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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.
Strad, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+strad/pmc12933830-170-15-17?v=Santa+Cruz+Biotechnology
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rabbit anti-lyk5 (stradα  (Millipore)
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Millipore rabbit anti-lyk5 (stradα
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.
Rabbit Anti Lyk5 (Stradα, 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
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strad  (Biorbyt)
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Biorbyt 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.
Strad, supplied by Biorbyt, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti strad  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology anti 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.
Anti Strad, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+strad/pm35595099-166-0-22?v=Santa+Cruz+Biotechnology
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anti strad - by Bioz Stars, 2026-07
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stradα  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology stradα
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.
Stradα, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+strad/pmc08727739-88-12-24?v=Santa+Cruz+Biotechnology
Average 93 stars, based on 1 article reviews
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anti strad n 13  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology anti strad n 13
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.
Anti Strad N 13, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+strad/10__1016_slash_j__jbc__2021__100929-362-0-5?v=Santa+Cruz+Biotechnology
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strad  (Danaher Inc)
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Danaher Inc 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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rabbit polyclonal anti lyk5  (Danaher Inc)
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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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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