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pi 3 5 p2 echelon biosciences  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences pi 3 5 p2 echelon biosciences
    Pi 3 5 P2 Echelon Biosciences, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pi 3 5 p2 echelon biosciences/product/Echelon Biosciences
    Average 91 stars, based on 1 article reviews
    pi 3 5 p2 echelon biosciences - by Bioz Stars, 2025-02
    91/100 stars

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    Structure of the TRPML1‐GCaMP6m‐based Ca 2+ sensor. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in Hela cells. Scale bar, 5 µm. ML‐SA1 (20 µM)‐induced peak GCaMP6m responses (ΔF/F 0 ) were increased in CRISPR‐Cas9‐mediated LAMTOR1 KD cells. N = 9–10 cells from 4 independent experiments. TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1 Ca 2+ release in both control and LAMTOR1 KD cells. Quantification of peak responses as shown in (D). N = 11–19 cells from 5 independent experiments. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in hippocampal neurons. Scale bar, 10 µm. Treatment with GPN (200 µM), BAPTA‐AM (20 µM), or ML‐SI1 (20 µM) blocked ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of responses in (G). N = 5–8 cells from 3 independent experiments. Both LAMTOR1 KD and TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of peak responses as shown in I. N = 6–13 cells from 3 independent experiments. LAMTOR1 KD increased <t>PI(3,5)P2</t> (0.5 µM)‐induced TRPML1‐GCaMP6m responses and the blocking effect of ML‐SI1 treatment (20 µM). Quantification of peak TRPML1‐GCaMP6m responses as shown in (K). N = 6–16 cells from 3 independent experiments. Data information: Data with error bars are represented as means ± SEM. Statistical significance was assessed by Student’s t ‐test (C), two‐way ANOVA with Tukey’s post‐hoc analysis (E, J, L), and one‐way ANOVA with Dunnett’s post‐test (H). * P < 0.05, ** P < 0.01, *** P < 0.001, ### P < 0.001, n.s., not significant. Note that the traces in D, G, I, and K represent the mean values of each group. See also Fig . Source data are available online for this figure.
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    Structure of the TRPML1‐GCaMP6m‐based Ca 2+ sensor. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in Hela cells. Scale bar, 5 µm. ML‐SA1 (20 µM)‐induced peak GCaMP6m responses (ΔF/F 0 ) were increased in CRISPR‐Cas9‐mediated LAMTOR1 KD cells. N = 9–10 cells from 4 independent experiments. TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1 Ca 2+ release in both control and LAMTOR1 KD cells. Quantification of peak responses as shown in (D). N = 11–19 cells from 5 independent experiments. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in hippocampal neurons. Scale bar, 10 µm. Treatment with GPN (200 µM), BAPTA‐AM (20 µM), or ML‐SI1 (20 µM) blocked ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of responses in (G). N = 5–8 cells from 3 independent experiments. Both LAMTOR1 KD and TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of peak responses as shown in I. N = 6–13 cells from 3 independent experiments. LAMTOR1 KD increased PI(3,5)P2 (0.5 µM)‐induced TRPML1‐GCaMP6m responses and the blocking effect of ML‐SI1 treatment (20 µM). Quantification of peak TRPML1‐GCaMP6m responses as shown in (K). N = 6–16 cells from 3 independent experiments. Data information: Data with error bars are represented as means ± SEM. Statistical significance was assessed by Student’s t ‐test (C), two‐way ANOVA with Tukey’s post‐hoc analysis (E, J, L), and one‐way ANOVA with Dunnett’s post‐test (H). * P < 0.05, ** P < 0.01, *** P < 0.001, ### P < 0.001, n.s., not significant. Note that the traces in D, G, I, and K represent the mean values of each group. See also Fig . Source data are available online for this figure.

    Journal: The EMBO Journal

    Article Title: LAMTOR1 inhibition of TRPML1‐dependent lysosomal calcium release regulates dendritic lysosome trafficking and hippocampal neuronal function

    doi: 10.15252/embj.2021108119

    Figure Lengend Snippet: Structure of the TRPML1‐GCaMP6m‐based Ca 2+ sensor. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in Hela cells. Scale bar, 5 µm. ML‐SA1 (20 µM)‐induced peak GCaMP6m responses (ΔF/F 0 ) were increased in CRISPR‐Cas9‐mediated LAMTOR1 KD cells. N = 9–10 cells from 4 independent experiments. TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1 Ca 2+ release in both control and LAMTOR1 KD cells. Quantification of peak responses as shown in (D). N = 11–19 cells from 5 independent experiments. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in hippocampal neurons. Scale bar, 10 µm. Treatment with GPN (200 µM), BAPTA‐AM (20 µM), or ML‐SI1 (20 µM) blocked ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of responses in (G). N = 5–8 cells from 3 independent experiments. Both LAMTOR1 KD and TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of peak responses as shown in I. N = 6–13 cells from 3 independent experiments. LAMTOR1 KD increased PI(3,5)P2 (0.5 µM)‐induced TRPML1‐GCaMP6m responses and the blocking effect of ML‐SI1 treatment (20 µM). Quantification of peak TRPML1‐GCaMP6m responses as shown in (K). N = 6–16 cells from 3 independent experiments. Data information: Data with error bars are represented as means ± SEM. Statistical significance was assessed by Student’s t ‐test (C), two‐way ANOVA with Tukey’s post‐hoc analysis (E, J, L), and one‐way ANOVA with Dunnett’s post‐test (H). * P < 0.05, ** P < 0.01, *** P < 0.001, ### P < 0.001, n.s., not significant. Note that the traces in D, G, I, and K represent the mean values of each group. See also Fig . Source data are available online for this figure.

    Article Snippet: Shuttle PIP Kit, PI(3,5)P2 , Echelon Biosciences , Cat#P‐9035.

    Techniques: CRISPR, Blocking Assay

    The source and dilution of the antibodies used in western blotting experiments. Dilution for secondary antibodies is 1:2000.

    Journal: Neuroscience

    Article Title: Early Life Sleep Deprivation: Role of Oxido-Inflammatory Processes

    doi: 10.1016/j.neuroscience.2019.02.021

    Figure Lengend Snippet: The source and dilution of the antibodies used in western blotting experiments. Dilution for secondary antibodies is 1:2000.

    Article Snippet: Protein Primary antibody Company Primary antibody Cat # Primary antibody Dilution Primary antibody RRID # Secondary antibody TNF-α Cell Signaling 3707 1:1000 AB_2240625 Goat anti-rabbit IL-6 Thermo Fisher Scientific ARC0062 1:1000 AB_J501203 Goat anti-mouse P-P38 MAPK Abeam Ab47363 1:1000 AB_881848 Goat anti-rabbit P38 MAPK Abeam Ab31828 1:1000 AB_881839 Goat anti-mouse P-JNK1,2,3 Abeam Ab124956 1:1000 AB_10973183 Goat anti-rabbit JNK1,2,3 Abeam Ab208035 1:1000 Goat anti-rabbit BDNF Santa Cruz SC-546 1:500 AB_630940 Goat anti-rabbit P-ERK 1/2 Cell Signaling 9106S 1:1000 AB_331768 Goat anti-mouse ERK 1/2 Cell Signaling 9107S 1:1000 AB_10695739 Goat anti-rabbit MKP1 Thermo fisher Scientific PA5–17973 1:1000 AB_10986429 Rabbit Anti-goat PSD95 Thermo fisher Scientific MA 1–045 1:1000 AB_325399 Goat anti-mouse GluA1 Cell Signaling D4N9V 1:1000 AB_2732897 Goat anti-rabbit GluN2b Abeam Ab65783 1:1000 AB_1658870 Goat anti-rabbit P-CaM KII Santa Cruz SC-32289 1:1000 AB_626786 Goat anti-mouse CaM KII Santa Cruz SC-9035 1:1000 AB_634551 Goat anti-rabbit P-CREB Cell Signaling 06–519 1:250 AB_626786 Goat anti-rabbit CREB Santa Cruz SC-58 1:1000 AB_631314 Goat anti-rabbit β -actin Cell Signaling 3700S 1:1000 AB_2242334 Goat anti-mouse Open in a separate window The source and dilution of the antibodies used in western blotting experiments.

    Techniques: Western Blot