Silver staining kit

Manufactured by Thermo Fisher Scientific

Sourced in United States

The Silver staining kit is a laboratory product designed for the detection and visualization of proteins in gels. It utilizes a silver-based staining method to enhance the contrast and visibility of protein bands, enabling their identification and analysis.

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SilverQuest Silver Staining Kit (120 citations) Silver staining (52 citations) Pierce Silver Staining Kit (27 citations) SilverXpress Silver Staining Kit (25 citations) PageSilver silver staining kit (2 citations)

55 protocols using silver staining kit

High-resolution Separation of Multiprotein Complexes

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Three to twelve percentage of BN-PAGE (Invitrogen, Carlsbad, CA, USA) was carried out using 1 μg of purified HIS-tagged recombinant proteins according to the manufacturer. This technique allows the separation of very high molecular weight multiprotein complexes. Gels were run in Running buffer (0.002% Coomassie G-250, 50 mM BisTris/50 mM Tricine, pH 6.8) at 150 V for approximately 2 h. Gels were incubated in Tris/glycine/SDS buffer for 30 min and either stained with a Silver Staining kit (Invitrogen) or processed for western blot as described.

Lalle M., Camerini S., Cecchetti S., Finelli R., Sferra G., Müller J., Ricci G, & Pozio E. (2015). The FAD-dependent glycerol-3-phosphate dehydrogenase of Giardia duodenalis: an unconventional enzyme that interacts with the g14-3-3 and it is a target of the antitumoral compound NBDHEX. Frontiers in Microbiology, 6, 544.

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SDS-PAGE Protocol for Parasite Analysis

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All the samples (n=60) were analyzed on SDS-PAGE gels (10% separation gel, 5% stacking gel). A suspension containing 1×10⁵ parasites per ml was mixed with an equal volume of SDS-PAGE sample buffer with 8–16% Tris-Glycine (Novex, US) and loaded onto SDS-PAGE gels. Standard molecular weight markers, including 14–97 kDa (Santa Cruz, US) were also loaded onto SDS-PAGE gels. Electrophoresis was carried out at 100 V (gel electrophoresis apparatus, BioRad). Gels were stained with Silver Staining Kit (SilverQuest
^TM, Invitrogen).

OZLEM-CALISKAN S., ERTABAKLAR H., BILGIN M.D, & ERTUG S. (2016). Assessment of the Effects of Extremely Low Frequency Electromagnetic Fields on Toxoplasma gondii. Iranian Journal of Parasitology, 11(2), 159-167.

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Identification of Mutant p53-Binding Proteins

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To determine potential mutp53-binding proteins, p53^−/− RKO cells transduced with the empty control vector or vectors expressing R175H mutp53 or wtp53 were employed for co-IP by using the anti-p53 (DO-1) beads (Santa Cruz Biotechnology, sc-126AC). The p53 protein complex was eluted with 0.1 M glycine solution, separated in a SDS-PAGE gel, visualized by silver staining using a silver staining kit (Invitrogen), and analyzed by LC-MS/MS at the Biological Mass Spectrometry facility of Rutgers University.

Liu J., Zhang C., Xu D., Zhang T., Chang C.Y., Wang J., Liu J., Zhang L., Haffty B.G., Zong W.X., Hu W, & Feng Z. (2023). The ubiquitin ligase TRIM21 regulates mutant p53 accumulation and gain of function in cancer. The Journal of Clinical Investigation, 133(6), e164354.

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Immunoblotting Analysis of Malaria Virion Proteins

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Virions (2 × 10⁹ v.p./lane) were lysed in 1x SDS sample buffer, denatured by heating at 70°C for 10 min, and applied onto a 4–12% gradient polyacrylamide gel under a reducing condition. After electrophoresis, the gel was stained with a silver staining kit (Invitrogen Carlsbad, CA, USA). For Western blotting, the separated proteins were blotted onto a nitrocellulose membrane. The membrane was blocked in 3% skim milk, and then incubated with Protein G-purified mouse monoclonal anti-NANP antibody (2A10)[7 (link)]. After washing, the blots were incubated with horseradish peroxidase (HRP) - labeled goat anti-mouse IgG antibody (Thermo Fisher Scientific Inc., Waltham, MA, USA), and the signal was developed using an ECL detection system (GE Healthcare).

Shiratsuchi T., Rai U., Kaneko I., Zhang M., Iwanaga S., Yuda M, & Tsuji M. (2017). A potent malaria vaccine based on adenovirus with dual modifications at Hexon and pVII. Vaccine, 35(50), 6990-7000.

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Virus Purification and Protein Analysis

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Purified viruses (10¹⁰ vp) were resuspended in Laemmli lysis buffer, boiled for 10 min and loaded onto a 10% NuPage gel (Novex, Invitrogen, CA, USA). After electrophoresis, the gel was stained with a silver staining kit (Invitrogen, Carlsbad, CA, USA). Alternatively, the gel was transferred on nitrocellulose membrane and the membrane was incubated with a rabbit polyclonal antibody directed against the fiber protein.

Anchim A., Raddi N., Zig L., Perrieau P., Le Goffic R., Ryffel B, & Benihoud K. (2018). Humoral Responses Elicited by Adenovirus Displaying Epitopes Are Induced Independently of the Infection Process and Shaped by the Toll-Like Receptor/MyD88 Pathway. Frontiers in Immunology, 9, 124.

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Identification of RRAD-binding Proteins

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To determine the potential RRAD binding proteins, RRAD-Flag protein in H1299-RRAD cells was pulled down by IP using anti-Flag (M2) beads and eluted with 0.1M glycine solution. H1299-con cells were used as a control. Eluted materials were separated in a 4-16% SDS-PAGE gel and visualized by silver staining using the silver staining kit (Invitrogen). LC-MS/MS analysis was performed at the Biological Mass Spectrometry facility of Rutgers University.

Liu J., Zhang C., Wu R., Lin M., Liang Y., Liu J., Wang X., Yang B, & Feng Z. (2015). RRAD inhibits the Warburg effect through negative regulation of the NF-κB signaling. Oncotarget, 6(17), 14982-14992.

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Isolation and Quantification of Amyloid-β Peptides

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Stable isotopically-labeled (SIL) human Aβ1-38 (¹³C-labeled at Phe and Ile) and Aβ1-40 (¹³C, ¹⁵N-labeled at Arg and Lys) were used for internal standards. They were purchased from AnaSpec (San Jose, CA). The lyophilized stocks of SIL-Aβ1-38 and SIL-Aβ1-40 were dissolved in 50 mM NaOH and subsequently applied to a COSMOSIL(R) 5Diol-120-II [7.5 mm I.D. × 600 mm] column (Nacalai Tesque, Kyoto) attached to a Prominence HPLC System (Shimadzu Corp., Kyoto, Japan). Mobile phase, flow rate, column temperature, and detection wavelength were as follows: 40 mM Tris-HCl, pH 8.0, one mL/min, 25 ℃, and 214/280 nm, respectively. Portions of the fractions were analyzed using 15–20% Tricine-SDS-PAGE under non-reducing conditions. Peptides were visualized using a silver staining kit (Invitrogen, Carlsbad, CA). The eluates were collected in fractions with bands corresponding to the molecular weight of monomers and were diluted with 40 mM Tris-HCl, 150 mM NaCl, pH 8.0 containing one mg/mL bovine serum albumin. Monomeric SIL-Aβ1-38 and SIL-Aβ1-40 were dispensed in tubes and stored at −80 ℃.

KANEKO N., YAMAMOTO R., SATO T.A, & TANAKA K. (2014). Identification and quantification of amyloid beta-related peptides in human plasma using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Proceedings of the Japan Academy. Series B, Physical and Biological Sciences, 90(3), 104-117.

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Analytical-SEC Protein Fractionation and Visualization

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Eluted fractions following analytical-SEC were further examined by SDS–PAGE (12% gels) (Bio-rad, California, U.S.A.) and bands were visualised using a Silver staining kit (Invitrogen, California, U.S.A.) for analytical-SEC fraction analysis and Coomassie Brilliant Blue stain (ThermoFisher, Massachusetts, U.S.A.) for band density analysis. Both techniques were performed according to the manufacturer's instructions. Band densities were calculated using GelAnalyzer 9.1 (http://www.gelanalyzer.com/).

Sanders H.M., Jovcevski B., Carver J.A, & Pukala T.L. (2020). The molecular chaperone β-casein prevents amorphous and fibrillar aggregation of α-lactalbumin by stabilisation of dynamic disorder. Biochemical Journal, 477(3), 629-643.

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Identifying Mutp53 Interactors in Mouse Tissues

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To determine mutp53 binding partners in mouse tissues, mouse mutp53 protein complexes were purified from lysates from tumor and normal tissues of mutp53^R172H/R172H mice by IP using anti-p53 (FL393) beads and eluted with 0.1 M Glycine solution. Eluted materials were separated in a 4–15% Tris SDS gel and visualized by silver staining using the silver staining kit (Invitrogen, Grand Island, NY) and coomassie blue staining. Coomassie blue-stained protein bands were excised from the gel and subsequently analyzed by LC-MS/MS at the Biological MS facility of Rutgers University.
IP assays were performed as previously described (Zheng et al., 2013 (link)). In brief, 1 mg cell or tissue lysates in NP-40 buffer were used for IP using anti-p53 (DO-1 for human cells and FL393 for mouse tissues, Santa Cruz, Dallas, Texas), anti-HA and anti-Flag antibodies to pull down mutp53, BAG2-HA and BAG2-Flag protein, respectively.

Yue X., Zhao Y., Liu J., Zhang C., Yu H., Wang J., Zheng T., Liu L., Li J., Feng Z, & Hu W. (2015). BAG2 promotes tumorigenesis through enhancing mutant p53 protein levels and function. eLife, 4, e08401.

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Protein Extraction and Characterization

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Preparation of cell lysates, measurement of protein concentration and western blotting analysis were recently described.^{12 (link)} Cell membrane, cytosol fractions or cell lysates minus cell membrane were prepared using the Mem-PER Eukaryotic Membrane Protein Extraction Reagent Kit (Thermo Scientific, Waltham, MA, USA). Cell culture medium was concentrated 20-fold using Centricon (Millipore, Billerica, MA, USA) before analysis. In experiments measuring the binding of PEPD or NRG-1 to ErbB2 ECD, ErbB3 ECD or ErbB4 ECD, a silver staining kit (Invitrogen) was used to display the proteins after gel electrophoresis. To detect ErbB2 receptor dimerization, PEPD-treated cells and control cells were washed with ice-cold PBS and incubated with cross linker BS3 (Pierce, Rockford, IL, USA) at 2 mM for 30 min at room temperature. The cross-linking reaction was terminated by adding 50 mM Tris (final, pH7.5), followed by incubation at room temperature for 15 min. Cell lysates were analyzed by western blotting (3.5% SDS-PAGE).

Yang L., Li Y, & Zhang Y. (2014). Identification of prolidase as a high affinity ligand of the ErbB2 receptor and its regulation of ErbB2 signaling and cell growth. Cell Death & Disease, 5(5), e1211-.

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