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Cited by 315

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Membrane molecules mobile even after chemical fixation

Tanaka, Kenji A K, Suzuki, Kenichi G N, Shirai, Yuki M, Shibutani, Shusaku T, Miyahara, Manami S H, Tsuboi, Hisae, Yahara, Miyako, Yoshimura, Akihiko, Mayor, Satyajit, Fujiwara, Takahiro K, Kusumi, Akihiro·2010·Nature Methods
DOI 10.1038/nmeth.f.314
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Abstract

Lyn, H-ras, Cbp and TfR (we observed ~70% immobilization of GPI-anchored proteins, on average, depending strongly on the protein; Fig. 1b and Supplementary Figs. 3–5). Increasing glutaraldehyde concentration to 0.2% or methanol (100%) fixation resulted in immobilization of >80% GPI-anchored proteins but not of phospholipids or cholesterol. We then investigated antibody-induced clustering under different fixation conditions by measuring the fluorescence intensities of individual spots (Supplementary Fig. 6). Whereas treatment with 4% paraformaldehyde with or without 0.1% glutaraldehyde did not itself induce clustering, paraformaldehyde treatment did not block antibody-induced clustering of Halo-GPI and Halo–H-ras. Including 0.1% glutaraldehyde in addition to 4% paraformaldehyde suppressed clustering but did not entirely inhibit it. These results indicate that, in interpreting immunolocalization data, antibody-induced clustering Membrane molecules mobile even after chemical fixation

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Authors
Tanaka, K. A. K., Suzuki, K. G. N., Shirai, Y. M., Shibutani, S. T., Miyahara, M. S. H., Tsuboi, H., Yahara, M., Yoshimura, A., Mayor, S., Fujiwara, T. K., & Kusumi, A.
Venue
Nature Methods
Publisher
Springer Science and Business Media LLC
Published
2010-10-03
Volume
7
Issue
11
Pages
865-866
ISSN
  • 1548-7091 (ISSN-L)
  • 1548-7105
DOI
10.1038/nmeth.f.314
OpenAlex
W2062409614
Cited by
315
References
0
FWCI
4.61
Type
journal article
Language
en
Open access
closed

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