Publication

Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots

Giepmans, B. N. G., Deerinck, T. J., Smarr, B. L., Jones, Y. Z. & Ellisman, M. H., 22-Sep-2005, In : Nature Methods. 2, 10, p. 743-9 7 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Giepmans, B. N. G., Deerinck, T. J., Smarr, B. L., Jones, Y. Z., & Ellisman, M. H. (2005). Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots. Nature Methods, 2(10), 743-9. https://doi.org/10.1038/nmeth791

Author

Giepmans, Ben N G ; Deerinck, Thomas J ; Smarr, Benjamin L ; Jones, Ying Z ; Ellisman, Mark H. / Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots. In: Nature Methods. 2005 ; Vol. 2, No. 10. pp. 743-9.

Harvard

Giepmans, BNG, Deerinck, TJ, Smarr, BL, Jones, YZ & Ellisman, MH 2005, 'Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots', Nature Methods, vol. 2, no. 10, pp. 743-9. https://doi.org/10.1038/nmeth791

Standard

Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots. / Giepmans, Ben N G; Deerinck, Thomas J; Smarr, Benjamin L; Jones, Ying Z; Ellisman, Mark H.

In: Nature Methods, Vol. 2, No. 10, 22.09.2005, p. 743-9.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Giepmans BNG, Deerinck TJ, Smarr BL, Jones YZ, Ellisman MH. Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots. Nature Methods. 2005 Sep 22;2(10):743-9. https://doi.org/10.1038/nmeth791


BibTeX

@article{95266a4bc3f844e188faa3f13e7fa32e,
title = "Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots",
abstract = "The importance of locating proteins in their context within cells has been heightened recently by the accomplishments in molecular structure and systems biology. Although light microscopy (LM) has been extensively used for mapping protein localization, many studies require the additional resolution of the electron microscope. Here we report the application of small nanocrystals (Quantum dots; QDs) to specifically and efficiently label multiple distinct endogenous proteins. QDs are both fluorescent and electron dense, facilitating their use for correlated microscopic analysis. Furthermore, QDs can be discriminated optically by their emission wavelength and physically by size, making them invaluable for multilabeling analysis. We developed pre-embedding labeling criteria using QDs that allows optimization at the light level, before continuing with electron microscopy (EM). We provide examples of double and triple immunolabeling using light, electron and correlated microscopy in rat cells and mouse tissue. We conclude that QDs aid precise high-throughput determination of protein distribution.",
keywords = "Animals, Cells, Cultured, Mice, Microscopy, Microscopy, Electron, Proteins, Quantum Dots, Rats, Tissue Distribution",
author = "Giepmans, {Ben N G} and Deerinck, {Thomas J} and Smarr, {Benjamin L} and Jones, {Ying Z} and Ellisman, {Mark H}",
year = "2005",
month = "9",
day = "22",
doi = "10.1038/nmeth791",
language = "English",
volume = "2",
pages = "743--9",
journal = "Nature Methods",
issn = "1548-7105",
publisher = "Nature Publishing Group",
number = "10",

}

RIS

TY - JOUR

T1 - Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots

AU - Giepmans, Ben N G

AU - Deerinck, Thomas J

AU - Smarr, Benjamin L

AU - Jones, Ying Z

AU - Ellisman, Mark H

PY - 2005/9/22

Y1 - 2005/9/22

N2 - The importance of locating proteins in their context within cells has been heightened recently by the accomplishments in molecular structure and systems biology. Although light microscopy (LM) has been extensively used for mapping protein localization, many studies require the additional resolution of the electron microscope. Here we report the application of small nanocrystals (Quantum dots; QDs) to specifically and efficiently label multiple distinct endogenous proteins. QDs are both fluorescent and electron dense, facilitating their use for correlated microscopic analysis. Furthermore, QDs can be discriminated optically by their emission wavelength and physically by size, making them invaluable for multilabeling analysis. We developed pre-embedding labeling criteria using QDs that allows optimization at the light level, before continuing with electron microscopy (EM). We provide examples of double and triple immunolabeling using light, electron and correlated microscopy in rat cells and mouse tissue. We conclude that QDs aid precise high-throughput determination of protein distribution.

AB - The importance of locating proteins in their context within cells has been heightened recently by the accomplishments in molecular structure and systems biology. Although light microscopy (LM) has been extensively used for mapping protein localization, many studies require the additional resolution of the electron microscope. Here we report the application of small nanocrystals (Quantum dots; QDs) to specifically and efficiently label multiple distinct endogenous proteins. QDs are both fluorescent and electron dense, facilitating their use for correlated microscopic analysis. Furthermore, QDs can be discriminated optically by their emission wavelength and physically by size, making them invaluable for multilabeling analysis. We developed pre-embedding labeling criteria using QDs that allows optimization at the light level, before continuing with electron microscopy (EM). We provide examples of double and triple immunolabeling using light, electron and correlated microscopy in rat cells and mouse tissue. We conclude that QDs aid precise high-throughput determination of protein distribution.

KW - Animals

KW - Cells, Cultured

KW - Mice

KW - Microscopy

KW - Microscopy, Electron

KW - Proteins

KW - Quantum Dots

KW - Rats

KW - Tissue Distribution

U2 - 10.1038/nmeth791

DO - 10.1038/nmeth791

M3 - Article

C2 - 16179920

VL - 2

SP - 743

EP - 749

JO - Nature Methods

JF - Nature Methods

SN - 1548-7105

IS - 10

ER -

ID: 13998007