciences) software for comparative analysis of two-dimensional gels were used, which allowed to define differentially spots expressed between two or more situations analysed using the complimentary statistical analysis.
Moraga N.B., Irazusta V., Amoroso M.J, & Rajal V.B. (2017). BIO-PRECIPITATES PRODUCED BY TWO AUTOCHTHONOUS BORON TOLERANT STREPTOMYCES STRAINS. Journal of environmental chemical engineering, 5(4), 3373-3383.
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3

Proteomic Analysis of OPTN-Interacting Proteins

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For liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis, proteins were separated by 10% SDS-PAGE under reducing conditions. Proteins were visualised by silver staining with ProteoSilver Plus (Sigma), bands were excised from both the OPTN-IP and control-IP gel lanes and processed for in-gel digestion and LC-MS/MS with the LTQ-Orbitrap mass spectrometer (Thermo Fisher Scientific, Loughborough, UK), as previously described (Mulvey et al., 2013 (link)). Raw MS files were analysed by the Mascot search engine 2.3.02 (Matrix Science, London, UK) and searched against a SwissProt human database 2013_10 (containing 39,696 entries including common contaminants). Mascot search analysis parameters included: trypsin enzyme specificity, allowance for 2 missed cleavages, peptide mass tolerance of 20 ppm for precursor ions and fragment mass tolerance of 0.8 Da. Oxidation (M) was selected as a variable modification and carbamidomethyl (C) was selected as a fixed modification.
Chew T.S., O'Shea N.R., Sewell G.W., Oehlers S.H., Mulvey C.M., Crosier P.S., Godovac-Zimmermann J., Bloom S.L., Smith A.M, & Segal A.W. (2015). Optineurin deficiency in mice contributes to impaired cytokine secretion and neutrophil recruitment in bacteria-driven colitis. Disease Models & Mechanisms, 8(8), 817-829.
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4

Comparative SILAC Proteomics Analysis

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The protein concentration of all the samples was evaluated with the Bio-Rad protein assay kit (Bio-Rad, Hemel Hempstead, UK). For comparative SILAC analysis, heavy and light total cell lysates and nuclear and cytoplasmic fractions were mixed in a 1:1 ratio based on the final protein concentration (30 μg) and separated by 12% SDS-PAGE, under reducing conditions. Proteins were visualized by silver staining (ProteoSilver Plus, Sigma Aldrich, Poole, U.K.), and bands (33 horizontal slices), excised from the gel lane, were destained using a solution containing 100 mM sodium thiosulphate and 30 mM potassium ferricyanide in ratio 1:1. Samples were reduced by 10 mM DTT and alkylated with 100 mM iodoacetamide using the ProGest Investigator Instrument (DigiLab, Genomics Solutions, Cambs, U.K.) according to the established protocol.37 (link) Finally, each dry gel piece was rehydrated in 30 μL of 50 mM ammonium bicarbonate solution containing 250 ng of Trypsin Gold, Mass Spectrometry grade (Promega, Madison, USA), and incubated at 37 °C overnight. The trypsinolysis was stopped with 0.1% formic acid (FA), and tryptic peptides were eluted, vacuum-dried, and dissolved in 0.1% formic acid for LC–MS/MS analysis.
Pinto G., Alhaiek A.A., Amadi S., Qattan A.T., Crawford M., Radulovic M, & Godovac-Zimmermann J. (2014). Systematic Nucleo-Cytoplasmic Trafficking of Proteins Following Exposure of MCF7 Breast Cancer Cells to Estradiol. Journal of proteome research, 13(2), 1112-1127.
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5

Proteomics Analysis of Decellularized Liver

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A proof-of-concept proteomics analysis was performed comparing fresh liver, DET and EDTA-DET scaffolds (n = 1). Prior to proteomics analysis a punch biopsy and standard histology confirmed appropriate decellularization. Proteins extracted from fresh liver samples, EDTA-DET and DET treated liver samples were separated by 12% SDS-PAGE, under reducing conditions. Proteins were visualized by silver staining (ProteoSilver Plus, Sigma, UK), and bands (32 horizontal slices for each sample) excised from the gel lane and destained using a solution containing 100 mM sodium thiosulphate and 30 mM potassium ferricyanide in ratio 1:1. Samples were reduced by 10 mM DTT and alkylated with 100 mM iodoacetamide using the ProGest Investigator Instrument (DigiLab, Genomics Solutions, Cambs, UK) according to the established protocol [24 (link)]. Finally, each dry gel piece was rehydrated in 30 μL of 50 mM ammonium bicarbonate solution containing 250 ng of Trypsin Gold, Mass Spectrometry grade (Promega, Madison, USA), and incubated at 37°C overnight. The trypsinolysis was stopped with 0.1% formic acid (FA), and tryptic peptides were eluted, vacuum dried, and dissolved in 0.1% FA for LC−MS/MS.
Maghsoudlou P., Georgiades F., Smith H., Milan A., Shangaris P., Urbani L., Loukogeorgakis S.P., Lombardi B., Mazza G., Hagen C., Sebire N.J., Turmaine M., Eaton S., Olivo A., Godovac-Zimmermann J., Pinzani M., Gissen P, & De Coppi P. (2016). Optimization of Liver Decellularization Maintains Extracellular Matrix Micro-Architecture and Composition Predisposing to Effective Cell Seeding. PLoS ONE, 11(5), e0155324.
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