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strad  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology strad
    Taurine activates the AMPK/NRF2 pathway by promoting the formation of <t>the</t> <t>LKB1-STRAD-MO25</t> kinase complex (A) Quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (B-C) Analysis of the binding of Taurine to purified LKB1 and MO25 WT proteins using surface plasmon resonance assay (SPR). (D) Plots of RMSD estimate averaged over all 10 trials versus simulation time for taurine docked with LKB1-STRAD-MO25 complex were calculated using Binding-pose metadynamics. A docking pose with a low PoseScore and high PersScore suggests a stable and reliable binding mode. (E) 3D diagram showing the most stable binding mode of taurine and LKB1-STRAD-MO25 (IFD2). (F) The LKB1 (Glu165 Arg301) and MO25 (Arg194 Leu197) sites were mutated to Ala, and quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (G) The difference in the binding ability of LKB1 to MO25 in WT-NPCs and LKB1&MO25 point mutant NPCs (Mut-NPCs) was detected by co-immunoprecipitation after A1TP-HX-EVs treatment. Statistical analysis was performed using a two‐tailed unpaired Student's t‐test. n = 3, ∗∗ P < 0.01. (H) WT-NPCs and Mut-NPCs were induced with TBHP, and then treated with A1TP-HX-EVs for 24 h. Cell lysates were immunoblotted with antibodies against IVDD markers and ferroptosis-related proteins. (I) Cell lysates were immunoblotted with antibodies against AMPK signaling pathway-related proteins. (J) Representative images of mitochondrial morphology of TBHP-induced WT-NPCs and Mut-NPCs using TEM after 24 h of treatment as indicated. n = 3. Scale bar, 500 nm. (K-L) Representative oxygen consumption traces of WT-NPCs and Mut-NPCs induced with TBHP and then treated with A1TP-HX-EVs for 24 h. Maximal respiration of NPCs were quantified. All data are expressed as the mean ± SD. One‐way ANOVA with Tukey's multiple comparison tests were used for statistical analysis. n = 3, ∗ P < 0.05. ∗∗ P < 0.01. ns, not significant.
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    Images

    1) Product Images from "ADGRG1-targeted hypoxia preconditioned extracellular vesicles ameliorate intervertebral disc degeneration by delivering taurine to disrupt the oxidative stress feedback loop-driven ferroptosis in nucleus pulposus cells"

    Article Title: ADGRG1-targeted hypoxia preconditioned extracellular vesicles ameliorate intervertebral disc degeneration by delivering taurine to disrupt the oxidative stress feedback loop-driven ferroptosis in nucleus pulposus cells

    Journal: Bioactive Materials

    doi: 10.1016/j.bioactmat.2026.02.029

    Taurine activates the AMPK/NRF2 pathway by promoting the formation of the LKB1-STRAD-MO25 kinase complex (A) Quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (B-C) Analysis of the binding of Taurine to purified LKB1 and MO25 WT proteins using surface plasmon resonance assay (SPR). (D) Plots of RMSD estimate averaged over all 10 trials versus simulation time for taurine docked with LKB1-STRAD-MO25 complex were calculated using Binding-pose metadynamics. A docking pose with a low PoseScore and high PersScore suggests a stable and reliable binding mode. (E) 3D diagram showing the most stable binding mode of taurine and LKB1-STRAD-MO25 (IFD2). (F) The LKB1 (Glu165 Arg301) and MO25 (Arg194 Leu197) sites were mutated to Ala, and quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (G) The difference in the binding ability of LKB1 to MO25 in WT-NPCs and LKB1&MO25 point mutant NPCs (Mut-NPCs) was detected by co-immunoprecipitation after A1TP-HX-EVs treatment. Statistical analysis was performed using a two‐tailed unpaired Student's t‐test. n = 3, ∗∗ P < 0.01. (H) WT-NPCs and Mut-NPCs were induced with TBHP, and then treated with A1TP-HX-EVs for 24 h. Cell lysates were immunoblotted with antibodies against IVDD markers and ferroptosis-related proteins. (I) Cell lysates were immunoblotted with antibodies against AMPK signaling pathway-related proteins. (J) Representative images of mitochondrial morphology of TBHP-induced WT-NPCs and Mut-NPCs using TEM after 24 h of treatment as indicated. n = 3. Scale bar, 500 nm. (K-L) Representative oxygen consumption traces of WT-NPCs and Mut-NPCs induced with TBHP and then treated with A1TP-HX-EVs for 24 h. Maximal respiration of NPCs were quantified. All data are expressed as the mean ± SD. One‐way ANOVA with Tukey's multiple comparison tests were used for statistical analysis. n = 3, ∗ P < 0.05. ∗∗ P < 0.01. ns, not significant.
    Figure Legend Snippet: Taurine activates the AMPK/NRF2 pathway by promoting the formation of the LKB1-STRAD-MO25 kinase complex (A) Quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (B-C) Analysis of the binding of Taurine to purified LKB1 and MO25 WT proteins using surface plasmon resonance assay (SPR). (D) Plots of RMSD estimate averaged over all 10 trials versus simulation time for taurine docked with LKB1-STRAD-MO25 complex were calculated using Binding-pose metadynamics. A docking pose with a low PoseScore and high PersScore suggests a stable and reliable binding mode. (E) 3D diagram showing the most stable binding mode of taurine and LKB1-STRAD-MO25 (IFD2). (F) The LKB1 (Glu165 Arg301) and MO25 (Arg194 Leu197) sites were mutated to Ala, and quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (G) The difference in the binding ability of LKB1 to MO25 in WT-NPCs and LKB1&MO25 point mutant NPCs (Mut-NPCs) was detected by co-immunoprecipitation after A1TP-HX-EVs treatment. Statistical analysis was performed using a two‐tailed unpaired Student's t‐test. n = 3, ∗∗ P < 0.01. (H) WT-NPCs and Mut-NPCs were induced with TBHP, and then treated with A1TP-HX-EVs for 24 h. Cell lysates were immunoblotted with antibodies against IVDD markers and ferroptosis-related proteins. (I) Cell lysates were immunoblotted with antibodies against AMPK signaling pathway-related proteins. (J) Representative images of mitochondrial morphology of TBHP-induced WT-NPCs and Mut-NPCs using TEM after 24 h of treatment as indicated. n = 3. Scale bar, 500 nm. (K-L) Representative oxygen consumption traces of WT-NPCs and Mut-NPCs induced with TBHP and then treated with A1TP-HX-EVs for 24 h. Maximal respiration of NPCs were quantified. All data are expressed as the mean ± SD. One‐way ANOVA with Tukey's multiple comparison tests were used for statistical analysis. n = 3, ∗ P < 0.05. ∗∗ P < 0.01. ns, not significant.

    Techniques Used: Binding Assay, Liquid Chromatography with Mass Spectroscopy, Purification, SPR Assay, Mutagenesis, Immunoprecipitation, Two Tailed Test, Comparison



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    Millipore lkb1-strad-mo25
    Taurine activates the AMPK/NRF2 pathway by promoting the formation of <t>the</t> <t>LKB1-STRAD-MO25</t> kinase complex (A) Quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (B-C) Analysis of the binding of Taurine to purified LKB1 and MO25 WT proteins using surface plasmon resonance assay (SPR). (D) Plots of RMSD estimate averaged over all 10 trials versus simulation time for taurine docked with LKB1-STRAD-MO25 complex were calculated using Binding-pose metadynamics. A docking pose with a low PoseScore and high PersScore suggests a stable and reliable binding mode. (E) 3D diagram showing the most stable binding mode of taurine and LKB1-STRAD-MO25 (IFD2). (F) The LKB1 (Glu165 Arg301) and MO25 (Arg194 Leu197) sites were mutated to Ala, and quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (G) The difference in the binding ability of LKB1 to MO25 in WT-NPCs and LKB1&MO25 point mutant NPCs (Mut-NPCs) was detected by co-immunoprecipitation after A1TP-HX-EVs treatment. Statistical analysis was performed using a two‐tailed unpaired Student's t‐test. n = 3, ∗∗ P < 0.01. (H) WT-NPCs and Mut-NPCs were induced with TBHP, and then treated with A1TP-HX-EVs for 24 h. Cell lysates were immunoblotted with antibodies against IVDD markers and ferroptosis-related proteins. (I) Cell lysates were immunoblotted with antibodies against AMPK signaling pathway-related proteins. (J) Representative images of mitochondrial morphology of TBHP-induced WT-NPCs and Mut-NPCs using TEM after 24 h of treatment as indicated. n = 3. Scale bar, 500 nm. (K-L) Representative oxygen consumption traces of WT-NPCs and Mut-NPCs induced with TBHP and then treated with A1TP-HX-EVs for 24 h. Maximal respiration of NPCs were quantified. All data are expressed as the mean ± SD. One‐way ANOVA with Tukey's multiple comparison tests were used for statistical analysis. n = 3, ∗ P < 0.05. ∗∗ P < 0.01. ns, not significant.
    Lkb1 Strad Mo25, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lkb1-strad-mo25/product/Millipore
    Average 90 stars, based on 1 article reviews
    lkb1-strad-mo25 - by Bioz Stars, 2026-06
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    synthetic dna fragments encoding the intracellular part of lyk5 7kr and lyk5 17kr  (Thermo Fisher)
    90
    Thermo Fisher synthetic dna fragments encoding the intracellular part of lyk5 7kr and lyk5 17kr
    Taurine activates the AMPK/NRF2 pathway by promoting the formation of <t>the</t> <t>LKB1-STRAD-MO25</t> kinase complex (A) Quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (B-C) Analysis of the binding of Taurine to purified LKB1 and MO25 WT proteins using surface plasmon resonance assay (SPR). (D) Plots of RMSD estimate averaged over all 10 trials versus simulation time for taurine docked with LKB1-STRAD-MO25 complex were calculated using Binding-pose metadynamics. A docking pose with a low PoseScore and high PersScore suggests a stable and reliable binding mode. (E) 3D diagram showing the most stable binding mode of taurine and LKB1-STRAD-MO25 (IFD2). (F) The LKB1 (Glu165 Arg301) and MO25 (Arg194 Leu197) sites were mutated to Ala, and quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (G) The difference in the binding ability of LKB1 to MO25 in WT-NPCs and LKB1&MO25 point mutant NPCs (Mut-NPCs) was detected by co-immunoprecipitation after A1TP-HX-EVs treatment. Statistical analysis was performed using a two‐tailed unpaired Student's t‐test. n = 3, ∗∗ P < 0.01. (H) WT-NPCs and Mut-NPCs were induced with TBHP, and then treated with A1TP-HX-EVs for 24 h. Cell lysates were immunoblotted with antibodies against IVDD markers and ferroptosis-related proteins. (I) Cell lysates were immunoblotted with antibodies against AMPK signaling pathway-related proteins. (J) Representative images of mitochondrial morphology of TBHP-induced WT-NPCs and Mut-NPCs using TEM after 24 h of treatment as indicated. n = 3. Scale bar, 500 nm. (K-L) Representative oxygen consumption traces of WT-NPCs and Mut-NPCs induced with TBHP and then treated with A1TP-HX-EVs for 24 h. Maximal respiration of NPCs were quantified. All data are expressed as the mean ± SD. One‐way ANOVA with Tukey's multiple comparison tests were used for statistical analysis. n = 3, ∗ P < 0.05. ∗∗ P < 0.01. ns, not significant.
    Synthetic Dna Fragments Encoding The Intracellular Part Of Lyk5 7kr And Lyk5 17kr, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/synthetic dna fragments encoding the intracellular part of lyk5 7kr and lyk5 17kr/product/Thermo Fisher
    Average 90 stars, based on 1 article reviews
    synthetic dna fragments encoding the intracellular part of lyk5 7kr and lyk5 17kr - by Bioz Stars, 2026-06
    90/100 stars
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    Image Search Results


    Taurine activates the AMPK/NRF2 pathway by promoting the formation of the LKB1-STRAD-MO25 kinase complex (A) Quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (B-C) Analysis of the binding of Taurine to purified LKB1 and MO25 WT proteins using surface plasmon resonance assay (SPR). (D) Plots of RMSD estimate averaged over all 10 trials versus simulation time for taurine docked with LKB1-STRAD-MO25 complex were calculated using Binding-pose metadynamics. A docking pose with a low PoseScore and high PersScore suggests a stable and reliable binding mode. (E) 3D diagram showing the most stable binding mode of taurine and LKB1-STRAD-MO25 (IFD2). (F) The LKB1 (Glu165 Arg301) and MO25 (Arg194 Leu197) sites were mutated to Ala, and quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (G) The difference in the binding ability of LKB1 to MO25 in WT-NPCs and LKB1&MO25 point mutant NPCs (Mut-NPCs) was detected by co-immunoprecipitation after A1TP-HX-EVs treatment. Statistical analysis was performed using a two‐tailed unpaired Student's t‐test. n = 3, ∗∗ P < 0.01. (H) WT-NPCs and Mut-NPCs were induced with TBHP, and then treated with A1TP-HX-EVs for 24 h. Cell lysates were immunoblotted with antibodies against IVDD markers and ferroptosis-related proteins. (I) Cell lysates were immunoblotted with antibodies against AMPK signaling pathway-related proteins. (J) Representative images of mitochondrial morphology of TBHP-induced WT-NPCs and Mut-NPCs using TEM after 24 h of treatment as indicated. n = 3. Scale bar, 500 nm. (K-L) Representative oxygen consumption traces of WT-NPCs and Mut-NPCs induced with TBHP and then treated with A1TP-HX-EVs for 24 h. Maximal respiration of NPCs were quantified. All data are expressed as the mean ± SD. One‐way ANOVA with Tukey's multiple comparison tests were used for statistical analysis. n = 3, ∗ P < 0.05. ∗∗ P < 0.01. ns, not significant.

    Journal: Bioactive Materials

    Article Title: ADGRG1-targeted hypoxia preconditioned extracellular vesicles ameliorate intervertebral disc degeneration by delivering taurine to disrupt the oxidative stress feedback loop-driven ferroptosis in nucleus pulposus cells

    doi: 10.1016/j.bioactmat.2026.02.029

    Figure Lengend Snippet: Taurine activates the AMPK/NRF2 pathway by promoting the formation of the LKB1-STRAD-MO25 kinase complex (A) Quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (B-C) Analysis of the binding of Taurine to purified LKB1 and MO25 WT proteins using surface plasmon resonance assay (SPR). (D) Plots of RMSD estimate averaged over all 10 trials versus simulation time for taurine docked with LKB1-STRAD-MO25 complex were calculated using Binding-pose metadynamics. A docking pose with a low PoseScore and high PersScore suggests a stable and reliable binding mode. (E) 3D diagram showing the most stable binding mode of taurine and LKB1-STRAD-MO25 (IFD2). (F) The LKB1 (Glu165 Arg301) and MO25 (Arg194 Leu197) sites were mutated to Ala, and quantitative abundance of taurine binding with LKB1-STRAD-MO25 complex subunits was measured using an LC-MS/MS-based trace-level detection method, n = 3. (G) The difference in the binding ability of LKB1 to MO25 in WT-NPCs and LKB1&MO25 point mutant NPCs (Mut-NPCs) was detected by co-immunoprecipitation after A1TP-HX-EVs treatment. Statistical analysis was performed using a two‐tailed unpaired Student's t‐test. n = 3, ∗∗ P < 0.01. (H) WT-NPCs and Mut-NPCs were induced with TBHP, and then treated with A1TP-HX-EVs for 24 h. Cell lysates were immunoblotted with antibodies against IVDD markers and ferroptosis-related proteins. (I) Cell lysates were immunoblotted with antibodies against AMPK signaling pathway-related proteins. (J) Representative images of mitochondrial morphology of TBHP-induced WT-NPCs and Mut-NPCs using TEM after 24 h of treatment as indicated. n = 3. Scale bar, 500 nm. (K-L) Representative oxygen consumption traces of WT-NPCs and Mut-NPCs induced with TBHP and then treated with A1TP-HX-EVs for 24 h. Maximal respiration of NPCs were quantified. All data are expressed as the mean ± SD. One‐way ANOVA with Tukey's multiple comparison tests were used for statistical analysis. n = 3, ∗ P < 0.05. ∗∗ P < 0.01. ns, not significant.

    Article Snippet: The primary antibodies included LKB1 (sc-32245, Santa Cruz Biotechnology), MO25 (2716S, Cell Signaling Technology), and STRAD (sc-515635, Santa Cruz Biotechnology).

    Techniques: Binding Assay, Liquid Chromatography with Mass Spectroscopy, Purification, SPR Assay, Mutagenesis, Immunoprecipitation, Two Tailed Test, Comparison