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fis1  (Boster Bio)


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    Structured Review

    Boster Bio fis1
    Fis1, supplied by Boster Bio, used in various techniques. Bioz Stars score: 91/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fis1/Anti-TTC11%2FFIS1+Antibody+Picoband/pm42002787-80-63-68
    Average 91 stars, based on 9 article reviews
    fis1 - by Bioz Stars, 2026-10
    91/100 stars

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    Related Articles

    Immunolabeling:

    Article Title: A Role for PGC-1a in the Control of Abnormal Mitochondrial Dynamics in Alzheimer’s Disease
    Article Snippet: .. Brain sections were immunolabeled with an antibody against OPA1 (1:200, cat # PB0773, Boster, Wuhan, China), MFN2 (1:100, Bioss, cat # bs-23685R, Beijing, China), DRP1 (1:200, Wanleibio, cat # WL03028, Shenyang, China), FIS1 (1:200, Boster, cat # A01932-2, Wuhan, China) and incubated with the corresponding secondary antibody. .. After washing, DAB (Boster, cat # AR1022, Wuhan, China) was used for dyeing, and hematoxylin was used for retaining.

    Incubation:

    Article Title: A Role for PGC-1a in the Control of Abnormal Mitochondrial Dynamics in Alzheimer’s Disease
    Article Snippet: .. Brain sections were immunolabeled with an antibody against OPA1 (1:200, cat # PB0773, Boster, Wuhan, China), MFN2 (1:100, Bioss, cat # bs-23685R, Beijing, China), DRP1 (1:200, Wanleibio, cat # WL03028, Shenyang, China), FIS1 (1:200, Boster, cat # A01932-2, Wuhan, China) and incubated with the corresponding secondary antibody. .. After washing, DAB (Boster, cat # AR1022, Wuhan, China) was used for dyeing, and hematoxylin was used for retaining.

    Article Title: Electroacupuncture improves motor function after ischemic stroke via regulating mitochondrial dynamics.
    Article Snippet: .. 10 % SDS-PAGE gel electrophoresis, PVDF membrane electrowetting transfer, 8 % milk sealed for 2 h, Tris buffered saline-tween (TBST) washing, adding the corresponding primary antibody: Mfn1 (Proteintech, 13798–1-AP), Mfn2 (Proteintech, 12186–1- AP), Fis1 (Boster, A01932–3), Drp1 (Proteintech, 12957–1-AP), Opa1 (Proteintech, 27733–1-AP), GAPDH (Proteintech, 60004–1-Ig), the membrane were incubated (with shaking) overnight at 4◦C. .. The corresponding goat anti-rabbit secondary antibody (Proteintech, PR30011, 1: 5000) or goat anti-mouse secondary antibody (Proteintech, PR30012, 1:5000), the membrane were incubated at room temperature for 1 h, and and then stained with ECL reagent.

    Software:

    Article Title: DMOG pretreatment restores osteogenic-adipogenic balance and mitochondrial function in ONFH BMSCs through the HIF-1α/Homer3 pathway.
    Article Snippet: .. Band intensity was quantified using ImageJ software.The primary antibodies used were Runt-related transcription factor 2 (RUNX2, 1:1000, Cat No. PB0171, Boster, China), and Osteopontin (OPN, 1:1000, Cat No. BM4208, Boster, China), and GAPDH (1:5000, Cat No. BM3874, Boster, China), β-Actin (1:50000, Cat No. AC026, ABclonal, China), and LC3B (1:2000, Cat No. BM4827, Boster, China), and DRP1 (1:2000, Cat No. A00556-2, Boster, China), and FIS1 (1:2000, Cat No. A01932-2, Boster, China), and OPA1 (1:2000, Cat No. PB0773, Boster, China), and MFN1 (1:2000, Cat No. PB0263, Boster, China), and HIF-1α (1:2000, Cat No. 20960-1-AP, Proteintech, China), and Homer3(1:1000, Cat No. 16624-1-AP, Proteintech, China). ..

    Pyrolysis Gas Chromatography:

    Article Title: A Role for PGC-1a in the Control of Abnormal Mitochondrial Dynamics in Alzheimer’s Disease
    Article Snippet: N 2 A cells were transfected with the Vector plasmid or plasmid-encoding APPswe or co-transfectioned with APPswe and pEnCMV / Ppargc1a plasmids for 48 h, cell homogenate was lysed and Western blots were performed as described previously [ ]. .. Primary antibodies against EGFP (1:1000, Beyotime, cat # AG281, Shanghai, China), Flag (1:1000, abm, cat # G188, Zhenjiang, China), OPA1 (1:1000, Boster, cat # PB0773, Wuhan, China), MFN1 (1:1000, Boster, cat # PB0263, Wuhan, China), MFN2 (1:800, Bioss, cat # bs-23685R, Beijing, China), DRP1 (1:1000, Wanleibio, cat # WL03028, Shenyang, China), FIS1 (1:1000, Boster, cat # A01932-2, Wuhan, China), BAX (1:5000, Abcam, cat # ab32503, Cambridge, MA, USA), Bcl-2 (1:2000, Abcam, cat # ab182858, Cambridge, MA, USA), PGC-1a (1:1000, Bioss, cat # bs-1832R, Beijing, China), KIF5A Flag (diluted 1:1000, Bioword, cat # BS71526, Nanjing, China), KIF5B (diluted 1:1000, Wanleibio, cat # WL04906, Shenyang, China), and the horseradish peroxidase-linked antibodies (1:5000, Beyotime, goat anti mouse IgG, cat # A0216 and goat anti rabbit IgG, cat # A0208, Shanghai, China) were used to probe these blots. .. Protein visualization was carried out using enhanced chemiluminescence (ECL, Beyotime Institute of Biotechnology, Shanghai, China).

    Control:

    Article Title: Short-Term DMOG treatment rejuvenates senescent mesenchymal stem cells by enhancing mitochondrial function and mitophagy through the HIF-1α/BNIP3 pathway
    Article Snippet: Total proteins were extracted from MSCs using RIPA lysis buffer (Boster, China), separated via SDS-PAGE, and transferred to PVDF membranes. .. The primary antibodies used were p53 (1:1000, BM4309, Boster, China), p21 (1:1000, BM3990, Boster, China), HIF-1α (1:1000, BM4083, Boster, China), MFN1 (1:1000, BM4882, Boster, China), MFN2 (1:1000, BM4906, Boster, China), FIS1 (1:1000, A01932-3, Boster, China), BNIP3 (1:1000, BA4304-2, Boster, China), and GAPDH (1:5000, BM1632, Boster, China) as an internal control. ..

    other:

    Article Title: Short-Term DMOG treatment rejuvenates senescent mesenchymal stem cells by enhancing mitochondrial function and mitophagy through the HIF-1α/BNIP3 pathway.
    Article Snippet: Total proteins were extracted from MSCs using RIPA lysis buffer (Boster, China), separated via SDS-PAGE, and transferred to PVDF membranes.

    SDS Page:

    Article Title: Electroacupuncture improves motor function after ischemic stroke via regulating mitochondrial dynamics.
    Article Snippet: .. 10 % SDS-PAGE gel electrophoresis, PVDF membrane electrowetting transfer, 8 % milk sealed for 2 h, Tris buffered saline-tween (TBST) washing, adding the corresponding primary antibody: Mfn1 (Proteintech, 13798–1-AP), Mfn2 (Proteintech, 12186–1- AP), Fis1 (Boster, A01932–3), Drp1 (Proteintech, 12957–1-AP), Opa1 (Proteintech, 27733–1-AP), GAPDH (Proteintech, 60004–1-Ig), the membrane were incubated (with shaking) overnight at 4◦C. .. The corresponding goat anti-rabbit secondary antibody (Proteintech, PR30011, 1: 5000) or goat anti-mouse secondary antibody (Proteintech, PR30012, 1:5000), the membrane were incubated at room temperature for 1 h, and and then stained with ECL reagent.

    Nucleic Acid Electrophoresis:

    Article Title: Electroacupuncture improves motor function after ischemic stroke via regulating mitochondrial dynamics.
    Article Snippet: .. 10 % SDS-PAGE gel electrophoresis, PVDF membrane electrowetting transfer, 8 % milk sealed for 2 h, Tris buffered saline-tween (TBST) washing, adding the corresponding primary antibody: Mfn1 (Proteintech, 13798–1-AP), Mfn2 (Proteintech, 12186–1- AP), Fis1 (Boster, A01932–3), Drp1 (Proteintech, 12957–1-AP), Opa1 (Proteintech, 27733–1-AP), GAPDH (Proteintech, 60004–1-Ig), the membrane were incubated (with shaking) overnight at 4◦C. .. The corresponding goat anti-rabbit secondary antibody (Proteintech, PR30011, 1: 5000) or goat anti-mouse secondary antibody (Proteintech, PR30012, 1:5000), the membrane were incubated at room temperature for 1 h, and and then stained with ECL reagent.

    Membrane:

    Article Title: Electroacupuncture improves motor function after ischemic stroke via regulating mitochondrial dynamics.
    Article Snippet: .. 10 % SDS-PAGE gel electrophoresis, PVDF membrane electrowetting transfer, 8 % milk sealed for 2 h, Tris buffered saline-tween (TBST) washing, adding the corresponding primary antibody: Mfn1 (Proteintech, 13798–1-AP), Mfn2 (Proteintech, 12186–1- AP), Fis1 (Boster, A01932–3), Drp1 (Proteintech, 12957–1-AP), Opa1 (Proteintech, 27733–1-AP), GAPDH (Proteintech, 60004–1-Ig), the membrane were incubated (with shaking) overnight at 4◦C. .. The corresponding goat anti-rabbit secondary antibody (Proteintech, PR30011, 1: 5000) or goat anti-mouse secondary antibody (Proteintech, PR30012, 1:5000), the membrane were incubated at room temperature for 1 h, and and then stained with ECL reagent.

    Saline:

    Article Title: Electroacupuncture improves motor function after ischemic stroke via regulating mitochondrial dynamics.
    Article Snippet: .. 10 % SDS-PAGE gel electrophoresis, PVDF membrane electrowetting transfer, 8 % milk sealed for 2 h, Tris buffered saline-tween (TBST) washing, adding the corresponding primary antibody: Mfn1 (Proteintech, 13798–1-AP), Mfn2 (Proteintech, 12186–1- AP), Fis1 (Boster, A01932–3), Drp1 (Proteintech, 12957–1-AP), Opa1 (Proteintech, 27733–1-AP), GAPDH (Proteintech, 60004–1-Ig), the membrane were incubated (with shaking) overnight at 4◦C. .. The corresponding goat anti-rabbit secondary antibody (Proteintech, PR30011, 1: 5000) or goat anti-mouse secondary antibody (Proteintech, PR30012, 1:5000), the membrane were incubated at room temperature for 1 h, and and then stained with ECL reagent.



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    Effects of maternal non-esterified fatty acid (NEFA) levels on mitochondrial dynamics and related protein expression in the biceps femoris muscle of newborn calves. A and B Western blot analysis of mitochondrial fission-related proteins (DRP1, <t>FIS1)</t> and STING. Protein abundance was normalized to β-tubulin. C Relative mRNA expression of mitochondrial dynamics-related genes in biceps femoris muscle. DL-NEFA, dry cows with low serum NEFA concentration; DH-NEFA, dry cows with high serum NEFA concentration. For relative expression analysis, DL-NEFA group was set to 1, and values in the DH-NEFA are expressed relative to the DL-NEFA group. Data are presented as LSmean ± SEM ( n = 8 per group)
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    ABclonal Biotechnology anti rabbit fis1 antibody
    ( A to Db ) Cross sections through the Gas muscle of Pax +/+ , Myh7 fl/+ (A to Bb) and Pax7 icre/+ , Myh7 Δ/fl (C to Db) mice at 2 and 12 months, respectively, labeled by immunofluorescence for MyHC-slow (green), troponin T1 (red), and DAPI (blue). Scale bars, 100 μm (Cb and Db). ( E to H ) SDH staining on Gas muscle sections of Pax +/+ , Myh7 fl/+ (E and G) and Pax7 icre/+ , Myh7 Δ/fl (Ea and Ga) mice and quantification of the percentage SDH activity (F and H) at 2 and 12 months of age, respectively ( n = 5). Scale bars, 100 μm (Ea and Ga). ( I to L ) Representative Western blots for troponin T1, PGC-1α, and α-tubulin (loading control) using Gas muscle protein lysates of Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl (P0), and Pax7 icre/+ , Myh7 Δ/fl mice at P0 and 2 and 6 months (I) and their densitometric quantification (J to L) ( n = 4). ( M to P ) Representative Western blots for mitochondrial complexes and α-tubulin (loading control) using protein lysates from the Gas muscle of Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl (P0), and Pax7 icre/+ , Myh7 Δ/fl mice at P0 and 6 months (M and O) and their densitometric quantification (N to P) ( n = 4 to 6). ( Q to T ) Representative Western blots for <t>FIS1,</t> pDRP1, DRP1, OPA1, Mitofusin 1, Mitofusin 2, and α-tubulin (loading control) using protein lysates from the Gas muscle of Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl (P0), and Pax7 icre/+ , Myh7 Δ/fl mice at P0 and 2 and 6 months (Q) and densitometric quantification (R to T) ( n = 4). ( U and V ) Quantification of ATP levels in the Gas muscle of Pax +/+ , Myh7 fl/+ and Pax7 icre/+ , Myh7 Δ/fl mice at 2 and 12 months of age ( n = 5). Data are presented as means ± SEM. * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, and **** P ≤ 0.0001.
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    COPN restores mitochondrial quality control and interrupts the ROS‒cGAS‒inflammation axis in OGD/R-treated R28 cells. a , TEM images showing changes in the mitochondrial ultrastructure of R28 cells subjected to various treatments (PBS, PDNs, COPN-L, and COPN-H) after OGD/R. Scale bar: 500 nm b , Quantitative analyses of mitochondrial length and number in R28 cells as indicated in a . c , Representative fluorescence images showing JC-1 staining of the mitochondrial Δψm: aggregates (red) indicate healthy mitochondria, whereas monomers (green) represent depolarized mitochondria. Nuclei were stained with DAPI (blue). Scale bar: 50 μm d , Intracellular ATP content assay revealing improved energy production after COPN treatment under OGD/R stress conditions. e , mRNA expression analysis of mitochondrial dynamic regulatory genes (Opa1, Mfn2, Drp1, and <t>Fis1)</t> and mitochondrial DNA transcription levels (mt-ND1 and mt-COX1). f , Quantitative analysis of the JC-1 fluorescence ratio (aggregates/monomers) and mitochondrial ROS levels (MitoSOX staining). g–h , Western blot analysis of proteins involved in mitochondrial autophagy (Pink1, Parkin, and P62) (g) and mitochondrial fusion/fission (Opa1, Mfn2, Mfn1, Drp1, and Fis1) (h) . i , Confocal fluorescence microscopy images of mitochondria (green, MitoTracker) and lysosomes (red, LysoTracker) in R28 cells after different treatments. Nuclei were stained with Hoechst (blue). Scale bar: 50 μm ∗ ∗∗∗P < 0.0001. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
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    COPN restores mitochondrial quality control and interrupts the ROS‒cGAS‒inflammation axis in OGD/R-treated R28 cells. a , TEM images showing changes in the mitochondrial ultrastructure of R28 cells subjected to various treatments (PBS, PDNs, COPN-L, and COPN-H) after OGD/R. Scale bar: 500 nm b , Quantitative analyses of mitochondrial length and number in R28 cells as indicated in a . c , Representative fluorescence images showing JC-1 staining of the mitochondrial Δψm: aggregates (red) indicate healthy mitochondria, whereas monomers (green) represent depolarized mitochondria. Nuclei were stained with DAPI (blue). Scale bar: 50 μm d , Intracellular ATP content assay revealing improved energy production after COPN treatment under OGD/R stress conditions. e , mRNA expression analysis of mitochondrial dynamic regulatory genes (Opa1, Mfn2, Drp1, and <t>Fis1)</t> and mitochondrial DNA transcription levels (mt-ND1 and mt-COX1). f , Quantitative analysis of the JC-1 fluorescence ratio (aggregates/monomers) and mitochondrial ROS levels (MitoSOX staining). g–h , Western blot analysis of proteins involved in mitochondrial autophagy (Pink1, Parkin, and P62) (g) and mitochondrial fusion/fission (Opa1, Mfn2, Mfn1, Drp1, and Fis1) (h) . i , Confocal fluorescence microscopy images of mitochondria (green, MitoTracker) and lysosomes (red, LysoTracker) in R28 cells after different treatments. Nuclei were stained with Hoechst (blue). Scale bar: 50 μm ∗ ∗∗∗P < 0.0001. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
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    Image Search Results


    Effects of maternal non-esterified fatty acid (NEFA) levels on mitochondrial dynamics and related protein expression in the biceps femoris muscle of newborn calves. A and B Western blot analysis of mitochondrial fission-related proteins (DRP1, FIS1) and STING. Protein abundance was normalized to β-tubulin. C Relative mRNA expression of mitochondrial dynamics-related genes in biceps femoris muscle. DL-NEFA, dry cows with low serum NEFA concentration; DH-NEFA, dry cows with high serum NEFA concentration. For relative expression analysis, DL-NEFA group was set to 1, and values in the DH-NEFA are expressed relative to the DL-NEFA group. Data are presented as LSmean ± SEM ( n = 8 per group)

    Journal: Journal of Animal Science and Biotechnology

    Article Title: Elevated maternal non-esterified fatty acid concentrations during late gestation are associated with altered skeletal muscle development and mitochondrial dynamics related-markers in calves

    doi: 10.1186/s40104-026-01422-x

    Figure Lengend Snippet: Effects of maternal non-esterified fatty acid (NEFA) levels on mitochondrial dynamics and related protein expression in the biceps femoris muscle of newborn calves. A and B Western blot analysis of mitochondrial fission-related proteins (DRP1, FIS1) and STING. Protein abundance was normalized to β-tubulin. C Relative mRNA expression of mitochondrial dynamics-related genes in biceps femoris muscle. DL-NEFA, dry cows with low serum NEFA concentration; DH-NEFA, dry cows with high serum NEFA concentration. For relative expression analysis, DL-NEFA group was set to 1, and values in the DH-NEFA are expressed relative to the DL-NEFA group. Data are presented as LSmean ± SEM ( n = 8 per group)

    Article Snippet: Membranes were blocked with 1.5% skim milk for 2 h at RT, and further incubated overnight at 4 °C with primary antibodies against DRP1 (1:200; Cat. #A21968, ABclonal, Wuhan, China), FIS1 (1:500; Cat. #A5821, ABclonal, Wuhan, China), STING (1:500; Cat. #A21051, ABclonal, Wuhan, China), TBK1 (1:1,000; Cat. #A3458, ABclonal, Wuhan, China), or β-tubulin (1:1,000; Cat. #AF2835, Beyotime, Shanghai, China), respectively.

    Techniques: Expressing, Western Blot, Quantitative Proteomics, Concentration Assay

    Effects of maternal non-esterified fatty acid (NEFA) levels on mitochondrial dynamics and related protein expression in the skeletal muscle of one-month-old calves. A and B Western blot analysis of mitochondrial fission-related proteins (DRP1, FIS1) and STING. Protein abundance was normalized to β-tubulin. C Relative mRNA expression of mitochondrial dynamics-related genes in biceps femoris muscle. DL-NEFA, dry cows with low serum NEFA concentration; DH-NEFA, dry cows with high serum NEFA concentration. For relative expression analysis, DL-NEFA group was set to 1, and values in the DH-NEFA are expressed relative to the DL-NEFA group. Data are presented as LSmean ± SEM ( n = 8 calves per group)

    Journal: Journal of Animal Science and Biotechnology

    Article Title: Elevated maternal non-esterified fatty acid concentrations during late gestation are associated with altered skeletal muscle development and mitochondrial dynamics related-markers in calves

    doi: 10.1186/s40104-026-01422-x

    Figure Lengend Snippet: Effects of maternal non-esterified fatty acid (NEFA) levels on mitochondrial dynamics and related protein expression in the skeletal muscle of one-month-old calves. A and B Western blot analysis of mitochondrial fission-related proteins (DRP1, FIS1) and STING. Protein abundance was normalized to β-tubulin. C Relative mRNA expression of mitochondrial dynamics-related genes in biceps femoris muscle. DL-NEFA, dry cows with low serum NEFA concentration; DH-NEFA, dry cows with high serum NEFA concentration. For relative expression analysis, DL-NEFA group was set to 1, and values in the DH-NEFA are expressed relative to the DL-NEFA group. Data are presented as LSmean ± SEM ( n = 8 calves per group)

    Article Snippet: Membranes were blocked with 1.5% skim milk for 2 h at RT, and further incubated overnight at 4 °C with primary antibodies against DRP1 (1:200; Cat. #A21968, ABclonal, Wuhan, China), FIS1 (1:500; Cat. #A5821, ABclonal, Wuhan, China), STING (1:500; Cat. #A21051, ABclonal, Wuhan, China), TBK1 (1:1,000; Cat. #A3458, ABclonal, Wuhan, China), or β-tubulin (1:1,000; Cat. #AF2835, Beyotime, Shanghai, China), respectively.

    Techniques: Expressing, Western Blot, Quantitative Proteomics, Concentration Assay

    Effects of dosed non-esterified fatty acids (NEFA) treatment on myogenic differentiation and mitochondrial dynamics in C2C12 cells. A Immunofluorescence staining and relative fold changes of Desmin intensity with DAPI nuclear counterstaining (scale bar = 50 μm). B The mRNA expression of fast-twitch fiber formation-associated genes. C The mRNA expression of mitochondrial dynamics- and STING-signaling-related genes. D Western blot analysis of DRP1, FIS1, STING and TBK1. Protein abundance was normalized to β-tubulin. The 0 μmol/L NEFA group was set to 1, and treatment groups were expressed relative to the 0 μmol/L NEFA group. Data are presented as LSmean ± SEM ( n = 3 independent experiments; each treatment performed in triplicate)

    Journal: Journal of Animal Science and Biotechnology

    Article Title: Elevated maternal non-esterified fatty acid concentrations during late gestation are associated with altered skeletal muscle development and mitochondrial dynamics related-markers in calves

    doi: 10.1186/s40104-026-01422-x

    Figure Lengend Snippet: Effects of dosed non-esterified fatty acids (NEFA) treatment on myogenic differentiation and mitochondrial dynamics in C2C12 cells. A Immunofluorescence staining and relative fold changes of Desmin intensity with DAPI nuclear counterstaining (scale bar = 50 μm). B The mRNA expression of fast-twitch fiber formation-associated genes. C The mRNA expression of mitochondrial dynamics- and STING-signaling-related genes. D Western blot analysis of DRP1, FIS1, STING and TBK1. Protein abundance was normalized to β-tubulin. The 0 μmol/L NEFA group was set to 1, and treatment groups were expressed relative to the 0 μmol/L NEFA group. Data are presented as LSmean ± SEM ( n = 3 independent experiments; each treatment performed in triplicate)

    Article Snippet: Membranes were blocked with 1.5% skim milk for 2 h at RT, and further incubated overnight at 4 °C with primary antibodies against DRP1 (1:200; Cat. #A21968, ABclonal, Wuhan, China), FIS1 (1:500; Cat. #A5821, ABclonal, Wuhan, China), STING (1:500; Cat. #A21051, ABclonal, Wuhan, China), TBK1 (1:1,000; Cat. #A3458, ABclonal, Wuhan, China), or β-tubulin (1:1,000; Cat. #AF2835, Beyotime, Shanghai, China), respectively.

    Techniques: Cell Characterization, Immunofluorescence, Staining, Expressing, Western Blot, Quantitative Proteomics

    ( A to Db ) Cross sections through the Gas muscle of Pax +/+ , Myh7 fl/+ (A to Bb) and Pax7 icre/+ , Myh7 Δ/fl (C to Db) mice at 2 and 12 months, respectively, labeled by immunofluorescence for MyHC-slow (green), troponin T1 (red), and DAPI (blue). Scale bars, 100 μm (Cb and Db). ( E to H ) SDH staining on Gas muscle sections of Pax +/+ , Myh7 fl/+ (E and G) and Pax7 icre/+ , Myh7 Δ/fl (Ea and Ga) mice and quantification of the percentage SDH activity (F and H) at 2 and 12 months of age, respectively ( n = 5). Scale bars, 100 μm (Ea and Ga). ( I to L ) Representative Western blots for troponin T1, PGC-1α, and α-tubulin (loading control) using Gas muscle protein lysates of Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl (P0), and Pax7 icre/+ , Myh7 Δ/fl mice at P0 and 2 and 6 months (I) and their densitometric quantification (J to L) ( n = 4). ( M to P ) Representative Western blots for mitochondrial complexes and α-tubulin (loading control) using protein lysates from the Gas muscle of Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl (P0), and Pax7 icre/+ , Myh7 Δ/fl mice at P0 and 6 months (M and O) and their densitometric quantification (N to P) ( n = 4 to 6). ( Q to T ) Representative Western blots for FIS1, pDRP1, DRP1, OPA1, Mitofusin 1, Mitofusin 2, and α-tubulin (loading control) using protein lysates from the Gas muscle of Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl (P0), and Pax7 icre/+ , Myh7 Δ/fl mice at P0 and 2 and 6 months (Q) and densitometric quantification (R to T) ( n = 4). ( U and V ) Quantification of ATP levels in the Gas muscle of Pax +/+ , Myh7 fl/+ and Pax7 icre/+ , Myh7 Δ/fl mice at 2 and 12 months of age ( n = 5). Data are presented as means ± SEM. * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, and **** P ≤ 0.0001.

    Journal: Science Advances

    Article Title: The skeletal muscle slow myosin heavy chain regulates mammalian metabolic homeostasis through the NRF2 pathway

    doi: 10.1126/sciadv.aed2478

    Figure Lengend Snippet: ( A to Db ) Cross sections through the Gas muscle of Pax +/+ , Myh7 fl/+ (A to Bb) and Pax7 icre/+ , Myh7 Δ/fl (C to Db) mice at 2 and 12 months, respectively, labeled by immunofluorescence for MyHC-slow (green), troponin T1 (red), and DAPI (blue). Scale bars, 100 μm (Cb and Db). ( E to H ) SDH staining on Gas muscle sections of Pax +/+ , Myh7 fl/+ (E and G) and Pax7 icre/+ , Myh7 Δ/fl (Ea and Ga) mice and quantification of the percentage SDH activity (F and H) at 2 and 12 months of age, respectively ( n = 5). Scale bars, 100 μm (Ea and Ga). ( I to L ) Representative Western blots for troponin T1, PGC-1α, and α-tubulin (loading control) using Gas muscle protein lysates of Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl (P0), and Pax7 icre/+ , Myh7 Δ/fl mice at P0 and 2 and 6 months (I) and their densitometric quantification (J to L) ( n = 4). ( M to P ) Representative Western blots for mitochondrial complexes and α-tubulin (loading control) using protein lysates from the Gas muscle of Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl (P0), and Pax7 icre/+ , Myh7 Δ/fl mice at P0 and 6 months (M and O) and their densitometric quantification (N to P) ( n = 4 to 6). ( Q to T ) Representative Western blots for FIS1, pDRP1, DRP1, OPA1, Mitofusin 1, Mitofusin 2, and α-tubulin (loading control) using protein lysates from the Gas muscle of Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl (P0), and Pax7 icre/+ , Myh7 Δ/fl mice at P0 and 2 and 6 months (Q) and densitometric quantification (R to T) ( n = 4). ( U and V ) Quantification of ATP levels in the Gas muscle of Pax +/+ , Myh7 fl/+ and Pax7 icre/+ , Myh7 Δ/fl mice at 2 and 12 months of age ( n = 5). Data are presented as means ± SEM. * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, and **** P ≤ 0.0001.

    Article Snippet: The antibodies used for Western blotting were as follows: anti-mouse MyHC-IIa antibody (SC-71, Developmental Studies Hybridoma Bank) at 1:10 dilution; anti-mouse MyHC-IIb antibody (BFF3, Developmental Studies Hybridoma Bank) at 1:10; anti-mouse alpha-tubulin antibody (30021290, Cell Signaling Technology) at 1:10,000; anti-rabbit GAPDH antibody (PAB932Mu01, Cloud-Clone Corp) at 1:10,000; anti-rabbit Akt antibody (4641, Cell Signaling Technology) at 1:1000; anti-rabbit P-Akt S473 (4640, Cell Signaling Technology) at 1:1000; anti-rabbit Histone H3 antibody (Ab1741, Abcam) at 1:10,000; anti-rabbit troponin T1 antibody (NBP238855, Novus Biologicals) at 1:5000; anti-rabbit PGC-1α antibody (A12348, ABclonal; 66369, Proteintech; and 2178S, Cell Signaling Technology) at 1:2000, 1:2000, and 1:1000, respectively; anti-mouse total OXPHOS cocktail (ab110413, Abcam) at 1:1000; anti-rabbit DRP1 antibody (A21968, ABclonal) at 1:2000; anti-rabbit FIS1 antibody (A19666, ABclonal) at 1:2000; anti-rabbit mitofusin1 antibody (A9880, ABclonal) at 1:2000; anti-rabbit mitofusin2 antibody (A12771, ABclonal) at 1:2000; anti-rabbit GLUT4 (MA5-17176, Thermo Fisher Scientific) at 1:1000; anti-rabbit NRF2 antibody (A0674, ABclonal and 98020000, Proteintech) at 1:2000; anti-rabbit P-NRF2 antibody (AP1133, ABclonal) at 1:2000; anti-rabbit SOD1 antibody (A0274, ABclonal) at 1:2000; anti-rabbit Prdx1 antibody (A13524, ABclonal) at 1:2000; anti-rabbit Gpx1 antibody (A1110, ABclonal) at 1:1000; anti-rabbit catalase antibody (A11220, ABclonal) at 1:2000; anti-rabbit KEAP1 antibody (A1820, ABclonal) at 1:1000; anti-rabbit Tom20 antibody (HPA011582, Merck) at 1:2500, anti-rabbit VDAC1 antibody ( Ab154856 , Abcam) at 1:2500; anti-rabbit pDRP1 (S616) antibody (AP0849, ABclonal) at 1:2500; and anti-rabbit OPA1 antibody (A9833, ABclonal) at 1:2500.

    Techniques: Labeling, Immunofluorescence, Staining, Activity Assay, Western Blot, Control

    ( A ) Venn diagram depicting the number of unique and shared proteins expressed in the Gas muscle of Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice at P0 ( n = 6). KO, knockout. ( B ) PCA plot of the Gas muscle from Pax +/+ , Myh7 fl/+ (red) and Pax3 cre/+ , Myh7 Δ/fl (green) mice at P0, where each dot represents a biological replicate ( n = 6). ( C ) Volcano plot showing up-regulated and down-regulated proteins in the Gas muscle from Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice at P0 ( n = 6). ( D ) Pathway analysis (Reactome database) of Gas muscle proteins from Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice at P0. ( E ) Heatmap depicting the NRF2 pathway target protein expression in the Gas muscle of Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice at P0 ( n = 6). ( F and G ) Representative Western blots for SOD1, GPx1, Prdx2, Prdx1, catalase, and α-tubulin (loading control) using protein lysates from the Gas muscle of P0 Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl , and Pax7 icre/+ , Myh7 Δ/fl mice (F) and their densitometry (G) ( n = 5). ( H to M ) Representative Western blots for NRF2, P-NRF2, and α-tubulin (loading control) using Gas and TA muscle protein lysates of P0 Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl , and Pax7 icre/+ , Myh7 Δ/fl mice (H and I) and their densitometry (J to M) ( n = 5). ( N and O ) Label-free quantitation (LFQ) intensity of DRP1 and FIS1 by mass spectrometry on P0 Gas muscle protein lysates of Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice ( n = 6). ( P ) Heatmap depicting the expression of mitochondrial proteins in the Gas muscle of P0 Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice ( n = 6). Data are presented as means ± SEM. * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, and **** P ≤ 0.0001.

    Journal: Science Advances

    Article Title: The skeletal muscle slow myosin heavy chain regulates mammalian metabolic homeostasis through the NRF2 pathway

    doi: 10.1126/sciadv.aed2478

    Figure Lengend Snippet: ( A ) Venn diagram depicting the number of unique and shared proteins expressed in the Gas muscle of Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice at P0 ( n = 6). KO, knockout. ( B ) PCA plot of the Gas muscle from Pax +/+ , Myh7 fl/+ (red) and Pax3 cre/+ , Myh7 Δ/fl (green) mice at P0, where each dot represents a biological replicate ( n = 6). ( C ) Volcano plot showing up-regulated and down-regulated proteins in the Gas muscle from Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice at P0 ( n = 6). ( D ) Pathway analysis (Reactome database) of Gas muscle proteins from Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice at P0. ( E ) Heatmap depicting the NRF2 pathway target protein expression in the Gas muscle of Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice at P0 ( n = 6). ( F and G ) Representative Western blots for SOD1, GPx1, Prdx2, Prdx1, catalase, and α-tubulin (loading control) using protein lysates from the Gas muscle of P0 Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl , and Pax7 icre/+ , Myh7 Δ/fl mice (F) and their densitometry (G) ( n = 5). ( H to M ) Representative Western blots for NRF2, P-NRF2, and α-tubulin (loading control) using Gas and TA muscle protein lysates of P0 Pax +/+ , Myh7 fl/+ , Pax3 cre/+ , Myh7 Δ/fl , and Pax7 icre/+ , Myh7 Δ/fl mice (H and I) and their densitometry (J to M) ( n = 5). ( N and O ) Label-free quantitation (LFQ) intensity of DRP1 and FIS1 by mass spectrometry on P0 Gas muscle protein lysates of Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice ( n = 6). ( P ) Heatmap depicting the expression of mitochondrial proteins in the Gas muscle of P0 Pax +/+ , Myh7 fl/+ and Pax3 cre/+ , Myh7 Δ/fl mice ( n = 6). Data are presented as means ± SEM. * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, and **** P ≤ 0.0001.

    Article Snippet: The antibodies used for Western blotting were as follows: anti-mouse MyHC-IIa antibody (SC-71, Developmental Studies Hybridoma Bank) at 1:10 dilution; anti-mouse MyHC-IIb antibody (BFF3, Developmental Studies Hybridoma Bank) at 1:10; anti-mouse alpha-tubulin antibody (30021290, Cell Signaling Technology) at 1:10,000; anti-rabbit GAPDH antibody (PAB932Mu01, Cloud-Clone Corp) at 1:10,000; anti-rabbit Akt antibody (4641, Cell Signaling Technology) at 1:1000; anti-rabbit P-Akt S473 (4640, Cell Signaling Technology) at 1:1000; anti-rabbit Histone H3 antibody (Ab1741, Abcam) at 1:10,000; anti-rabbit troponin T1 antibody (NBP238855, Novus Biologicals) at 1:5000; anti-rabbit PGC-1α antibody (A12348, ABclonal; 66369, Proteintech; and 2178S, Cell Signaling Technology) at 1:2000, 1:2000, and 1:1000, respectively; anti-mouse total OXPHOS cocktail (ab110413, Abcam) at 1:1000; anti-rabbit DRP1 antibody (A21968, ABclonal) at 1:2000; anti-rabbit FIS1 antibody (A19666, ABclonal) at 1:2000; anti-rabbit mitofusin1 antibody (A9880, ABclonal) at 1:2000; anti-rabbit mitofusin2 antibody (A12771, ABclonal) at 1:2000; anti-rabbit GLUT4 (MA5-17176, Thermo Fisher Scientific) at 1:1000; anti-rabbit NRF2 antibody (A0674, ABclonal and 98020000, Proteintech) at 1:2000; anti-rabbit P-NRF2 antibody (AP1133, ABclonal) at 1:2000; anti-rabbit SOD1 antibody (A0274, ABclonal) at 1:2000; anti-rabbit Prdx1 antibody (A13524, ABclonal) at 1:2000; anti-rabbit Gpx1 antibody (A1110, ABclonal) at 1:1000; anti-rabbit catalase antibody (A11220, ABclonal) at 1:2000; anti-rabbit KEAP1 antibody (A1820, ABclonal) at 1:1000; anti-rabbit Tom20 antibody (HPA011582, Merck) at 1:2500, anti-rabbit VDAC1 antibody ( Ab154856 , Abcam) at 1:2500; anti-rabbit pDRP1 (S616) antibody (AP0849, ABclonal) at 1:2500; and anti-rabbit OPA1 antibody (A9833, ABclonal) at 1:2500.

    Techniques: Knock-Out, Expressing, Western Blot, Control, Quantitation Assay, Mass Spectrometry

    COPN restores mitochondrial quality control and interrupts the ROS‒cGAS‒inflammation axis in OGD/R-treated R28 cells. a , TEM images showing changes in the mitochondrial ultrastructure of R28 cells subjected to various treatments (PBS, PDNs, COPN-L, and COPN-H) after OGD/R. Scale bar: 500 nm b , Quantitative analyses of mitochondrial length and number in R28 cells as indicated in a . c , Representative fluorescence images showing JC-1 staining of the mitochondrial Δψm: aggregates (red) indicate healthy mitochondria, whereas monomers (green) represent depolarized mitochondria. Nuclei were stained with DAPI (blue). Scale bar: 50 μm d , Intracellular ATP content assay revealing improved energy production after COPN treatment under OGD/R stress conditions. e , mRNA expression analysis of mitochondrial dynamic regulatory genes (Opa1, Mfn2, Drp1, and Fis1) and mitochondrial DNA transcription levels (mt-ND1 and mt-COX1). f , Quantitative analysis of the JC-1 fluorescence ratio (aggregates/monomers) and mitochondrial ROS levels (MitoSOX staining). g–h , Western blot analysis of proteins involved in mitochondrial autophagy (Pink1, Parkin, and P62) (g) and mitochondrial fusion/fission (Opa1, Mfn2, Mfn1, Drp1, and Fis1) (h) . i , Confocal fluorescence microscopy images of mitochondria (green, MitoTracker) and lysosomes (red, LysoTracker) in R28 cells after different treatments. Nuclei were stained with Hoechst (blue). Scale bar: 50 μm ∗ ∗∗∗P < 0.0001. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Journal: Materials Today Bio

    Article Title: A dual-responsive CO-releasing nanogel ameliorates retinal ischemia–reperfusion injury by restoring mitochondrial homeostasis and attenuating cGAS-STING pathway activation

    doi: 10.1016/j.mtbio.2026.102974

    Figure Lengend Snippet: COPN restores mitochondrial quality control and interrupts the ROS‒cGAS‒inflammation axis in OGD/R-treated R28 cells. a , TEM images showing changes in the mitochondrial ultrastructure of R28 cells subjected to various treatments (PBS, PDNs, COPN-L, and COPN-H) after OGD/R. Scale bar: 500 nm b , Quantitative analyses of mitochondrial length and number in R28 cells as indicated in a . c , Representative fluorescence images showing JC-1 staining of the mitochondrial Δψm: aggregates (red) indicate healthy mitochondria, whereas monomers (green) represent depolarized mitochondria. Nuclei were stained with DAPI (blue). Scale bar: 50 μm d , Intracellular ATP content assay revealing improved energy production after COPN treatment under OGD/R stress conditions. e , mRNA expression analysis of mitochondrial dynamic regulatory genes (Opa1, Mfn2, Drp1, and Fis1) and mitochondrial DNA transcription levels (mt-ND1 and mt-COX1). f , Quantitative analysis of the JC-1 fluorescence ratio (aggregates/monomers) and mitochondrial ROS levels (MitoSOX staining). g–h , Western blot analysis of proteins involved in mitochondrial autophagy (Pink1, Parkin, and P62) (g) and mitochondrial fusion/fission (Opa1, Mfn2, Mfn1, Drp1, and Fis1) (h) . i , Confocal fluorescence microscopy images of mitochondria (green, MitoTracker) and lysosomes (red, LysoTracker) in R28 cells after different treatments. Nuclei were stained with Hoechst (blue). Scale bar: 50 μm ∗ ∗∗∗P < 0.0001. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Article Snippet: The following primary antibodies were used: Drp1 (CST, #8570, 1:1000, ∼80 kDa), Fis1 (Proteintech, 10956-1-AP, 1:1000, ∼17 kDa), Mfn1 (Abcam, ab104274, 1:1000, ∼84 kDa), Mfn2 (CST, #9482, 1:1000, ∼86 kDa), Opa1 (CST, #80471, 1:1000, ∼100–120 kDa), Pink1 (CST, #6946, 1:1000, ∼63 kDa), cGAS (CST, #15102, 1:1000, ∼60 kDa), STING (CST, #13647, 1:1000, ∼42–45 kDa), TBK1 (CST, #3013, 1:1000, ∼84 kDa), p-TBK1 (CST, #5483, 1:1000, ∼84 kDa), COX IV (Abcam, ab14744, 1:2000, ∼17 kDa), β-actin (Proteintech, 66009-1-Ig, 1:5000, ∼43 kDa), and GAPDH (Proteintech, 60004-1-Ig, 1:5000, After washing, the membranes were incubated with HRP-conjugated secondary antibodies (goat anti-rabbit or goat anti-mouse IgG, CST, 1:5000) for 1 h at room temperature.

    Techniques: Control, Fluorescence, Staining, Expressing, Western Blot, Microscopy