MarkerGene™ Hydrophobic Protein Analysis Kit

Product ID: M0794

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  • Buy 5 for $224.91 each and save 20%

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This kit allows fast and easy measurement of hydrophobic proteins in complex mixtures using either solution analysis or 1D- or 2D-SDS-PAGE analysis. Both denatured or native conformations of proteins isolated from cell preparations can be analyzed.

The isolation of hydrophobic membrane proteins can result in complex protein mixtures that are difficult to purify, identify, and quantitate by bioinformatics. Utilizing 2D gel electrophoresis analysis, individual bands can typically be isolated but may contain multiple protein samples or a variety of functional components. This kit uses the environment-sensitive fluorescent probe 6-p-Toluidino-2-naphthalenesulfonic acid(TNS) M0704. TNS is practically non-fluorescent in water or buffer solutions, but exhibits a strong fluorescence enhancement when bound to hydrophobic regions of proteins. By incorporating the TNS dye in standard gel-electrophoresis procedures, hydrophobic proteins (typically from membranes) become fluorescent. The kit contains enough reagents and buffers for numerous assays and control experiments, and also contains reference standards and a detailed protocol for use. See the references below for more information and applications. NOTE: Marker Gene also sells the more water soluble potassium salt of TNS M0720.

Technical Data
SKU M0794
Unit Size 1kit

References and Citations


  • Schneider A, Aghamirzaie D, Elmarakeby H, Poudel AN, Koo AJ, Heath LS, Grene R, Collakova E.(2015) "Potential targets of VIVIPAROUS1/ABI3-LIKE1 (VAL1) repression in developing Arabidopsis thaliana embryos." Plant J.
  • Capito F, Kolmar H, Edelmann B, Skudas R.(2014) "Feasibility of polyelectrolyte-driven Fab fragment separation." Biotechnol J. 9(5):698-701.
  • Collakova E, Aghamirzaie D, Fang Y, Klumas C, Tabataba F, Kakumanu A, Myers E, Heath LS, Grene R. (2013) "Metabolic and Transcriptional Reprogramming in Developing Soybean (Glycine max) Embryos." Metabolites. 3(2):347-72.
  • Capito F, Skudas R, Stanislawski B, Kolmar H.(2012) "Customization of copolymers to optimize selectivity and yield in polymer-driven antibody purification processes." Biotechnol Prog. 29(6):1484-93.
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  • Neff TL, Naleway JJ. (2003) "Development of a sensitive proteomic hydrophobicity assay based on 2-p-toluidinylnapthalene-6-sulfonic acid (TNS) as the protein-detecting reagent." Anal Biochem (submitted for publication).
  • Batlle N, Carbonell JV, Sendra JM. (2000) "Determination of depolymerization kinetics of amylose, amylopectin, and soluble starch by aspergillus oryzae alpha-amylase using a fluorimetric 2-p-toluidinylnaphthalene-6-sulfonate/flow-injection analysis system." Biotechnol Bioeng 70:544-552.
  • QaDan M, Spyres LM, Ballard JD. (2000)"pH-Induced conformational changes in Clostridium difficile toxin B." Infect Immun68:2470-2474.
  • Jones M, Keenan, RW, Horowitz P. (1982) "Use of 6-p-toluidino-2-naphthalenesulfonic acid to quantitate lipids after thin-layer chromatography." J Chromatogr 237:522.
  • McClure, WO, Edelman GM. (1966)"Fluorescent probes for conformational states of proteins. I. Mechanism of fluorescence of 2-p-toluidinylnaphthalene-6-sulfonate, a hydrophobic probe" Biochemistry 5(6):1908-1919.
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