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1.4 nm Nanogold® Labeling Reagents
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Monomaleimido-Nanogold®

  1. E Biocentre, E Tartu. The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake. The FASEB Journal, vol. 23 no. 1 214-223.

    2. Monomaleimido Nanogold® is used to track the activity of a cell-penetrating peptide during uptake.

  2. Ackerly, C. A.; Tilups, A., and Becker, L. E.: Strategies insuring the optimal use of IgG or Fab' fragments covalently bound to 1.4 nm Nanogold® in immunogold labeling procedures. Proc. 56th Ann. Mtg., Micros. Soc. Amer.; Bailey, G. W.; Alexander, K. B.; Jerome, W. G.; Bond, M. G., and McCarthy, J. J., Eds.; Springer, New York, NY, 1998, 988-989.
  3. Hainfeld, J. F., and Powell, R. D.: New frontiers in gold labeling J. Histochem. Cytochem., 48, 471-480 (2000).
  4. Jeon, H., and Shipley, G. G. Localization of the N-Terminal Domain of the Low Density Lipoprotein Receptor. J. Biol. Chem.,, 275, 30465-30470 (2000).
  5. Jeon, H., and Shipley, G. G. Vesicle-Reconstituted Low Density Lipoprotein Receptor: Visualization by Cryoelectron Microscopy. J. Biol. Chem., 275, 30458-30464 (2000).
  6. Mahdi, F.; Madar, Z. S.; Figueroa, C. D., and Schmaier, A. H.: Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin 1 on endothelial cell membranes. Blood, 99, 3585-3596 (2002).
  7. Malecki, M.; Hsu, A.; Truong, L., and Sanchez, S: Molecular immunolabeling with recombinant single-chain variable fragment (scFv) antibodies designed with metal-binding domains; Proc. Natl. Acad. Sci. USA, 99, 213-218 (2002).
  8. Medalia, O.; Heim, M.; Guckenberger, R.; Sperling, R., and Sperling, J.: Gold-tagged RNA-A probe for macromolecular assemblies. J. Struct. Biol., 127, 113-119 (1999).
  9. Montesano-Roditis, L.; Glitz, D. G.; Traut, R. R., and Stewart, P. L.: Cryo-electron microscopic localization of protein L7/L12 within the Escherichia coli 70S ribosome by difference mapping and Nanogold labeling. J. Biol. Chem., e-publication ahead of print.
  10. Qualmann, B.; Kessels, M. M.; Thole, H. H., and Sierralta, W. D.; A hormone pulse induces transient changes in the subcellular distribution and leads to a lysosomal accumulation of the estradiol receptor alpha in target tissues. Eur. J. Cell Biol., 79, 383-93 (2000).
  11. Robinson, J. M.; Takizawa, T.; Vandré, D. D., and Burry, R. W.: Ultrasmall immunogold particles: important probes for immunocytochemistry; Microsc. Res. Tech., 42, 13-23 (1998).
  12. Scheibel, T.; Kowal, A. S.; Bloom, J. D., and Lindquist, S.L.: Bidirectional amyloid fiber growth for a yeast prion determinant. Current Biology, 11, 366-369 (2001).
  13. Schwartz, M. P., and Matouschek, A.: The dimensions of the protein import channels in the outer and inner mitochondrial membranes. Proc. Natl. Acad. Sci. USA, 96, 13086-13090 (1999).
  14. Tolstonog, G. V.; Sabasch, M., and Traub, P.: Cytoplasmic Intermediate Filaments Are Stably Associated with Nuclear Matrices and Potentially Modulate Their DNA-Binding Function. DNA Cell Biol., 21, 213-39 (2002).
  15. Traxler, K. W.; Norcum, M. T.; Hainfeld, J. F., and Carlson, G. M.: Direct Visualization of the Calmodulin Subunit of Phosphorylase Kinase via Electron Microscopy Following Subunit Exchange. J. Struct. Biol., 135, 231-8 (2001).
  16. Woldin, C. N.; Hing, F. S.; Lee, J.; Pilch, P. F., and Shipley, G. G.: Structural studies of the detergent-solubilized and vesicle-reconstituted insulin receptor J. Biol. Chem, 274, 34981-34992 (1999).
  17. Alivisatos, A. P., Johnsson, K. P., Peng, X., Wilson, T. E., Loweth, C. J., Bruchez, M. P., Jr., and Schultz, P. G.: Organization of 'Nanocrystal Molecules' using DNA. Nature, 382, 609 (1996).
  18. Boisset, N., Penczek, P., Pochon, F., Frank, J., and Lamy, J. Three-dimensional reconstruction of human alpha 2-macroglbulin and refinement of the localization of thiol ester bonds with monomaleimido Nanogold;. Ann. NY Acad. Sci., 737, 229-44 (1994).
  19. Boisset, N., Grassucci, R., Penczek, P., Delain, E., Pochon, F., Frank, J., and Lamy, J.N. Three-dimensional reconstruction of a complex of human alpha-2-macroglobulin with monomaleimido Nanogold; (Au1.4nm) embedded in ice. J. Struct. Biol., 109;39-45 (1992).
  20. Gregori, L., Hainfeld, J. F., Simon, M. N., and Goldgaber, D. Binding of amyloid beta protein to the 20S proteasome. J. Biol. Chem., 272, 58-62 (1997).
  21. Hainfeld, J. F.: Labeling with Nanogold and undecagold: techniques and results. Scanning Microsc. Suppl. (Proc. 14th Pfefferkorn Conf.); Malecki, M., and Roomans, G. M. (Eds.). Scanning Microscopy International, Chicago, IL, 10, 309-322 (1996).
  22. Hainfeld, J. F., and Powell, R. D.: Nanogold Technology: New Frontiers in Gold Labeling. Cell Vision, 4, 408-432 (1997).
  23. Lin, M., Sistina, Y., and Rodger, J. C.: Electron-microscopic localisation of thiol and disulphide groups by direct monomaleimido-nanogold labeling in the spermatozoa of a marsupial, the tammar wallaby (Macropus eugenii); Cell Tisue Res., 282, 291-296 (1995).
  24. Malecki, M.: Energy filtering transmission electron microscopy of transfected DNA; In Proc 54th Ann. Mtg. Micros. Soc. Amer., G. W. Bailey, J. M. Corbett, R. V. W. Dimlich, J. R. Michael and N. J., Zaluzec (Eds.). San Francisco Press, San Francisco, CA, pp. 924-925 (1996).
  25. Rayner, S. L., and Stephenson, F. A. Labelling and characterization of gamma-aminobutyric acidA receptor subunit-specific antibodies with monomaleimido-Nanogold. Biochem. Soc. Trans., 25, 546S (1997).
  26. Spin, J. M., and Atkinson, D.: Cryoelectron microscopy of low density lipoprotein in vitreous ice. Biophys. J., 68, 2115-2123 (1995).
  27. Wagenknecht, T,; Berkowitz, J.; Grassucci, R.; Timerman, A. P., and Fleischer, S.: Localization of calmodulin binding sites on the ryanodine receptor from skeletal muscle by electron microscopy. Biophys. J., 67, 2286-2295 (1994).
  28. Wenzel, T., and Baumeister, W.: Conformational restraints in protein degradation by the 20S proteasome. Nature Struct. Biol., 2, 199-204 (1995).
  29. Wilkens, S. and Capaldi, R.A. Monomaleimidogold Labeling of the g subunit of the E. coli F1 ATPase examined by cryoelectron Microscopy. Arch Biochem. Biophys., 229, 105-109 (1992).
  30. Yanase, K.; Smith, R. M.; Cizman, B.; Foster, M. H.; Peachey, L. D.; Jarrett, L., and Madaio, M. P.: A subgroup of Murine monoclonal anti-deoxyribonucleic acid antibodies traverse the cytoplasm and enter the nucleus in a time- and temperature- dependent manner; Laboratory Investigation, 71, 52-60 (1994).
  31. Yang, Y. S.; Datta, A.; Hainfeld, J. F.; Furuya, F. R.; Wall, J. S., and Frey, P. A.: Mapping the lipoyl groups of the pyruvate dehydrogenase complex by use of gold cluster labels and scanning transmission electron microscopy. Biochemistry, 16;33(32), 9428-9437 (1994).

 

Nanogold® Labeling Reagents: Catalog Information | Technical Help | Product Instructions

 

Mono-Sulfo-NHS-Nanogold®

  1. Hainfeld, J. F.: Labeling with Nanogold and undecagold: techniques and results. Scanning Microsc. Suppl. (Proc. 14th Pfefferkorn Conf.); Malecki, M., and Roomans, G. M. (Eds.). Scanning Microscopy International, Chicago, IL, 10, 309-322 (1996).
  2. Hainfeld, J. F., and Powell, R. D.: New frontiers in gold labeling J. Histochem. Cytochem., 48, 471-480 (2000).
  3. Hainfeld, J. F., and Powell, R. D.: Nanogold Technology: New Frontiers in Gold Labeling. Cell Vision, 4, 408-432 (1997).
  4. Hamad-Schifferli, K.; Schwartz, J. J.; Santos, A. T.; Zhang, S., and Jacobson, J. M.: Remote electronic control of DNA hybridization through inductive coupling to an attached metal nanocrystal antenna. Nature, 2002, 415, 152-155.
  5. Luo, R. Z.-T.; Beniac, D. R.; Fernandes, A.; Yip, C. C., and Ottensmeyer, F. P.: Quaternary structure of the insulin-insulin receptor complex. Science, 285, 1077-1080 (1999).
  6. Ottensmeyer, F. P.; Luo, R. Z.-T.; Fernandes, A. B.; Beniac, D., and Yip, C. C.: Insulin receptor: 3D reconstruction from darkfield STEM images, structural interpretation and functional model; Proc. 57th Ann. Mtg., Micros. Soc. Amer.; G. W. Bailey, W. G. Jerome, S. McKernan, J. F. Mansfield, and R. L. Price (Eds.); Springer-Verlag, New York, NY; 1999, 408-409.
  7. Segond von Banchet, G., Schindler, M., Hervieu, G. J.; Beckmann, B., Emson, P. C., and Heppelmann, B.: Distribution of somatostain receptor subtypes in rat lumbar spinal cord examined with gold-labelled somatostatin and anti-receptor antibodies; Brain Res., 816, 254 (1999).
  8. Ribrioux, S., Kleymann, G., Haase, W., Heitmann, K., Ostermeier, C., and Michel, H. Use of Nanogold- and Fluorescent-labeled Antibody Fv Fragments in Immunocytochemistry. J. Histochem. Cytochem., 44, 207-213 (1996).
  9. Segond von Banchet, G., and Heppelman, B.: Non-radioactive localization of substance P binding sites in rat brain and spinal cord using peptides labeled with 1.4 nm gold particles; J. Histochem. Cytochem., 43, 821 (1995).

 

Nanogold® Labeling Reagents: Catalog Information | Technical Help | Product Instructions

 

Monoamino-Nanogold®

  1. Wille, H.; Michelitsch, M. D.; Guenebaut, V.; Supattapone, S.; Serban, A.; Cohen, F. E.; Agard, D. A, and Prusiner, S. B.: Structural studies of the scrapie prion protein by electron crystallography. Proc. Natl. Acad. Sci. USA, 99, 3563-8 (2002).
  2. Shah, N., Zhang, S., Harada, S., Smith, R. M., and Jarrett, L.: Electron microscopic visualization of insulin translocation into the cytoplasm and nuclei of intact H35 hepatoma cells using covalently linked Nanogold-insulin. Endocrinology, 136, 2825-2835 (1995).

 

Nanogold® Labeling Reagents: Catalog Information | Technical Help | Product Instructions

 

Positively Charged Nanogold®

  1. Seron, K., Tieaho, V., Prescianotto-Baschong, C., Aust, T., Blondel, M. O., Guillard, P., Devilliers, G., Rossanese, O. W., Glick, B. S., Riezman, H., Keranen, S., and Haguenauer-Tapis, R.: A yeast t-SNARE involved in endocytosis; Mol. Biol. Cell, 9, 2873 (1998).
  2. Prescianotto-Baschong, C., and Riezman, H.: Morphology of the yeast endocytic pathway. Mol. Cell Biol., 9, 173-189 (1998).

 

Nanogold® Labeling Reagents: Catalog Information | Technical Help | Product Instructions

 

Negatively Charged Nanogold®

  1. Akaki, M.; Nagayasu, E.; Nakano, Y., and Aikawa, M.: Surface charge of Plasmodium falciparum merozoites as revealed by atomic force microscopy with surface potential spectroscopy. Parasitol. Res., 88, 16-20 (2002).

 

Nanogold® Labeling Reagents: Catalog Information | Technical Help | Product Instructions

 

Nanogold® Enzyme Substrates

  1. Mayer, G.; Leone. R. D.; Hainfeld, J. F., and Bendayan, M.: Introduction of a novel HRP substrate-Nanogold probe for signal amplification in immunocytochemistry J. Histochem. Cytochem., 48, 461-469 (2000).

 

Nanogold® Labeling Reagents: Catalog Information | Technical Help | Product Instructions

 

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