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fluorescent hilyte 647 tubulin  (Cytoskeleton Inc)


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    Cytoskeleton Inc fluorescent hilyte 647 tubulin
    Fluorescent Hilyte 647 Tubulin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 113 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hilyte+647+tubulin+protein/Tubulin+protein+-+fluorescent+HiLyte+647+porcine+brain/pm41989917-284-29-33
    Average 95 stars, based on 113 article reviews
    fluorescent hilyte 647 tubulin - by Bioz Stars, 2026-10
    95/100 stars

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    Related Articles

    Injection:

    Article Title: Spatiotemporal organization of dynein in bulk cytoplasm promotes aster growth and positioning in large embryos
    Article Snippet: .. To visualize MTs simultaneously with green and red fluorescent proteins in early embryos, HiLyte 647-tubulin protein (Cytoskeleton, Inc. TL670M) was injected. ..



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    Representative movie from MD simulations showing interactions of the Y-αCTT with the tubulin body over 240 ns. The tubulin body is shown in cartoon and colored gray. The αCTT is shown in stick and colored yellow with the glutamate side chains in red. Residues in site 1 (green), site 2 (cyan), and site 3 (magenta) appear as spheres when the αCTT is forming salt bridges with those residues.
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    Representative movie from MD simulations showing interactions of the Y-αCTT with the tubulin body over 240 ns. The tubulin body is shown in cartoon and colored gray. The αCTT is shown in stick and colored yellow with the glutamate side chains in red. Residues in site 1 (green), site 2 (cyan), and site 3 (magenta) appear as spheres when the αCTT is forming salt bridges with those residues.
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    Representative movie from MD simulations showing interactions of the Y-αCTT with the tubulin body over 240 ns. The tubulin body is shown in cartoon and colored gray. The αCTT is shown in stick and colored yellow with the glutamate side chains in red. Residues in site 1 (green), site 2 (cyan), and site 3 (magenta) appear as spheres when the αCTT is forming salt bridges with those residues.

    Journal: eLife

    Article Title: Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation

    doi: 10.7554/eLife.109308

    Figure Lengend Snippet: Representative movie from MD simulations showing interactions of the Y-αCTT with the tubulin body over 240 ns. The tubulin body is shown in cartoon and colored gray. The αCTT is shown in stick and colored yellow with the glutamate side chains in red. Residues in site 1 (green), site 2 (cyan), and site 3 (magenta) appear as spheres when the αCTT is forming salt bridges with those residues.

    Article Snippet: Peptide, recombinant protein , HiLyte647 porcine brain tubulin , Cytoskeleton , Cat# TL670M , .

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