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anti myhc  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology anti myhc
    srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody <t>(anti-MyHC).</t> The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).
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    Images

    1) Product Images from "Loss of SREBF1 disrupts lipid signaling and causes slow muscle fiber degeneration"

    Article Title: Loss of SREBF1 disrupts lipid signaling and causes slow muscle fiber degeneration

    Journal: iScience

    doi: 10.1016/j.isci.2026.117447

    srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody (anti-MyHC). The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).
    Figure Legend Snippet: srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody (anti-MyHC). The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).

    Techniques Used: CRISPR, Knock-Out, Western Blot, Analysis, Expressing, Immunostaining, Gene Expression, RNA Sequencing, MANN-WHITNEY, Standard Deviation


    Figure Legend Snippet:

    Techniques Used: Cell-Signaling, Radio Immunoprecipitation, Lysis, Protease Inhibitor, Tissue, Microscopy, Knock-Out, Gene Knockout, Software, Micro-CT, Analysis

    Related Articles

    Incubation:

    Article Title: Biomimetic cell-actuated artificial muscle with nanofibrous bundles
    Article Snippet: .. Primary antibodies raised against skeletal muscle myosin (Santa Cruz, sc-32732) or α-actinin (Abcam, ab9465) were incubated overnight at 4 °C on a rotary shaker. .. One day later, the cell-laden fiber was washed thrice with phosphate buffer solution containing 0.5% Triton X-100 and subsequently incubated for 1 h at room temperature with Alexa Fluor 488-conjugated anti-mouse IgG (Invitrogen) and Hoechst 33342 (Invitrogen).

    Article Title: Detecting the Effects of the Glucocorticoid Dexamethasone on Primary Human Skeletal Muscle Cells—Differences to the Murine Cell Line
    Article Snippet: After two washing steps with PBS (Gibco ® InvitrogenTM Life Technologies, Carlsbad, CA, USA), cells were fixed and permeabilized with ice cold methanol for 20 min followed by several washing steps in PBS. .. Pax7 (ab199010, 1:200), Myf5 (M-18: sc-31949, 1:100), MyoD (M-318: sc-760, 1:150), and skeletal muscle Myosin (F59: sc-32732, 1:200, Santa Cruz Biotechnology, Dallas, TX, USA) were used as primary antibodies and incubated over night at 4 °C. .. After washing with 0.5% BSA/PBS cells were stained with Alexa Fluor ® 488 (A11001 and A11008, 1:200, InvitrogenTM Life Technologies, Carlsbad, CA, USA), (CyTM3-conjugated donkey anti-Goat IgG (H+L) 705-165-003, 1:450, Jackson Immuno Research Laboratories, Inc, West Grove, PA, USA) (1h) in the dark at room temperature.

    Article Title: Novel insights into the molecular mechanisms of LGMDD2: role of TNPO3 in experimental cell and zebrafish models
    Article Snippet: After three additional washes in PBST, non-specific binding sites were blocked by PBST containing 5% goat serum (Merck) for 1 h at room temperature with gentle rocking. .. Embryos were then incubated overnight at 4 °C with a specific monoclonal anti α-actinin (A7811, Merck) and anti skeletal muscle myosin (sc-32732, Santa Cruz) antibody in PBST with 1% goat serum. .. The next day, embryos were washed three times in PBST with gentle rocking and incubated overnight at 4 °C with a CyTM3 AffiniPure Goat Anti-Mouse IgG (H + L) secondary antibody (Jackson ImmunoResearch).

    Cell-Signaling:

    Article Title: Biophysical and Chemical Effects of Fibrin on Mesenchymal Stromal Cell Gene Expression
    Article Snippet: Briefly, samples were lysed in RIPA buffer (Pierce, Rockford, IL) at specified incubation periods, resolved by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and then transferred onto nitrocellulose membranes (Invitrogen). .. Primary antibodies consisted of FLK1 (Cell Signaling Technology, Danvers, MA), CNN1 (Millipore, Billerica, MA), MYF5 (Novus Biologicals, Littleton, CO), skeletal muscle myosin (Santa Cruz Biotechnology, Santa Cruz, CA) GFAP (Novus Biologicals), ACTA2 (Sigma), and total actin (Sigma). ..

    Sonication:

    Article Title: Spectrin is a mechanoresponsive protein shaping fusogenic synapse architecture during myoblast fusion
    Article Snippet: Briefly, approximately 3×10 5 cells were seeded on each well of a 6-well tissue culture dish and transfected with the individual siRNAs against βV-spectrin (10uM final concentration) using HiPerFect transfection reagent (Qiagen). .. The cell lysates were briefly sonicated, centrifuged, analyzed by SDS-PAGE and western blotting with antibodies against MyoD (1:100; sc-377460), Myogenin (1:100; sc-52903), skeletal muscle myosin (1:100; sc-32732) and α-tubulin (1:100; sc-58666) from Santa Cruz Biotechnology. .. Five days post-differentiation, cells were fixed and stained with anti-skeletal muscle myosin antibody (1:100; Santa Cruz Biotechnology; F59, sc-32732) to identify differentiated cells.

    SDS Page:

    Article Title: Spectrin is a mechanoresponsive protein shaping fusogenic synapse architecture during myoblast fusion
    Article Snippet: Briefly, approximately 3×10 5 cells were seeded on each well of a 6-well tissue culture dish and transfected with the individual siRNAs against βV-spectrin (10uM final concentration) using HiPerFect transfection reagent (Qiagen). .. The cell lysates were briefly sonicated, centrifuged, analyzed by SDS-PAGE and western blotting with antibodies against MyoD (1:100; sc-377460), Myogenin (1:100; sc-52903), skeletal muscle myosin (1:100; sc-32732) and α-tubulin (1:100; sc-58666) from Santa Cruz Biotechnology. .. Five days post-differentiation, cells were fixed and stained with anti-skeletal muscle myosin antibody (1:100; Santa Cruz Biotechnology; F59, sc-32732) to identify differentiated cells.

    Western Blot:

    Article Title: Spectrin is a mechanoresponsive protein shaping fusogenic synapse architecture during myoblast fusion
    Article Snippet: Briefly, approximately 3×10 5 cells were seeded on each well of a 6-well tissue culture dish and transfected with the individual siRNAs against βV-spectrin (10uM final concentration) using HiPerFect transfection reagent (Qiagen). .. The cell lysates were briefly sonicated, centrifuged, analyzed by SDS-PAGE and western blotting with antibodies against MyoD (1:100; sc-377460), Myogenin (1:100; sc-52903), skeletal muscle myosin (1:100; sc-32732) and α-tubulin (1:100; sc-58666) from Santa Cruz Biotechnology. .. Five days post-differentiation, cells were fixed and stained with anti-skeletal muscle myosin antibody (1:100; Santa Cruz Biotechnology; F59, sc-32732) to identify differentiated cells.

    other:

    Article Title: Skeletal Muscle Dysfunction in Experimental Pulmonary Hypertension
    Article Snippet: The following antibodies were used: skeletal muscle myosin (Santa Cruz Biotechnology, Dallas, TE, USA), Glut4 (Proteintech, Rosemont, IL, USA), Myomesin1 (Proteintech), Hexokinase II (Cell Signaling Technology), FoxO1 (Cell Signaling Technology), phospho-FoxO1 (Cell Signaling Technology) (rabbit), Histone H3 (Cell Signaling Technology), Glut1 (Cell Signaling Technology), GAPDH (Cell Signaling Technology), Vinculin (Cell Signaling Technology), Desmin (Milipore/Sigma-Aldrich), Troponin-I (Milipore/Sigma-Aldrich), b-Actin (mouse; Milipore/Sigma-Aldrich), anti-mouse HRP (GE Healthcare, Chicago, IL, USA), and anti-rabbit HRP (GE Healthcare).



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    Santa Cruz Biotechnology f59
    srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody <t>(anti-MyHC).</t> The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).
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    srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody (anti-MyHC). The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).

    Journal: iScience

    Article Title: Loss of SREBF1 disrupts lipid signaling and causes slow muscle fiber degeneration

    doi: 10.1016/j.isci.2026.117447

    Figure Lengend Snippet: srebf1 −/− ZF alters the organization of slow muscle fibers (A) CRISPR-Cas9-induced srebf1 knockout in whole-cell lysate fraction of ZF larvae at 7 days post fertilization (dpf) was confirmed by western blot analysis. (B) Quantification of relative expression units showed that levels of the mature form of Srebp1 protein were significantly reduced in srebf1 −/− ZF compared to srebf1 +/+ siblings (∗∗ p < 0.002). Whole-cell lysate was extracted with n = 10 animals per genotype, and reduced expression of Srebp1 was determined in two pools. (C) Whole-mount immunostaining of slow muscle myosin in 5 dpf ZF larvae was performed using F59 antibody (anti-MyHC). The slow muscle fibers of srebf1 −/− larvae were found to be disorganized and gaps between fibers alignments indicated by orange arrow heads (bottom) as compared to srebf1 +/+ siblings (top). (D) Shorter somites with non-significant alteration of pennation angle (not shown) were found in srebf1 knockout with respect to fish with no genetic perturbation (∗∗ p < 0.001). (E) Using DanioVision apparatus, locomotion tracking (15 min light on, 5 min light off/dark, 15 min light on) of both srebf1 +/+ and srebf1 −/− larvae ( n = 46 per group) was determined at 7 dpf. Knockout larvae traveled faster in dark conditions compared to srebf1 +/+ . One-way ANOVA. This figure complementary of summarizes the gene expression of slow muscle genes, such as sm y hc1 and sm y hc 2 is unaltered while upregulation of the slow muscle-associated metabolic gene tnnt1 ( p = 0.0056) was found in KO larvae; moreover, expression of muscle progenitors i.e., pax3a/b significantly ( p = 4.57–06 and p = 0.001, respectively) was increased in mining of RNA-seq data in srebf1 KO larvae. Each dot represents the total distance traveled by the larva or the number of quantifications. Magnification: 5×, Mann-Whitney statistical test, ∗∗ p = 0.0036. Data are presented as mean ± standard deviation (SD).

    Article Snippet: anti-Myhc , Santa Cruz Biotechnology , Cat#sc-32732.

    Techniques: CRISPR, Knock-Out, Western Blot, Analysis, Expressing, Immunostaining, Gene Expression, RNA Sequencing, MANN-WHITNEY, Standard Deviation

    Journal: iScience

    Article Title: Loss of SREBF1 disrupts lipid signaling and causes slow muscle fiber degeneration

    doi: 10.1016/j.isci.2026.117447

    Figure Lengend Snippet:

    Article Snippet: anti-Myhc , Santa Cruz Biotechnology , Cat#sc-32732.

    Techniques: Cell-Signaling, Radio Immunoprecipitation, Lysis, Protease Inhibitor, Tissue, Microscopy, Knock-Out, Gene Knockout, Software, Micro-CT, Analysis