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tubulin protein  (Cytoskeleton Inc)


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    Structured Review

    Cytoskeleton Inc tubulin protein
    Representative lowest energy docking poses of (a) cis -PST-1, (b) trans -PST-1, (c) cis -proPST-1, and (d) trans -proPST-1 within the colchicine binding pocket of <t>tubulin</t> (PDB ID: 5LYJ). Ligands are represented as orange sticks, while interacting amino acid residues are shown as yellow sticks and labelled using single-letter amino acid notation. Hydrogen-bonding and hydrophobic interactions are indicated by red and blue dashed lines, respectively, with corresponding interaction distances (Å) shown. Structures and interaction maps were generated using PyMOL v3.0.
    Tubulin Protein, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 94/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/brain+mapping/Tubulin+protein+MAP+rich+porcine+brain/pmc13673699-47-6-36
    Average 94 stars, based on 36 article reviews
    tubulin protein - by Bioz Stars, 2026-11
    94/100 stars

    Images

    1) Product Images from "Simultaneous activation and release of a microtubule inhibitor from amphiphilic polymeric nanoparticles"

    Article Title: Simultaneous activation and release of a microtubule inhibitor from amphiphilic polymeric nanoparticles

    Journal: Nanoscale Advances

    doi: 10.1039/d6na00763e

    Representative lowest energy docking poses of (a) cis -PST-1, (b) trans -PST-1, (c) cis -proPST-1, and (d) trans -proPST-1 within the colchicine binding pocket of tubulin (PDB ID: 5LYJ). Ligands are represented as orange sticks, while interacting amino acid residues are shown as yellow sticks and labelled using single-letter amino acid notation. Hydrogen-bonding and hydrophobic interactions are indicated by red and blue dashed lines, respectively, with corresponding interaction distances (Å) shown. Structures and interaction maps were generated using PyMOL v3.0.
    Figure Legend Snippet: Representative lowest energy docking poses of (a) cis -PST-1, (b) trans -PST-1, (c) cis -proPST-1, and (d) trans -proPST-1 within the colchicine binding pocket of tubulin (PDB ID: 5LYJ). Ligands are represented as orange sticks, while interacting amino acid residues are shown as yellow sticks and labelled using single-letter amino acid notation. Hydrogen-bonding and hydrophobic interactions are indicated by red and blue dashed lines, respectively, with corresponding interaction distances (Å) shown. Structures and interaction maps were generated using PyMOL v3.0.

    Techniques Used: Docking Assay, Binding Assay, Generated

    (a) Schematic representation of light-controlled inhibition of microtubule polymerisation by proPST-1-loaded polymer nanoparticles (proPST-1@PN). Under dark conditions, the encapsulated photocaged prodrug remains inactive, allowing normal microtubule formation. Upon 365 nm irradiation, photolytic uncaging and release of active cis -PST-1 suppress microtubule assembly. Created in BioRender. Singh, H. (2026) https://BioRender.com/fac5r0eT . (b) Tubulin polymerisation kinetics monitored by absorbance at 340 nm for control samples, empty polymer nanoparticles (PN control), and proPST-1@PN under dark and irradiated conditions. Irradiation of proPST-1@PN results in pronounced inhibition of tubulin polymerisation, whereas no inhibition is observed in the dark. (c) Fluorescence microscopy images of microtubule structures formed in the presence of control samples, proPST-1@PN under dark conditions, and irradiated proPST-1@PN. Normal microtubule growth and network formation are observed in control and dark conditions, while irradiation results in substantial disruption of microtubule assembly. Scale bars: 10 µm.
    Figure Legend Snippet: (a) Schematic representation of light-controlled inhibition of microtubule polymerisation by proPST-1-loaded polymer nanoparticles (proPST-1@PN). Under dark conditions, the encapsulated photocaged prodrug remains inactive, allowing normal microtubule formation. Upon 365 nm irradiation, photolytic uncaging and release of active cis -PST-1 suppress microtubule assembly. Created in BioRender. Singh, H. (2026) https://BioRender.com/fac5r0eT . (b) Tubulin polymerisation kinetics monitored by absorbance at 340 nm for control samples, empty polymer nanoparticles (PN control), and proPST-1@PN under dark and irradiated conditions. Irradiation of proPST-1@PN results in pronounced inhibition of tubulin polymerisation, whereas no inhibition is observed in the dark. (c) Fluorescence microscopy images of microtubule structures formed in the presence of control samples, proPST-1@PN under dark conditions, and irradiated proPST-1@PN. Normal microtubule growth and network formation are observed in control and dark conditions, while irradiation results in substantial disruption of microtubule assembly. Scale bars: 10 µm.

    Techniques Used: Inhibition, Polymer, Irradiation, Control, Fluorescence, Microscopy, Disruption



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    Representative lowest energy docking poses of (a) cis -PST-1, (b) trans -PST-1, (c) cis -proPST-1, and (d) trans -proPST-1 within the colchicine binding pocket of <t>tubulin</t> (PDB ID: 5LYJ). Ligands are represented as orange sticks, while interacting amino acid residues are shown as yellow sticks and labelled using single-letter amino acid notation. Hydrogen-bonding and hydrophobic interactions are indicated by red and blue dashed lines, respectively, with corresponding interaction distances (Å) shown. Structures and interaction maps were generated using PyMOL v3.0.
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    Image Search Results


    Representative lowest energy docking poses of (a) cis -PST-1, (b) trans -PST-1, (c) cis -proPST-1, and (d) trans -proPST-1 within the colchicine binding pocket of tubulin (PDB ID: 5LYJ). Ligands are represented as orange sticks, while interacting amino acid residues are shown as yellow sticks and labelled using single-letter amino acid notation. Hydrogen-bonding and hydrophobic interactions are indicated by red and blue dashed lines, respectively, with corresponding interaction distances (Å) shown. Structures and interaction maps were generated using PyMOL v3.0.

    Journal: Nanoscale Advances

    Article Title: Simultaneous activation and release of a microtubule inhibitor from amphiphilic polymeric nanoparticles

    doi: 10.1039/d6na00763e

    Figure Lengend Snippet: Representative lowest energy docking poses of (a) cis -PST-1, (b) trans -PST-1, (c) cis -proPST-1, and (d) trans -proPST-1 within the colchicine binding pocket of tubulin (PDB ID: 5LYJ). Ligands are represented as orange sticks, while interacting amino acid residues are shown as yellow sticks and labelled using single-letter amino acid notation. Hydrogen-bonding and hydrophobic interactions are indicated by red and blue dashed lines, respectively, with corresponding interaction distances (Å) shown. Structures and interaction maps were generated using PyMOL v3.0.

    Article Snippet: Tubulin MAP-rich (porcine brain) (Cat. #ML116), Tubulin protein (fluorescent HiLyte 488): porcine brain (Cat. #TL488M), General tubulin buffer (Cat. #BST01), Tubulin glycerol buffer (Cat. #BST05) and Taxol (Cat. #TXD01) and GTP (Cat. #BTS06) were obtained from Cytoskeleton, Inc and used as per the instruction manual.

    Techniques: Docking Assay, Binding Assay, Generated

    (a) Schematic representation of light-controlled inhibition of microtubule polymerisation by proPST-1-loaded polymer nanoparticles (proPST-1@PN). Under dark conditions, the encapsulated photocaged prodrug remains inactive, allowing normal microtubule formation. Upon 365 nm irradiation, photolytic uncaging and release of active cis -PST-1 suppress microtubule assembly. Created in BioRender. Singh, H. (2026) https://BioRender.com/fac5r0eT . (b) Tubulin polymerisation kinetics monitored by absorbance at 340 nm for control samples, empty polymer nanoparticles (PN control), and proPST-1@PN under dark and irradiated conditions. Irradiation of proPST-1@PN results in pronounced inhibition of tubulin polymerisation, whereas no inhibition is observed in the dark. (c) Fluorescence microscopy images of microtubule structures formed in the presence of control samples, proPST-1@PN under dark conditions, and irradiated proPST-1@PN. Normal microtubule growth and network formation are observed in control and dark conditions, while irradiation results in substantial disruption of microtubule assembly. Scale bars: 10 µm.

    Journal: Nanoscale Advances

    Article Title: Simultaneous activation and release of a microtubule inhibitor from amphiphilic polymeric nanoparticles

    doi: 10.1039/d6na00763e

    Figure Lengend Snippet: (a) Schematic representation of light-controlled inhibition of microtubule polymerisation by proPST-1-loaded polymer nanoparticles (proPST-1@PN). Under dark conditions, the encapsulated photocaged prodrug remains inactive, allowing normal microtubule formation. Upon 365 nm irradiation, photolytic uncaging and release of active cis -PST-1 suppress microtubule assembly. Created in BioRender. Singh, H. (2026) https://BioRender.com/fac5r0eT . (b) Tubulin polymerisation kinetics monitored by absorbance at 340 nm for control samples, empty polymer nanoparticles (PN control), and proPST-1@PN under dark and irradiated conditions. Irradiation of proPST-1@PN results in pronounced inhibition of tubulin polymerisation, whereas no inhibition is observed in the dark. (c) Fluorescence microscopy images of microtubule structures formed in the presence of control samples, proPST-1@PN under dark conditions, and irradiated proPST-1@PN. Normal microtubule growth and network formation are observed in control and dark conditions, while irradiation results in substantial disruption of microtubule assembly. Scale bars: 10 µm.

    Article Snippet: Tubulin MAP-rich (porcine brain) (Cat. #ML116), Tubulin protein (fluorescent HiLyte 488): porcine brain (Cat. #TL488M), General tubulin buffer (Cat. #BST01), Tubulin glycerol buffer (Cat. #BST05) and Taxol (Cat. #TXD01) and GTP (Cat. #BTS06) were obtained from Cytoskeleton, Inc and used as per the instruction manual.

    Techniques: Inhibition, Polymer, Irradiation, Control, Fluorescence, Microscopy, Disruption