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Gelcode blue staining

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GelCode Blue staining is a laboratory product used for the detection and visualization of proteins in polyacrylamide gels. It is a ready-to-use, stable, and sensitive protein stain that provides a simple and reliable method for staining proteins.

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Lab products found in correlation

Nanoacquity hplc system, by Waters Corporation (2 mentions) Q exactive, by Thermo Fisher Scientific (2 mentions) Mascot server, by Matrix Science (2 mentions) Bca protein assay, by Thermo Fisher Scientific (2 mentions) Geneart, by Thermo Fisher Scientific (1 mentions) Ni nta resin, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

GelCode Blue (66 citations) GelCode (6 citations) GelCode Blue Staining Reagent (5 citations)

4 protocols using gelcode blue staining

1

Production and Purification of scFvs

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ScFvs based on LINGO1-specific monoclonal antibodies Li62 and Li81 synthesized by GeneArt (Thermo Fisher) and cloned into pSANG10. ScFvs were expressed overnight in 25 mL MagicMedia E. coli autoexpression medium (Thermo-Fisher). Periplasmic extracts were generated from autoinduction cultures as previously described (57 (link)). ScFvs were purified by immobilized metal affinity chromatography using NiNTA resin (Thermo-Fisher). Concentrations of purified scFvs were determined by bicinchoninic acid (BCA) protein assay (Thermo-Fisher). Purity of scFvs was confirmed by SDS-PAGE and GelCode™ Blue staining (Thermo Fisher).
Morales E.A., Dietze K.A., Baker J.M., Wang A., Avila S.V., Iglesias F., Radhakrishnan S.V., Mause E.V., Olson M.L., Sun W., Rosati E., Chidester S.L., Iraguha T., Fan X., Atanackovic D, & Luetkens T. (2024). Restricting CAR T Cell Trafficking Expands Targetable Antigen Space. bioRxiv.
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2

Immunoprecipitation and Mass Spectrometry

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Immunoprecipitation was set up with 20 mg membrane extract and 50 µg of syngeneic or allogeneic IgG coupled to protein G magnetic beads and incubated for 16 hr at 4°C. Beads were washed thrice with MEB and bound protein complexes were eluted with 2X Laemmli buffer. The eluted sample was subjected to SDS-PAGE on a 4–12% Bis-Tris gel followed by GelCode Blue staining (Thermo Scientific) to visualize protein bands. Protein bands were excised, digested with trypsin and analyzed (MS Bioworks) using a nano LC/MS/MS with a NanoAcquity HPLC system (Waters) interfaced to a Q Exactive (Thermo Fisher). The mass spectrometer was operated in data-dependent mode, with MS and MS/MS performed in the Orbitrap at 70,000 FWHM and 17,500 FWHM resolution, respectively. The fifteen most abundant ions were selected for MS/MS. The data were processed with the Mascot Server (Matrix Science). Mascot DAT files were parsed into the Scaffold software for validation, filtering and to create a non-redundant list per sample. Data were filtered at 1% protein and peptide FDR, requiring at least two unique peptides per protein. Mass spectrometry analysis of precipitated proteins was performed once.
Carmi Y., Spitzer M.H., Linde I.L., Burt B.M., Prestwood T.R., Perlman N., Davidson M.G., Kenkel J.A., Segal E., Pusapati G.V., Bhattacharya N, & Engleman E.G. (2015). Allogeneic IgG combined with dendritic cell stimuli induces anti-tumor T cell immunity. Nature, 521(7550), 99-104.
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3

Recombinant Fusion Protein Design

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Recombinant fusion proteins were designed starting from the sequence of MvDN30_long-sc60 [20 ] and decoyMETK842E [17 ], joining the two moieties by an amino acid sequence (linker). DecAb fusion proteins were obtained connecting the IPT4 domain of decoyMETK842E to the variable domain of the light chain of MvDN30_long-sc60. AbDec fusion proteins were generated linking the constant domain of the heavy chain of the antibody fragment to the α-chain of the SEMA domain of decoyMETK842E. At the C-terminus of each molecule, a triple Strep-tag (GAAWSHPQPEK) and a poly-histidine tag (HHHHHH) were added for protein purification and detection. cDNA synthesis, protein expression, and purification were performed by U-Protein Express BV (Utrecht, The Netherlands). Purified products were analyzed by SDS-PAGE followed by Gel Code Blue staining (Thermo Fisher Scientific, Waltham, MA, USA).
Modica C., Basilico C., Chiriaco C., Borrelli N., Comoglio P.M, & Vigna E. (2021). A receptor-antibody hybrid hampering MET-driven metastatic spread. Journal of Experimental & Clinical Cancer Research : CR, 40, 32.
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4

Immunoprecipitation and Mass Spectrometry

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Immunoprecipitation was set up with 20 mg membrane extract and 50 µg of syngeneic or allogeneic IgG coupled to protein G magnetic beads and incubated for 16 hr at 4°C. Beads were washed thrice with MEB and bound protein complexes were eluted with 2X Laemmli buffer. The eluted sample was subjected to SDS-PAGE on a 4–12% Bis-Tris gel followed by GelCode Blue staining (Thermo Scientific) to visualize protein bands. Protein bands were excised, digested with trypsin and analyzed (MS Bioworks) using a nano LC/MS/MS with a NanoAcquity HPLC system (Waters) interfaced to a Q Exactive (Thermo Fisher). The mass spectrometer was operated in data-dependent mode, with MS and MS/MS performed in the Orbitrap at 70,000 FWHM and 17,500 FWHM resolution, respectively. The fifteen most abundant ions were selected for MS/MS. The data were processed with the Mascot Server (Matrix Science). Mascot DAT files were parsed into the Scaffold software for validation, filtering and to create a non-redundant list per sample. Data were filtered at 1% protein and peptide FDR, requiring at least two unique peptides per protein. Mass spectrometry analysis of precipitated proteins was performed once.
Carmi Y., Spitzer M.H., Linde I.L., Burt B.M., Prestwood T.R., Perlman N., Davidson M.G., Kenkel J.A., Segal E., Pusapati G.V., Bhattacharya N, & Engleman E.G. (2015). Allogeneic IgG combined with dendritic cell stimuli induces anti-tumor T cell immunity. Nature, 521(7550), 99-104.
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