rabbit anti-myod Search Results


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  • 99
    Millipore rabbit polyclonal anti myod
    Rabbit Polyclonal Anti Myod, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Santa Cruz Biotechnology rabbit anti myod
    IL34 is required for myogenic lineage progression in cultured SCs. a Fresh SCs were seeded, cultured in growth medium, and then induced to differentiate for various amounts of time. The immunoblots presented here reveal the protein levels of IL34, p-STAT3, STAT3, and unrelated β-tubulin in cultured SCs at different time points after initiation of differentiation. b SCs were isolated from the hindlimbs of WT mice using FACS, cultured in growth medium for 3 days, and treated with shIL34 lentivirus or control shRNA (shScr) for 36 h. The positively infected SCs were then purified by FACS according to the intrinsic enhanced green fluorescent protein (EGFP) fluorescence expressed by the lentivirus. Purified infected SCs were cultured for further analysis. c Western blot analysis of the levels of IL34, p-STAT3, STAT3, and an unrelated protein (GAPDH) in WT cell cultures after shScr and shIL34 treatment. d Western blot analysis of the levels of MyHC, <t>MyoD,</t> Pax7, and an unrelated protein (GAPDH) in WT cell cultures after shScr and shIL34 treatment. e Representative merged photomicrographs of SCs stably infected with a lentivirus expressing shIL34 or shScr that were induced to differentiate for one day and stained for Pax7 and DAPI. Scale bar: 30 μm. f Quantification of the percentage of Pax7 + SCs after shScr and shIL34 infection. *** P
    Rabbit Anti Myod, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 583 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rabbit polyclonal anti myod
    Pax-7 overexpression down regulates <t>MyoD</t> and myogenin. (A) MM14 cells and mouse satellite cells (sc) were transfected with a Pax-7 expression vector. Proliferating cells were fixed 24 h after the transfection and stained for MyoD and Pax-7. Cells overexpressing Pax-7 (yellow arrowheads) exhibited low or undetectable MyoD staining. The exposures selected for visualizing ectopic Pax-7 protein precluded detection of endogenous Pax-7. (B) MM14 cells and satellite cells (sc) were transfected and grown as described for A, induced to differentiate for 24 h, and then fixed and stained for Pax-7 and myogenin proteins. Under these conditions, nuclear myogenin is not detectable in Pax-7-overexpressing cells. Although we observe low levels of perinuclear myogenin staining, this is present in all undifferentiated myogenic cells used in this study and is specific for the Santa Cruz <t>polyclonal</t> antibody utilized (see Materials and methods). Scale bar = 12 μm.
    Rabbit Polyclonal Anti Myod, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rabbit anti mouse myod
    Marker expression in SC clones cultured under normoxia and hypoxia. Immunofluorescence analyses of LPC and HPC cultured for 5 days at 20% and 2% O 2 revealed differences in the expression of <t>MyoD,</t> <t>Myf5</t> (only at 2% O 2 ) and CD34. Phase-contrast and corresponding immunostaining examples for the specific marker (in red) merged with DAPI (left, scale bar = 100 µm, insets with higher magnification). Graphs indicate the percentage of marker-positive cells per clone (right, mean±SEM, * p
    Rabbit Anti Mouse Myod, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 55 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Abcam anti myod1 antibody
    Co-localization of the R D BAI1 mAb with antibodies to Noggin and <t>MyoD</t> in the skin and eyes. Tissue sections of human tattooed skin (A and B), human anterior lens tissue (C) and rabbit anterior cavity (D-I) were double labeled with the R D BAI1 mAb and antibodies to noggin or MyoD. The colors of the fluorescent secondary antibodies are indicated in each photograph. Overlap of red and green appears yellow in merged images. Nuclei were stained with Hoechst dye. Double labeled cells were present in the skin (A and B), anterior human lens tissue (C) and the rabbit lens (D and G), ciliary body (E and H) and cornea (F and I). Bar = 9 μM.
    Anti Myod1 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 96/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rabbit anti myod c 20
    Co-localization of the R D BAI1 mAb with antibodies to Noggin and <t>MyoD</t> in the skin and eyes. Tissue sections of human tattooed skin (A and B), human anterior lens tissue (C) and rabbit anterior cavity (D-I) were double labeled with the R D BAI1 mAb and antibodies to noggin or MyoD. The colors of the fluorescent secondary antibodies are indicated in each photograph. Overlap of red and green appears yellow in merged images. Nuclei were stained with Hoechst dye. Double labeled cells were present in the skin (A and B), anterior human lens tissue (C) and the rabbit lens (D and G), ciliary body (E and H) and cornea (F and I). Bar = 9 μM.
    Rabbit Anti Myod C 20, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore antibody 1 200
    Co-localization of the R D BAI1 mAb with antibodies to Noggin and <t>MyoD</t> in the skin and eyes. Tissue sections of human tattooed skin (A and B), human anterior lens tissue (C) and rabbit anterior cavity (D-I) were double labeled with the R D BAI1 mAb and antibodies to noggin or MyoD. The colors of the fluorescent secondary antibodies are indicated in each photograph. Overlap of red and green appears yellow in merged images. Nuclei were stained with Hoechst dye. Double labeled cells were present in the skin (A and B), anterior human lens tissue (C) and the rabbit lens (D and G), ciliary body (E and H) and cornea (F and I). Bar = 9 μM.
    Antibody 1 200, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rabbit polyclonal anti myod c 20
    Co-localization of the R D BAI1 mAb with antibodies to Noggin and <t>MyoD</t> in the skin and eyes. Tissue sections of human tattooed skin (A and B), human anterior lens tissue (C) and rabbit anterior cavity (D-I) were double labeled with the R D BAI1 mAb and antibodies to noggin or MyoD. The colors of the fluorescent secondary antibodies are indicated in each photograph. Overlap of red and green appears yellow in merged images. Nuclei were stained with Hoechst dye. Double labeled cells were present in the skin (A and B), anterior human lens tissue (C) and the rabbit lens (D and G), ciliary body (E and H) and cornea (F and I). Bar = 9 μM.
    Rabbit Polyclonal Anti Myod C 20, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti myod antibody
    <t>MyoD</t> expression and in vivo localization of human myoblasts and of human MRC after transplantation. Twenty-one days after human myoblasts or MRC intramuscular injection, muscle sections were stained ( a ) with anti-human lamin A/C (red) and anti-MyoD (green) mAb. In panel ( b ), muscle sections were stained with anti-human lamin A/C (green nuclei), <t>anti-laminin</t> (green) and anti-Pax7 (red). Nuclei were counterstained with DAPI (blue). Some human lamin A/C + Pax7 + myogenic cells (white arrow) were observed beneath the basal lamina protein, laminin.
    Rabbit Anti Myod Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Proteintech rabbit anti myod1
    <t>MyoD</t> expression and in vivo localization of human myoblasts and of human MRC after transplantation. Twenty-one days after human myoblasts or MRC intramuscular injection, muscle sections were stained ( a ) with anti-human lamin A/C (red) and anti-MyoD (green) mAb. In panel ( b ), muscle sections were stained with anti-human lamin A/C (green nuclei), <t>anti-laminin</t> (green) and anti-Pax7 (red). Nuclei were counterstained with DAPI (blue). Some human lamin A/C + Pax7 + myogenic cells (white arrow) were observed beneath the basal lamina protein, laminin.
    Rabbit Anti Myod1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc 9750 anti myod1
    <t>MyoD</t> expression and in vivo localization of human myoblasts and of human MRC after transplantation. Twenty-one days after human myoblasts or MRC intramuscular injection, muscle sections were stained ( a ) with anti-human lamin A/C (red) and anti-MyoD (green) mAb. In panel ( b ), muscle sections were stained with anti-human lamin A/C (green nuclei), <t>anti-laminin</t> (green) and anti-Pax7 (red). Nuclei were counterstained with DAPI (blue). Some human lamin A/C + Pax7 + myogenic cells (white arrow) were observed beneath the basal lamina protein, laminin.
    9750 Anti Myod1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti myod1
    miR-378a-3p activates myogenic differentiation. (A) Immunoblot experiments. RH30 cells transfected with miR-378a-3p mimics or miR-Ctr were analysed for the expression of myogenic differentiation markers. Increased levels of <t>MyoD1</t> (1.6-foldchange by densitometry), desmin and MyHC proteins and down-regulation of MyoR and Myf5 factors were evident. Tubulin served as protein loading control. (B) Immunofluorescence analysis. MiR-378a-3p ectopic expression evoked noticeable changes in RH30 cell morphology, a more organized actin and myosin arrangement, as visualised by TRITC-phalloidin staining, and a significant positivity for anti-MyHC antibody (100× magnification).
    Anti Myod1, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit a myod1
    miR-378a-3p activates myogenic differentiation. (A) Immunoblot experiments. RH30 cells transfected with miR-378a-3p mimics or miR-Ctr were analysed for the expression of myogenic differentiation markers. Increased levels of <t>MyoD1</t> (1.6-foldchange by densitometry), desmin and MyHC proteins and down-regulation of MyoR and Myf5 factors were evident. Tubulin served as protein loading control. (B) Immunofluorescence analysis. MiR-378a-3p ectopic expression evoked noticeable changes in RH30 cell morphology, a more organized actin and myosin arrangement, as visualised by TRITC-phalloidin staining, and a significant positivity for anti-MyHC antibody (100× magnification).
    Rabbit A Myod1, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    IL34 is required for myogenic lineage progression in cultured SCs. a Fresh SCs were seeded, cultured in growth medium, and then induced to differentiate for various amounts of time. The immunoblots presented here reveal the protein levels of IL34, p-STAT3, STAT3, and unrelated β-tubulin in cultured SCs at different time points after initiation of differentiation. b SCs were isolated from the hindlimbs of WT mice using FACS, cultured in growth medium for 3 days, and treated with shIL34 lentivirus or control shRNA (shScr) for 36 h. The positively infected SCs were then purified by FACS according to the intrinsic enhanced green fluorescent protein (EGFP) fluorescence expressed by the lentivirus. Purified infected SCs were cultured for further analysis. c Western blot analysis of the levels of IL34, p-STAT3, STAT3, and an unrelated protein (GAPDH) in WT cell cultures after shScr and shIL34 treatment. d Western blot analysis of the levels of MyHC, MyoD, Pax7, and an unrelated protein (GAPDH) in WT cell cultures after shScr and shIL34 treatment. e Representative merged photomicrographs of SCs stably infected with a lentivirus expressing shIL34 or shScr that were induced to differentiate for one day and stained for Pax7 and DAPI. Scale bar: 30 μm. f Quantification of the percentage of Pax7 + SCs after shScr and shIL34 infection. *** P

    Journal: Cell Death and Differentiation

    Article Title: Fate decision of satellite cell differentiation and self-renewal by miR-31-IL34 axis

    doi: 10.1038/s41418-019-0390-x

    Figure Lengend Snippet: IL34 is required for myogenic lineage progression in cultured SCs. a Fresh SCs were seeded, cultured in growth medium, and then induced to differentiate for various amounts of time. The immunoblots presented here reveal the protein levels of IL34, p-STAT3, STAT3, and unrelated β-tubulin in cultured SCs at different time points after initiation of differentiation. b SCs were isolated from the hindlimbs of WT mice using FACS, cultured in growth medium for 3 days, and treated with shIL34 lentivirus or control shRNA (shScr) for 36 h. The positively infected SCs were then purified by FACS according to the intrinsic enhanced green fluorescent protein (EGFP) fluorescence expressed by the lentivirus. Purified infected SCs were cultured for further analysis. c Western blot analysis of the levels of IL34, p-STAT3, STAT3, and an unrelated protein (GAPDH) in WT cell cultures after shScr and shIL34 treatment. d Western blot analysis of the levels of MyHC, MyoD, Pax7, and an unrelated protein (GAPDH) in WT cell cultures after shScr and shIL34 treatment. e Representative merged photomicrographs of SCs stably infected with a lentivirus expressing shIL34 or shScr that were induced to differentiate for one day and stained for Pax7 and DAPI. Scale bar: 30 μm. f Quantification of the percentage of Pax7 + SCs after shScr and shIL34 infection. *** P

    Article Snippet: The following primary antibodies were used: mouse anti-Pax7 (1:100, Developmental Studies Hybridoma Bank (DSHB), lowa City, IA), mouse anti-MyoD1 (1:100, DAKO), rabbit anti-MyoD (1:100, Santa Cruz, sc-760), mouse anti-MyoD (1:100, Santa Cruz, sc-32758), mouse anti-embryonic Myosin Heavy Chain BF-45/F1.652 (1:40, DSHB, lowa City, IA), rabbit anti-myogenin (1:200, Santa Cruz, sc-576), rabbit anti-laminin (1:1000, Sigma-Aldrich, L9393), and rabbit anti-Ki67 (1:500, Invitrogen).

    Techniques: Cell Culture, Western Blot, Isolation, Mouse Assay, FACS, shRNA, Infection, Purification, Fluorescence, Stable Transfection, Expressing, Staining

    Inactivation of miR-31 promotes the myogenic lineage progression of SCs. a WT and miR-31-KO SCs were cultured in growth medium for 4 days and then switched to differentiation medium and cultured for 1 day. The cells were then fixed and labeled with anti-MyoD and anti-Ki67 antibodies. DAPI was used to identify nuclei. Representative individual and overlaid images of WT and miR-31-KO cultures after labeling with MyoD, Ki67, and DAPI. Scale bars: 30 μm. b Percentage of MyoD + Ki67 − cells (normalized to MyoD + cells) in WT and miR-31-KO cell cultures. ** P

    Journal: Cell Death and Differentiation

    Article Title: Fate decision of satellite cell differentiation and self-renewal by miR-31-IL34 axis

    doi: 10.1038/s41418-019-0390-x

    Figure Lengend Snippet: Inactivation of miR-31 promotes the myogenic lineage progression of SCs. a WT and miR-31-KO SCs were cultured in growth medium for 4 days and then switched to differentiation medium and cultured for 1 day. The cells were then fixed and labeled with anti-MyoD and anti-Ki67 antibodies. DAPI was used to identify nuclei. Representative individual and overlaid images of WT and miR-31-KO cultures after labeling with MyoD, Ki67, and DAPI. Scale bars: 30 μm. b Percentage of MyoD + Ki67 − cells (normalized to MyoD + cells) in WT and miR-31-KO cell cultures. ** P

    Article Snippet: The following primary antibodies were used: mouse anti-Pax7 (1:100, Developmental Studies Hybridoma Bank (DSHB), lowa City, IA), mouse anti-MyoD1 (1:100, DAKO), rabbit anti-MyoD (1:100, Santa Cruz, sc-760), mouse anti-MyoD (1:100, Santa Cruz, sc-32758), mouse anti-embryonic Myosin Heavy Chain BF-45/F1.652 (1:40, DSHB, lowa City, IA), rabbit anti-myogenin (1:200, Santa Cruz, sc-576), rabbit anti-laminin (1:1000, Sigma-Aldrich, L9393), and rabbit anti-Ki67 (1:500, Invitrogen).

    Techniques: Cell Culture, Labeling

    Inhibiting intracellular BMP signal mediation promotes myogenic differentiation. To inhibit BMP signaling, we used either Dorsomorphin, an inhibitor of Smad1/5/8 phosphorylation, or siRNA to knockdown the R-Smad, Smad5, or Co-Smad, Smad4, levels. ( a ) EDL myofibres and their associated satellite cells were cultured with or without 1 μ M Dorsomorphin and the plating medium changed daily. Dorsomorphin markedly decreased the mean total number of cells per fibre, particularly the number of cells with the Pax7 + MyoD + phenotype. ( b ) Satellite cell-derived myoblasts were plated at high cell density (80–90% confluency) and cultured in proliferation medium for 2 days with or without Dorsomorphin. Immunostaining for MyHC showed that Dorsomorphin promoted myogenic differentiation and fusion in a dose-dependent manner. ( c and d ) Efficient siRNA-mediated knockdown of Smad5 or Smad4 was confirmed by immunostaining of plated satellite cells 24 h after transfection. ( e , quantified in f and g ) Co-immunostaining for MyHC and Ki67 after Smad5 or Smad4 silencing for 3 days in proliferation medium was sufficient to promote cell cycle exit and induce precocious differentiation, characterised by a decreased proportion of cells with Ki67 + expression and an increase in MyHC + cells and myotubes. Data are mean±S.E.M. ( a ) or mean±S.D. ( f and g ) from at least three independent experiments. Asterisk indicates that data are significantly different from control conditions ( P

    Journal: Cell Death and Differentiation

    Article Title: BMP signalling permits population expansion by preventing premature myogenic differentiation in muscle satellite cells

    doi: 10.1038/cdd.2010.95

    Figure Lengend Snippet: Inhibiting intracellular BMP signal mediation promotes myogenic differentiation. To inhibit BMP signaling, we used either Dorsomorphin, an inhibitor of Smad1/5/8 phosphorylation, or siRNA to knockdown the R-Smad, Smad5, or Co-Smad, Smad4, levels. ( a ) EDL myofibres and their associated satellite cells were cultured with or without 1 μ M Dorsomorphin and the plating medium changed daily. Dorsomorphin markedly decreased the mean total number of cells per fibre, particularly the number of cells with the Pax7 + MyoD + phenotype. ( b ) Satellite cell-derived myoblasts were plated at high cell density (80–90% confluency) and cultured in proliferation medium for 2 days with or without Dorsomorphin. Immunostaining for MyHC showed that Dorsomorphin promoted myogenic differentiation and fusion in a dose-dependent manner. ( c and d ) Efficient siRNA-mediated knockdown of Smad5 or Smad4 was confirmed by immunostaining of plated satellite cells 24 h after transfection. ( e , quantified in f and g ) Co-immunostaining for MyHC and Ki67 after Smad5 or Smad4 silencing for 3 days in proliferation medium was sufficient to promote cell cycle exit and induce precocious differentiation, characterised by a decreased proportion of cells with Ki67 + expression and an increase in MyHC + cells and myotubes. Data are mean±S.E.M. ( a ) or mean±S.D. ( f and g ) from at least three independent experiments. Asterisk indicates that data are significantly different from control conditions ( P

    Article Snippet: Rabbit anti-BMPR-1A (Alk-3) from Orbigen (San Diego, CA, USA) and a gift from Professor B. Kay; rat anti-Ki67 from DakoCytomation (Ely, Cambridgeshire, UK); goat anti-Smad5, mouse anti-Smad4, mouse anti-MyoD and rabbit anti-MyoD antibodies were obtained from Santa Cruz (Santa Cruz, USA); goat anti-Noggin antibody was obtained from R & D systems; mouse anti-MyHC (MF20), anti-Pax7, anti-myogenin (F5D) and anti- β -tubulin antibodies (E7) were supplied by the DSHB (Iowa City, IA, USA); rabbit anti-pSmad1/5/8 antibody was from Cell Signalling Technology (Beverly, MA, USA); goat anti-collagen type 1 antibody was acquired from Southern Biotech (Birmingham, AL, USA).

    Techniques: Cell Culture, Derivative Assay, Immunostaining, Transfection, Expressing

    BMPR-1A, pSmad 1/5/8, Smad4 and Smad 5 are upregulated during satellite cell activation. Isolated EDL myofibres with their associated satellite cells were either immediately fixed (T0) or cultured in plating medium for either 48 h (T48) or 72 h (T72) before fixation and immunostaining. ( a ) BMPR-1A was undetectable on the majority of Pax7 + quiescent cells at T0, but robustly expressed in both Pax7 + and Pax7 − cells at both T48 and T72. ( b ) Quiescent Pax7 + satellite cells (T0) did not contain pSmad1/5/8, whereas pSmad1/5/8 became readily detectable in the nuclei of proliferating Pax7 + cells at T48, and both Pax7 + and Pax7 − cells at T72. ( c ) In accordance with the dynamics of pSmad1/5/8 expression, Smad5 levels were very low/absent in quiescent satellite cells at T0, but upregulated in both proliferating Pax7 + and MyoD + cells at T48, as was Smad4. Arrows indicate the same satellite cell at each time point to aid comparison. Representative images from at least three independent experiments are shown. Scale bar equals 30 μ m

    Journal: Cell Death and Differentiation

    Article Title: BMP signalling permits population expansion by preventing premature myogenic differentiation in muscle satellite cells

    doi: 10.1038/cdd.2010.95

    Figure Lengend Snippet: BMPR-1A, pSmad 1/5/8, Smad4 and Smad 5 are upregulated during satellite cell activation. Isolated EDL myofibres with their associated satellite cells were either immediately fixed (T0) or cultured in plating medium for either 48 h (T48) or 72 h (T72) before fixation and immunostaining. ( a ) BMPR-1A was undetectable on the majority of Pax7 + quiescent cells at T0, but robustly expressed in both Pax7 + and Pax7 − cells at both T48 and T72. ( b ) Quiescent Pax7 + satellite cells (T0) did not contain pSmad1/5/8, whereas pSmad1/5/8 became readily detectable in the nuclei of proliferating Pax7 + cells at T48, and both Pax7 + and Pax7 − cells at T72. ( c ) In accordance with the dynamics of pSmad1/5/8 expression, Smad5 levels were very low/absent in quiescent satellite cells at T0, but upregulated in both proliferating Pax7 + and MyoD + cells at T48, as was Smad4. Arrows indicate the same satellite cell at each time point to aid comparison. Representative images from at least three independent experiments are shown. Scale bar equals 30 μ m

    Article Snippet: Rabbit anti-BMPR-1A (Alk-3) from Orbigen (San Diego, CA, USA) and a gift from Professor B. Kay; rat anti-Ki67 from DakoCytomation (Ely, Cambridgeshire, UK); goat anti-Smad5, mouse anti-Smad4, mouse anti-MyoD and rabbit anti-MyoD antibodies were obtained from Santa Cruz (Santa Cruz, USA); goat anti-Noggin antibody was obtained from R & D systems; mouse anti-MyHC (MF20), anti-Pax7, anti-myogenin (F5D) and anti- β -tubulin antibodies (E7) were supplied by the DSHB (Iowa City, IA, USA); rabbit anti-pSmad1/5/8 antibody was from Cell Signalling Technology (Beverly, MA, USA); goat anti-collagen type 1 antibody was acquired from Southern Biotech (Birmingham, AL, USA).

    Techniques: Activation Assay, Isolation, Cell Culture, Immunostaining, Expressing

    Pax-7 overexpression down regulates MyoD and myogenin. (A) MM14 cells and mouse satellite cells (sc) were transfected with a Pax-7 expression vector. Proliferating cells were fixed 24 h after the transfection and stained for MyoD and Pax-7. Cells overexpressing Pax-7 (yellow arrowheads) exhibited low or undetectable MyoD staining. The exposures selected for visualizing ectopic Pax-7 protein precluded detection of endogenous Pax-7. (B) MM14 cells and satellite cells (sc) were transfected and grown as described for A, induced to differentiate for 24 h, and then fixed and stained for Pax-7 and myogenin proteins. Under these conditions, nuclear myogenin is not detectable in Pax-7-overexpressing cells. Although we observe low levels of perinuclear myogenin staining, this is present in all undifferentiated myogenic cells used in this study and is specific for the Santa Cruz polyclonal antibody utilized (see Materials and methods). Scale bar = 12 μm.

    Journal: Developmental Biology

    Article Title: Pax-7 up-regulation inhibits myogenesis and cell cycle progression in satellite cells: a potential mechanism for self-renewal

    doi: 10.1016/j.ydbio.2004.08.015

    Figure Lengend Snippet: Pax-7 overexpression down regulates MyoD and myogenin. (A) MM14 cells and mouse satellite cells (sc) were transfected with a Pax-7 expression vector. Proliferating cells were fixed 24 h after the transfection and stained for MyoD and Pax-7. Cells overexpressing Pax-7 (yellow arrowheads) exhibited low or undetectable MyoD staining. The exposures selected for visualizing ectopic Pax-7 protein precluded detection of endogenous Pax-7. (B) MM14 cells and satellite cells (sc) were transfected and grown as described for A, induced to differentiate for 24 h, and then fixed and stained for Pax-7 and myogenin proteins. Under these conditions, nuclear myogenin is not detectable in Pax-7-overexpressing cells. Although we observe low levels of perinuclear myogenin staining, this is present in all undifferentiated myogenic cells used in this study and is specific for the Santa Cruz polyclonal antibody utilized (see Materials and methods). Scale bar = 12 μm.

    Article Snippet: Primary myoblasts, isolated fibers, and cultured cells were fixed in 4% paraformaldehyde for 20 min. Primary antibodies and dilutions used were as follows: Mouse monoclonal anti-Pax7 (Hybridoma Bank, Iowa University) at 1:5 (cell culture supernatant); mouse monoclonal anti-BrdU (BMB) at 1:10 (cell culture supernatant); chick polyclonal anti-syndecan-4 extracellular domain ( ) at 1:1000; rabbit polyclonal anti-MyoD (Santa Cruz) at 1:30; rabbit polyclonal anti-myogenin (Santa Cruz) at 1:30; rabbit polyclonal anti-c-met (Santa Cruz) at 1:30.

    Techniques: Over Expression, Transfection, Expressing, Plasmid Preparation, Staining

    Marker expression in SC clones cultured under normoxia and hypoxia. Immunofluorescence analyses of LPC and HPC cultured for 5 days at 20% and 2% O 2 revealed differences in the expression of MyoD, Myf5 (only at 2% O 2 ) and CD34. Phase-contrast and corresponding immunostaining examples for the specific marker (in red) merged with DAPI (left, scale bar = 100 µm, insets with higher magnification). Graphs indicate the percentage of marker-positive cells per clone (right, mean±SEM, * p

    Journal: PLoS ONE

    Article Title: Hypoxia Increases Mouse Satellite Cell Clone Proliferation Maintaining both In Vitro and In Vivo Heterogeneity and Myogenic Potential

    doi: 10.1371/journal.pone.0049860

    Figure Lengend Snippet: Marker expression in SC clones cultured under normoxia and hypoxia. Immunofluorescence analyses of LPC and HPC cultured for 5 days at 20% and 2% O 2 revealed differences in the expression of MyoD, Myf5 (only at 2% O 2 ) and CD34. Phase-contrast and corresponding immunostaining examples for the specific marker (in red) merged with DAPI (left, scale bar = 100 µm, insets with higher magnification). Graphs indicate the percentage of marker-positive cells per clone (right, mean±SEM, * p

    Article Snippet: 1∶20), rabbit anti-mouse Myf5 (Santa Cruz Biotechnology, dilution 1∶20), rabbit anti-mouse MyoD (Santa Cruz, dil.

    Techniques: Marker, Expressing, Clone Assay, Cell Culture, Immunofluorescence, Immunostaining

    Paracrine WISP1 secretion from young FAPs stimulates the myogenic commitment of aged MuSCs (A) Experimental overview of the in-vivo transplantation of FAPs in WISP1−/− recipient mice. (B and C) Quantification and representative images of Pax7+/MyoD+ MuSCs by immunofluorescence in muscle cross-sections of WISP1−/− mice at 4dpi, after intra-muscular injection of vehicle or FAPs freshly isolated from young, aged or WISP1−/− mice at 1 dpi. n≥3 mice per condition. (D) Experimental overview of the in-vivo transplantation of FAPs in aged WT recipient mice. (E) Quantification of the number of Pax7+/MyoD+ MuSCs by immunofluorescence in muscle cross-sections of aged WT mice at 4dpi, after intra-muscular injection of vehicle or FAPs freshly isolated from young, aged or WISP1−/− mice at 1 dpi. n≥4 mice per condition. (B and E) Data are represented as means ± S.E.M. p-values are *

    Journal: Cell stem cell

    Article Title: Aging Disrupts Muscle Stem Cell Function by Impairing Matricellular WISP1 Secretion from Fibro-Adipogenic Progenitors

    doi: 10.1016/j.stem.2018.12.014

    Figure Lengend Snippet: Paracrine WISP1 secretion from young FAPs stimulates the myogenic commitment of aged MuSCs (A) Experimental overview of the in-vivo transplantation of FAPs in WISP1−/− recipient mice. (B and C) Quantification and representative images of Pax7+/MyoD+ MuSCs by immunofluorescence in muscle cross-sections of WISP1−/− mice at 4dpi, after intra-muscular injection of vehicle or FAPs freshly isolated from young, aged or WISP1−/− mice at 1 dpi. n≥3 mice per condition. (D) Experimental overview of the in-vivo transplantation of FAPs in aged WT recipient mice. (E) Quantification of the number of Pax7+/MyoD+ MuSCs by immunofluorescence in muscle cross-sections of aged WT mice at 4dpi, after intra-muscular injection of vehicle or FAPs freshly isolated from young, aged or WISP1−/− mice at 1 dpi. n≥4 mice per condition. (B and E) Data are represented as means ± S.E.M. p-values are *

    Article Snippet: Mouse anti-mouse Pax7 (DHSB, purified), rabbit-anti mouse MyoD antibody (Santa-Cruz #sc-304 or Abcam # ab198251), rabbit-anti mouse Ki67 (Abcam #ab15580) and chicken anti-human laminin (Life Span Bioscience #LC-C96142-100) antibodies were used at 2.5 μg/ml, 1/100, 1/100 and 1/200 in blocking solution, respectively.

    Techniques: In Vivo, Transplantation Assay, Mouse Assay, Immunofluorescence, Injection, Isolation

    Co-localization of the R D BAI1 mAb with antibodies to Noggin and MyoD in the skin and eyes. Tissue sections of human tattooed skin (A and B), human anterior lens tissue (C) and rabbit anterior cavity (D-I) were double labeled with the R D BAI1 mAb and antibodies to noggin or MyoD. The colors of the fluorescent secondary antibodies are indicated in each photograph. Overlap of red and green appears yellow in merged images. Nuclei were stained with Hoechst dye. Double labeled cells were present in the skin (A and B), anterior human lens tissue (C) and the rabbit lens (D and G), ciliary body (E and H) and cornea (F and I). Bar = 9 μM.

    Journal: PLoS ONE

    Article Title: Brain-specific angiogenesis inhibitor 1 is expressed in the Myo/Nog cell lineage

    doi: 10.1371/journal.pone.0234792

    Figure Lengend Snippet: Co-localization of the R D BAI1 mAb with antibodies to Noggin and MyoD in the skin and eyes. Tissue sections of human tattooed skin (A and B), human anterior lens tissue (C) and rabbit anterior cavity (D-I) were double labeled with the R D BAI1 mAb and antibodies to noggin or MyoD. The colors of the fluorescent secondary antibodies are indicated in each photograph. Overlap of red and green appears yellow in merged images. Nuclei were stained with Hoechst dye. Double labeled cells were present in the skin (A and B), anterior human lens tissue (C) and the rabbit lens (D and G), ciliary body (E and H) and cornea (F and I). Bar = 9 μM.

    Article Snippet: Double labeling also was performed with the R & D BAI1 mAb and the anti-Noggin goat polyclonal antiserum (AF719; R & D Systems), anti-MyoD IgG1 mAb (MA5-12902, ThermoFisher Scientific, Rockford, IL), anti-MyoD rabbit polyclonal antiserum (ab203383, Abcam, Cambridge, MA), anti-NeuN IgG mAb (ab104224, Abcam), anti-GFAP IgG mAb (ab10062, Abcam) and anti-Iba1 rabbit mAb (ab178846, Abcam), all diluted 1:100.

    Techniques: Labeling, Staining

    MyoD expression and in vivo localization of human myoblasts and of human MRC after transplantation. Twenty-one days after human myoblasts or MRC intramuscular injection, muscle sections were stained ( a ) with anti-human lamin A/C (red) and anti-MyoD (green) mAb. In panel ( b ), muscle sections were stained with anti-human lamin A/C (green nuclei), anti-laminin (green) and anti-Pax7 (red). Nuclei were counterstained with DAPI (blue). Some human lamin A/C + Pax7 + myogenic cells (white arrow) were observed beneath the basal lamina protein, laminin.

    Journal: Scientific Reports

    Article Title: Human myogenic reserve cells are quiescent stem cells that contribute to muscle regeneration after intramuscular transplantation in immunodeficient mice

    doi: 10.1038/s41598-017-03703-y

    Figure Lengend Snippet: MyoD expression and in vivo localization of human myoblasts and of human MRC after transplantation. Twenty-one days after human myoblasts or MRC intramuscular injection, muscle sections were stained ( a ) with anti-human lamin A/C (red) and anti-MyoD (green) mAb. In panel ( b ), muscle sections were stained with anti-human lamin A/C (green nuclei), anti-laminin (green) and anti-Pax7 (red). Nuclei were counterstained with DAPI (blue). Some human lamin A/C + Pax7 + myogenic cells (white arrow) were observed beneath the basal lamina protein, laminin.

    Article Snippet: Sections were stained with the following primary antibodies, overnight at 4 °C: mouse anti human lamin A/C (human specific, 1:100, Santa Cruz Biotechnology), rabbit anti lamin A/C (human specific, 1:2000, Abcam), rabbit anti dystrophin (1:500, Abcam), mouse anti Pax7 (1:20; DSHB, Iowa, USA), mouse anti spectrin (human specific, 1:50, LifeSpan BioScience, Seattle, WA, USA), rabbit anti-MyoD antibody (1:500; Cell Signaling) and rabbit anti laminin (1:1000, Abcam).

    Techniques: Expressing, In Vivo, Transplantation Assay, Injection, Staining

    The proportion of Pax7 + /MyoD − cells in MRC population decreases with time in differentiation. ( a ) Cultures of human myoblasts exposed to DM 48 h, DM 96 h and DM 120 h, were fixed and stained with anti-MEF2 (red) anti-MyHC (green) or anti-Pax7 (red)/MyoD (green) mAb, and with DAPI (blue). Images shown are representative of 3 independent experiments. Scale bars: 20 μm. ( b ) Fusion indexes (number of nuclei counted in MyHC positive myotubes) were calculated 48 h, 96 h and 120 h after differentiation initiation. Fusion indexes were significantly increased at 96 h and 120 h as compared to 48 h with value of 70.8 ± 2%, 73 ± 2.3% and of 61.9 ± 2.2% respectively (mean ± SEM, n = 3; P

    Journal: Scientific Reports

    Article Title: Human myogenic reserve cells are quiescent stem cells that contribute to muscle regeneration after intramuscular transplantation in immunodeficient mice

    doi: 10.1038/s41598-017-03703-y

    Figure Lengend Snippet: The proportion of Pax7 + /MyoD − cells in MRC population decreases with time in differentiation. ( a ) Cultures of human myoblasts exposed to DM 48 h, DM 96 h and DM 120 h, were fixed and stained with anti-MEF2 (red) anti-MyHC (green) or anti-Pax7 (red)/MyoD (green) mAb, and with DAPI (blue). Images shown are representative of 3 independent experiments. Scale bars: 20 μm. ( b ) Fusion indexes (number of nuclei counted in MyHC positive myotubes) were calculated 48 h, 96 h and 120 h after differentiation initiation. Fusion indexes were significantly increased at 96 h and 120 h as compared to 48 h with value of 70.8 ± 2%, 73 ± 2.3% and of 61.9 ± 2.2% respectively (mean ± SEM, n = 3; P

    Article Snippet: Blots were incubated with the primary antibodies diluted in TTBS with 5% milk as follows: mouse anti myosin heavy chain (recognize all myosin heavy chain isoforms, MF20, 1/2000, Developmental Studies Hybridoma Bank, Iowa city, USA); mouse anti human Pax7 (1/300, Developmental Studies Hybridoma Bank), rabbit anti MyoD (1/500, Cell Signaling), rabbit anti Myf5 (1/200, Santa Cruz) and mouse anti α-tubulin (1/6000, Sigma).

    Techniques: Staining

    80% of human MRC are quiescent myogenic Pax7 + /MyoD − cells. ( a ) Immunofluorescence of human myoblasts cultures exposed to GM or to DM 48 h, fixed and stained with antibodies against Pax7 (red), MyoD (green) and DAPI (blue). Inserts display Ki67 staining (red). The proportion of Pax7 +/− /MyoD +/− cells in myoblasts, myotubes or MRC population, as established from the slide are represented in graph (mean ± SEM, n = 3). ( b ) Western blot analysis of human myoblasts, human myotubes and human MRC. Data are representative of 4 independent experiments for western blots and the graph plotted is the mean ± SEM of 4 independent experiments. Scale bars: 20 μm. ( c ) Cell cycle analysis of human myogenic cells determined by FACS. After trypsinisation, myoblasts and MRC were fixed, permeabilized and stained with Hoechst 33342 and anti-Ki67 mAb conjugated to AlexaFluor®647. Left upper panels IgG1κ AlexaFluor®647-labeled isotype control. Left lower panels: specific antibody labeling; the gates of G0/G1/S/G2/M for each population (human myoblasts or human MRC) are displayed. Right histogram: data shown are mean ± SEM of 3 independent experiments derived from flow cytometry analysis.

    Journal: Scientific Reports

    Article Title: Human myogenic reserve cells are quiescent stem cells that contribute to muscle regeneration after intramuscular transplantation in immunodeficient mice

    doi: 10.1038/s41598-017-03703-y

    Figure Lengend Snippet: 80% of human MRC are quiescent myogenic Pax7 + /MyoD − cells. ( a ) Immunofluorescence of human myoblasts cultures exposed to GM or to DM 48 h, fixed and stained with antibodies against Pax7 (red), MyoD (green) and DAPI (blue). Inserts display Ki67 staining (red). The proportion of Pax7 +/− /MyoD +/− cells in myoblasts, myotubes or MRC population, as established from the slide are represented in graph (mean ± SEM, n = 3). ( b ) Western blot analysis of human myoblasts, human myotubes and human MRC. Data are representative of 4 independent experiments for western blots and the graph plotted is the mean ± SEM of 4 independent experiments. Scale bars: 20 μm. ( c ) Cell cycle analysis of human myogenic cells determined by FACS. After trypsinisation, myoblasts and MRC were fixed, permeabilized and stained with Hoechst 33342 and anti-Ki67 mAb conjugated to AlexaFluor®647. Left upper panels IgG1κ AlexaFluor®647-labeled isotype control. Left lower panels: specific antibody labeling; the gates of G0/G1/S/G2/M for each population (human myoblasts or human MRC) are displayed. Right histogram: data shown are mean ± SEM of 3 independent experiments derived from flow cytometry analysis.

    Article Snippet: Blots were incubated with the primary antibodies diluted in TTBS with 5% milk as follows: mouse anti myosin heavy chain (recognize all myosin heavy chain isoforms, MF20, 1/2000, Developmental Studies Hybridoma Bank, Iowa city, USA); mouse anti human Pax7 (1/300, Developmental Studies Hybridoma Bank), rabbit anti MyoD (1/500, Cell Signaling), rabbit anti Myf5 (1/200, Santa Cruz) and mouse anti α-tubulin (1/6000, Sigma).

    Techniques: Immunofluorescence, Staining, Western Blot, Cell Cycle Assay, FACS, Labeling, Antibody Labeling, Derivative Assay, Flow Cytometry, Cytometry

    miR-378a-3p activates myogenic differentiation. (A) Immunoblot experiments. RH30 cells transfected with miR-378a-3p mimics or miR-Ctr were analysed for the expression of myogenic differentiation markers. Increased levels of MyoD1 (1.6-foldchange by densitometry), desmin and MyHC proteins and down-regulation of MyoR and Myf5 factors were evident. Tubulin served as protein loading control. (B) Immunofluorescence analysis. MiR-378a-3p ectopic expression evoked noticeable changes in RH30 cell morphology, a more organized actin and myosin arrangement, as visualised by TRITC-phalloidin staining, and a significant positivity for anti-MyHC antibody (100× magnification).

    Journal: BMC Cancer

    Article Title: Deep Sequencing the microRNA profile in rhabdomyosarcoma reveals down-regulation of miR-378 family members

    doi: 10.1186/1471-2407-14-880

    Figure Lengend Snippet: miR-378a-3p activates myogenic differentiation. (A) Immunoblot experiments. RH30 cells transfected with miR-378a-3p mimics or miR-Ctr were analysed for the expression of myogenic differentiation markers. Increased levels of MyoD1 (1.6-foldchange by densitometry), desmin and MyHC proteins and down-regulation of MyoR and Myf5 factors were evident. Tubulin served as protein loading control. (B) Immunofluorescence analysis. MiR-378a-3p ectopic expression evoked noticeable changes in RH30 cell morphology, a more organized actin and myosin arrangement, as visualised by TRITC-phalloidin staining, and a significant positivity for anti-MyHC antibody (100× magnification).

    Article Snippet: The following antibodies were incubated over-night at +4°C: anti-IGFR1 (Cell Signaling), anti-phospho-Akt (Cell Signaling), anti-MyoR(Santa Cruz Biotechnology), anti-MyOD1 (Millipore), anti-Myf5 (Millipore), anti-desmin (Millipore) and anti-MyHC (Millipore).

    Techniques: Transfection, Expressing, Immunofluorescence, Staining