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  • 99
    New England Biolabs atp
    Atp, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore adenosine 5
    Adenosine 5, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore adenosine triphosphate
    Adenosine Triphosphate, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore amp pnp
    The majority of rings in cell ghosts undergo full contraction upon stabilization of actin filaments. (A, top) Rlc1-GFP rings in cell ghosts incubated with 0.5 mM ATP and 100 µM blebbistatin. (Bottom) Rlc1-mCherry rings in cell ghosts incubated with 0.5 mM <t>AMP-PNP.</t> (B) Rlc1-mCherry rings in cell ghosts were stained with GST-LifeAct-GFP and incubated with 0.5 mM AMP-PNP (four rings) or 0.5 mM ATP (11 rings). (C) Contraction of rings in cell ghosts in the presence of 20 µM jasp (56 rings); rings in cell ghosts that underwent full-ring contraction versus those that formed clusters were quantitated. Full, full-ring contraction. (D) The change of Rlc1-GFP ring perimeters over time in cell ghosts was quantitated (11 rings each sample). (E) Rlc1-mCherry rings in cell ghosts were incubated with ATP with or without 5 µM Pha for 40 min, and then stained with purified GST-LifeAct-GFP. (F) Pha treatment stabilizes actin filaments in rings in cell ghosts. Proteins were extracted from ATP-treated rings in cell ghosts with or without Pha, and immunoblots were probed with α-actin or Cdc8p. Asterisks, actin; S, supernatant; P, pellet. (G) Quantification of the intensity of bands in protein blots (four protein blots). (H) An ultracentrifugation assay of the actin proteins during contraction of rings in cell ghosts. G, globular actin; F, filamentous actin; S, supernatant; P, pellet. Quantification of the band intensity on the protein blots (two protein blots). Shown at top and bottom are blots exposed for different durations. The intensity of bands (G and F lanes) in protein blots was quantitated. (I) Inhibition of loss of actin filaments (flux out) by jasp or Pha from the rings in cell ghosts improves ring contraction efficiency in the absence of actin polymerization (flux in).
    Amp Pnp, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    The majority of rings in cell ghosts undergo full contraction upon stabilization of actin filaments. (A, top) Rlc1-GFP rings in cell ghosts incubated with 0.5 mM ATP and 100 µM blebbistatin. (Bottom) Rlc1-mCherry rings in cell ghosts incubated with 0.5 mM AMP-PNP. (B) Rlc1-mCherry rings in cell ghosts were stained with GST-LifeAct-GFP and incubated with 0.5 mM AMP-PNP (four rings) or 0.5 mM ATP (11 rings). (C) Contraction of rings in cell ghosts in the presence of 20 µM jasp (56 rings); rings in cell ghosts that underwent full-ring contraction versus those that formed clusters were quantitated. Full, full-ring contraction. (D) The change of Rlc1-GFP ring perimeters over time in cell ghosts was quantitated (11 rings each sample). (E) Rlc1-mCherry rings in cell ghosts were incubated with ATP with or without 5 µM Pha for 40 min, and then stained with purified GST-LifeAct-GFP. (F) Pha treatment stabilizes actin filaments in rings in cell ghosts. Proteins were extracted from ATP-treated rings in cell ghosts with or without Pha, and immunoblots were probed with α-actin or Cdc8p. Asterisks, actin; S, supernatant; P, pellet. (G) Quantification of the intensity of bands in protein blots (four protein blots). (H) An ultracentrifugation assay of the actin proteins during contraction of rings in cell ghosts. G, globular actin; F, filamentous actin; S, supernatant; P, pellet. Quantification of the band intensity on the protein blots (two protein blots). Shown at top and bottom are blots exposed for different durations. The intensity of bands (G and F lanes) in protein blots was quantitated. (I) Inhibition of loss of actin filaments (flux out) by jasp or Pha from the rings in cell ghosts improves ring contraction efficiency in the absence of actin polymerization (flux in).

    Journal: The Journal of Cell Biology

    Article Title: Actin turnover maintains actin filament homeostasis during cytokinetic ring contraction

    doi: 10.1083/jcb.201701104

    Figure Lengend Snippet: The majority of rings in cell ghosts undergo full contraction upon stabilization of actin filaments. (A, top) Rlc1-GFP rings in cell ghosts incubated with 0.5 mM ATP and 100 µM blebbistatin. (Bottom) Rlc1-mCherry rings in cell ghosts incubated with 0.5 mM AMP-PNP. (B) Rlc1-mCherry rings in cell ghosts were stained with GST-LifeAct-GFP and incubated with 0.5 mM AMP-PNP (four rings) or 0.5 mM ATP (11 rings). (C) Contraction of rings in cell ghosts in the presence of 20 µM jasp (56 rings); rings in cell ghosts that underwent full-ring contraction versus those that formed clusters were quantitated. Full, full-ring contraction. (D) The change of Rlc1-GFP ring perimeters over time in cell ghosts was quantitated (11 rings each sample). (E) Rlc1-mCherry rings in cell ghosts were incubated with ATP with or without 5 µM Pha for 40 min, and then stained with purified GST-LifeAct-GFP. (F) Pha treatment stabilizes actin filaments in rings in cell ghosts. Proteins were extracted from ATP-treated rings in cell ghosts with or without Pha, and immunoblots were probed with α-actin or Cdc8p. Asterisks, actin; S, supernatant; P, pellet. (G) Quantification of the intensity of bands in protein blots (four protein blots). (H) An ultracentrifugation assay of the actin proteins during contraction of rings in cell ghosts. G, globular actin; F, filamentous actin; S, supernatant; P, pellet. Quantification of the band intensity on the protein blots (two protein blots). Shown at top and bottom are blots exposed for different durations. The intensity of bands (G and F lanes) in protein blots was quantitated. (I) Inhibition of loss of actin filaments (flux out) by jasp or Pha from the rings in cell ghosts improves ring contraction efficiency in the absence of actin polymerization (flux in).

    Article Snippet: SMIFH2 (#344092; EMD Millipore), CK-666 (SML0006; Sigma-Aldrich), phallacidin (ab143532; water soluble; Abcam), blebbistatin (B0560; Sigma-Aldrich), and AMP-PNP (A2647; Sigma-Aldrich) were used at final concentrations as specified in the figure legends.

    Techniques: Incubation, Staining, Purification, Western Blot, Inhibition