mouse anti-myhc Search Results


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  • 96
    Thermo Fisher anti mouse mhc class ii
    Immunochemistry of muscles treated with rHyal- sk in the presence and absence of GET. Skeletal muscle FFPE sections were stained at 3h (d0), d7 and d14 after treatment with monoclonal antibodies specific for macrophages ( A , <t>F4/80)</t> and dendritic cells ( B , <t>MHC-II;</t> C , CD11c). Positive control samples were muscles treated with LPS. Negative control samples included skeletal muscle harvested from untreated mice. All sections were counterstained with hematoxylin and analysed by optical microscopy. 20× magnification. Scale bars, 50 μm. rHyal- sk , recombinant Hyal from Fidia Farmaceutici; bHyal, bovine Hyal from Sigma-Aldrich; Hyal + GET, electrotransfer after Hyal injection; LPS, lipopolysaccharide injection; NEG CTRL, untreated muscle.
    Anti Mouse Mhc Class Ii, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 131 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore monoclonal anti myosin skeletal fast antibody
    Immunochemistry of muscles treated with rHyal- sk in the presence and absence of GET. Skeletal muscle FFPE sections were stained at 3h (d0), d7 and d14 after treatment with monoclonal antibodies specific for macrophages ( A , <t>F4/80)</t> and dendritic cells ( B , <t>MHC-II;</t> C , CD11c). Positive control samples were muscles treated with LPS. Negative control samples included skeletal muscle harvested from untreated mice. All sections were counterstained with hematoxylin and analysed by optical microscopy. 20× magnification. Scale bars, 50 μm. rHyal- sk , recombinant Hyal from Fidia Farmaceutici; bHyal, bovine Hyal from Sigma-Aldrich; Hyal + GET, electrotransfer after Hyal injection; LPS, lipopolysaccharide injection; NEG CTRL, untreated muscle.
    Monoclonal Anti Myosin Skeletal Fast Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 837 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Developmental Studies Hybridoma Bank mouse anti myosin heavy chain
    MS induces a muscle type switch to slow-twitch fibers After crush injury and MS treatment, the quadriceps was retrieved and analyzed by western blot or histology. We found that the expression of muscle proteins was increased after MS treatment. (A) Desmin nearly doubled its expression levels, and (B) a specific increase in MyH type 1 could be detected. (C) No significant difference in MyH type 2 was found by WB. (D, E, F) Staining was performed with <t>anti-myosin-heavy-chain-slowtwitch/FITC-anti-mouse-IgM</t> (green), anti-myosin-heavy-chain-fast-twitch/Cy3-antimouse-IgG (red), and DAPI (blue). When compared with intact control quadriceps, no fiber type change was found in injured muscle without MS stimulation. (E) On the other hand, a shift to type 1 fibers was verified in MS-treated samples. (F) MyH type 1 expression was up to 3-fold higher in MS-treated samples than in native muscle. (G) As expected, a relative decrease in MyH type 2 was detected. +MS indicates magnetic stimulation treatment, whereas -MS represents the unstimulated controls (* P
    Mouse Anti Myosin Heavy Chain, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 91/100, based on 262 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore monoclonal anti myosin skeletal slow antibody
    <t>Myosin</t> heavy chain (MyHC) expression in parental C2C12 cells and C2C12-derived cells permanently expressing Wnt4. Parental C2C12 cells (a, b, e, and f) and W4-08 cells (c, d, g, and h) were cultured for 2 days in proliferation medium containing 10% fetal bovine serum (a–d), or in differentiation medium containing 2% horse serum (e–h), and then immunohistochemically stained with <t>anti-MyHC</t> <t>antibodies,</t> followed by counterstaining with DAPI. Spontaneous expression of <t>slow-type</t> MyHC was evident in W4-08 cells in proliferation medium and intensified in differentiation medium, although the proliferation rates were greatly reduced compared to those of the parental C2C12 cells, as observed in the reduced number of nuclei (blue).
    Monoclonal Anti Myosin Skeletal Slow Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 568 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bio-Rad mhc ii
    rHcSTP-1 suppressed both major histocompatibility complex <t>(MHC)</t> class-I and II on goat monocytes. Monocytes were cultured in the presence of control buffer, HisTag protein (pET32a), and multiple concentrations of rHcSTP-1 for 24 h. MHC-II expression was measured by flow <t>cytometric</t> analysis and calculated as the percentage of mean fluorescence intensity (MFI). (A) Histogram corresponds to one representative of three independent experiments. (B,C) Stagger offset showing expression level of MHCs on monocytes. (D,E) Bar graphs represent the MFI ± SD of controls. The data are representative of three independent experiments (*** p
    Mhc Ii, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 200 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Developmental Studies Hybridoma Bank mouse monoclonal anti myhc
    Effect of Lf on myoblast differentiation. (A) Myoblasts were cultured in differentiation medium containing Lf at various concentrations for six days. (B) Myoblasts were cultured in differentiation medium in the presence of Lf for six days (6 days) or in differentiation medium in the presence of Lf for one day and in the absence of Lf for the next 5 days (1 day). (A and B) The expression of <t>MyHC</t> and β-actin was analyzed by western blots. (C) Myoblasts were cultured in differentiation medium containing Lf (50 µg/ml). cDNA was synthesized and genes were amplified by polymerase chain reaction. (D) Myoblasts were transfected with control siRNA (siControl) or <t>LRP1</t> siRNA (siLRP1) and were differentiated in the presence of Lf (50 µg/ml) for three days. The expression of MyHC, LRP1, and GAPDH was analyzed by western blotting. (E) (Upper panel) Fixed cells were reacted with anti-MyHC antibody and a fluorescence-labeled secondary antibody (green). The nuclei were stained with DAPI (blue). (Lower panel) The fusion index was calculated. Statistically significant differences were determined by one-way ANOVA and Tukey's post-hoc test. *P
    Mouse Monoclonal Anti Myhc, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 88/100, based on 58 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Abcam mouse anti mhc
    The timing of the cardiac differentiation program is altered in TBX5-depleted embryos ( A ) RT-PCR analysis of the expression of heart-specific isoforms of <t>MHC,</t> <t>troponin</t> and tropomyosin; and skeletal muscle-specific genes MyoD and muscle actin, throughout early and mid-tadpole stages of development in CMO (‘C’) and T5MO (‘T’) stage-matched embryos. All samples are derived from a single batch of eggs, and identical results were achieved in at least two independent sets of experiments for each marker. EF1-Alpha was used as a loading control for all RT-PCR reactions. ( B–I ) Images depicting embryos injected with (B–E) CMO, or (F–I) T5MO and immunostained for Tmy, showing delayed expression of Tmy in the hearts of T5MO embryos. Shown are representative sibling embryos imaged at the indicated stages. White arrows denote expression of Tmy within the heart. ( J–Q ) Images of living cardiac actin:GFP transgenic embryos, showing a delay in the onset of cardiac actin expression in the heart. Representative sibling embryos obtained from a single batch of embryos were injected with (J – M) CMO or (N – Q) T5MO and imaged at the indicated stages. Shown is a representative pair of embryos, while identical results were observed in over 50 embryos. White arrows denote expression of GFP within the heart field.
    Mouse Anti Mhc, supplied by Abcam, used in various techniques. Bioz Stars score: 89/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Thermo Fisher anti mouse mhc class i
    MiR-17/20a enhances NK cell recognition by suppressing the expression of <t>MHC</t> <t>class</t> I
    Anti Mouse Mhc Class I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Miltenyi Biotec anti mhc class ii microbeads
    Stromal-derived factors inhibit DC RALDH expression. (a and b) BM from C57BL/6 mice was cultured with GM-CSF alone or in the presence of SNs derived from primary mouse skin lines (skin), 3T3 fibroblasts, or EL-4 cells. After 3 d, LPS was added and, 18 h later, cells were stained with ALD and CD11c to measure DC RALDH activity. (a) A representative contour plot depicting the expression of CD11c and ALD is shown with inset values indicating the percentage of CD11c + DCs that are ALD + . (b) BM was differentiated, as in a, with SNs at various concentrations. Bar graphs show the mean percentages of CD11c + DCs that are ALD + with SD. Data were pooled from between 2 and 18 experiments. (c) DCs were differentiated from BM with GM-CSF alone or in the presence of skin SN. Cells were treated with LPS at day 3. 16–18 h later, DCs were purified with anti-CD11c or <t>MHC</t> class II <t>microbeads</t> and analyzed for RALDH2 expression by real-time qPCR. RALDH2 expression was normalized to GAPDH. Shown is relative expression of RALDH2 by skin SN versus control DCs, with each dot representing an individual experiment and horizontal bars the pooled mean. (d) DCs were differentiated from BM with GM-CSF alone, or in the presence of skin SN. After 3 d, LPS was added and, 18 h later, MHC class II + DCs were purified, pulsed with NP 366–374 -peptide, and used to stimulate CFSE-labeled CD8 + F5 T cells. 4 d later, the expression of CCR9 and PSL was analyzed by flow cytometry. Dot plots show the expression of homing receptors versus CFSE on live (PI − ) TCR + cells. Inset values are the mean percentage of dividing T cells positive for each receptor pooled from between 7 and 17 experiments. (e) CD8 + F5 T cells were activated as in d. After 4 d, T cells were labeled with CFSE or CTO, pooled at a 1:1 ratio, and transferred into congenic B6.Ly5.1 recipients (∼2 × 10 6 /recipient) that had been primed with oxazolone and challenged on the ear. After 16–18 h, the relative frequency of donor (CD45.2 + ) T cells primed by control versus skin SN-conditioned DCs at the various sites was determined by flow cytometry. A representative contour plot gated on live (PI − ) CD45.2 + donor T cells is shown, where control T cells are labeled with CTO and skin SN DC-primed T cells with CFSE. Inset is the mean frequency of each population pooled from three independent experiments.
    Anti Mhc Class Ii Microbeads, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 95/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    R&D Systems myosin heavy chain antibody
    Stromal-derived factors inhibit DC RALDH expression. (a and b) BM from C57BL/6 mice was cultured with GM-CSF alone or in the presence of SNs derived from primary mouse skin lines (skin), 3T3 fibroblasts, or EL-4 cells. After 3 d, LPS was added and, 18 h later, cells were stained with ALD and CD11c to measure DC RALDH activity. (a) A representative contour plot depicting the expression of CD11c and ALD is shown with inset values indicating the percentage of CD11c + DCs that are ALD + . (b) BM was differentiated, as in a, with SNs at various concentrations. Bar graphs show the mean percentages of CD11c + DCs that are ALD + with SD. Data were pooled from between 2 and 18 experiments. (c) DCs were differentiated from BM with GM-CSF alone or in the presence of skin SN. Cells were treated with LPS at day 3. 16–18 h later, DCs were purified with anti-CD11c or <t>MHC</t> class II <t>microbeads</t> and analyzed for RALDH2 expression by real-time qPCR. RALDH2 expression was normalized to GAPDH. Shown is relative expression of RALDH2 by skin SN versus control DCs, with each dot representing an individual experiment and horizontal bars the pooled mean. (d) DCs were differentiated from BM with GM-CSF alone, or in the presence of skin SN. After 3 d, LPS was added and, 18 h later, MHC class II + DCs were purified, pulsed with NP 366–374 -peptide, and used to stimulate CFSE-labeled CD8 + F5 T cells. 4 d later, the expression of CCR9 and PSL was analyzed by flow cytometry. Dot plots show the expression of homing receptors versus CFSE on live (PI − ) TCR + cells. Inset values are the mean percentage of dividing T cells positive for each receptor pooled from between 7 and 17 experiments. (e) CD8 + F5 T cells were activated as in d. After 4 d, T cells were labeled with CFSE or CTO, pooled at a 1:1 ratio, and transferred into congenic B6.Ly5.1 recipients (∼2 × 10 6 /recipient) that had been primed with oxazolone and challenged on the ear. After 16–18 h, the relative frequency of donor (CD45.2 + ) T cells primed by control versus skin SN-conditioned DCs at the various sites was determined by flow cytometry. A representative contour plot gated on live (PI − ) CD45.2 + donor T cells is shown, where control T cells are labeled with CTO and skin SN DC-primed T cells with CFSE. Inset is the mean frequency of each population pooled from three independent experiments.
    Myosin Heavy Chain Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 96/100, based on 213 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore monoclonal anti myosin smooth antibody
    Increased expression of GATA-6 in obstruction-induced BSM hypertrophy in men with BPH. A: RNA was extracted from healthy (N) and BPH (B) human BSM tissues and subjected to RT-PCR for GATA-6 ( upper panel ) and GAPDH (lower panel) as control. B: Densitometric analysis of bands from A reported as GATA-6 expression relative to GAPDH. C: Nuclear protein was extracted from the same samples and subjected to immunoblotting. D: Densitometric analysis of bands in C presented as GATA-6 ( upper panel in C ) expression relative to nuclear protein p97 ( lower panel in C ). Data are from individual patients. E: Immunofluorescence images of endogenous GATA-6 in human BSM from healthy men ( upper panel ) and patients with BPH ( lower panel ). Human BSM tissue was stained with <t>anti-GATA-6</t> polyclonal <t>antibody</t> (1:100) followed by FITC-conjugated secondary antibody. The <t>smooth</t> muscle tissues were also stained with Cy3-conjugated smooth muscle <t>myosin</t> heavy-chain 1. Slides were mounted in VectaShield medium containing DAPI to counterstain nuclei. Original magnification, ×63. Scale bars = 20 μm.
    Monoclonal Anti Myosin Smooth Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    BioLegend apc anti mouse i a i e
    Increased expression of GATA-6 in obstruction-induced BSM hypertrophy in men with BPH. A: RNA was extracted from healthy (N) and BPH (B) human BSM tissues and subjected to RT-PCR for GATA-6 ( upper panel ) and GAPDH (lower panel) as control. B: Densitometric analysis of bands from A reported as GATA-6 expression relative to GAPDH. C: Nuclear protein was extracted from the same samples and subjected to immunoblotting. D: Densitometric analysis of bands in C presented as GATA-6 ( upper panel in C ) expression relative to nuclear protein p97 ( lower panel in C ). Data are from individual patients. E: Immunofluorescence images of endogenous GATA-6 in human BSM from healthy men ( upper panel ) and patients with BPH ( lower panel ). Human BSM tissue was stained with <t>anti-GATA-6</t> polyclonal <t>antibody</t> (1:100) followed by FITC-conjugated secondary antibody. The <t>smooth</t> muscle tissues were also stained with Cy3-conjugated smooth muscle <t>myosin</t> heavy-chain 1. Slides were mounted in VectaShield medium containing DAPI to counterstain nuclei. Original magnification, ×63. Scale bars = 20 μm.
    Apc Anti Mouse I A I E, supplied by BioLegend, used in various techniques. Bioz Stars score: 94/100, based on 85 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore monoclonal anti myosin skeletal fast alkaline phosphatase antibody
    Increased expression of GATA-6 in obstruction-induced BSM hypertrophy in men with BPH. A: RNA was extracted from healthy (N) and BPH (B) human BSM tissues and subjected to RT-PCR for GATA-6 ( upper panel ) and GAPDH (lower panel) as control. B: Densitometric analysis of bands from A reported as GATA-6 expression relative to GAPDH. C: Nuclear protein was extracted from the same samples and subjected to immunoblotting. D: Densitometric analysis of bands in C presented as GATA-6 ( upper panel in C ) expression relative to nuclear protein p97 ( lower panel in C ). Data are from individual patients. E: Immunofluorescence images of endogenous GATA-6 in human BSM from healthy men ( upper panel ) and patients with BPH ( lower panel ). Human BSM tissue was stained with <t>anti-GATA-6</t> polyclonal <t>antibody</t> (1:100) followed by FITC-conjugated secondary antibody. The <t>smooth</t> muscle tissues were also stained with Cy3-conjugated smooth muscle <t>myosin</t> heavy-chain 1. Slides were mounted in VectaShield medium containing DAPI to counterstain nuclei. Original magnification, ×63. Scale bars = 20 μm.
    Monoclonal Anti Myosin Skeletal Fast Alkaline Phosphatase Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher apc conjugated anti mouse mhc class ii
    Confocal microscopy of a live anesthetized mouse intradermally injected in the ear with <t>anti-MHC</t> class II reveals a significant decrease in the density of MHC class II + cells when locally irradiated. Two hours after intradermal injection of <t>APC-conjugated</t>
    Apc Conjugated Anti Mouse Mhc Class Ii, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Thermo Fisher anti hla antibodies
    Confocal microscopy of a live anesthetized mouse intradermally injected in the ear with <t>anti-MHC</t> class II reveals a significant decrease in the density of MHC class II + cells when locally irradiated. Two hours after intradermal injection of <t>APC-conjugated</t>
    Anti Hla Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 118 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher anti mouse mhc ii pe
    Flow cytometry strategy. Detection of T lymphocyte subpopulation and <t>MHC</t> molecules using flow cytometry technique (CD3 gated), a <t>CD4</t> + T lymphocytes (CD3 + CD4 + , region Q2). b CD8 + T lymphocytes (CD3 + CD8 + , region Q2). c MHC-I molecules (CD3 + MHC-I, region Q2). d . MHC-II molecules (CD3 + MHC-II, region Q2)
    Anti Mouse Mhc Ii Pe, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Miltenyi Biotec anti mhc class ii fitc
    Flow cytometry strategy. Detection of T lymphocyte subpopulation and <t>MHC</t> molecules using flow cytometry technique (CD3 gated), a <t>CD4</t> + T lymphocytes (CD3 + CD4 + , region Q2). b CD8 + T lymphocytes (CD3 + CD8 + , region Q2). c MHC-I molecules (CD3 + MHC-I, region Q2). d . MHC-II molecules (CD3 + MHC-II, region Q2)
    Anti Mhc Class Ii Fitc, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 93/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    BioLegend brilliant violet 785 anti mouse i a i e mhc ii
    Flow cytometry strategy. Detection of T lymphocyte subpopulation and <t>MHC</t> molecules using flow cytometry technique (CD3 gated), a <t>CD4</t> + T lymphocytes (CD3 + CD4 + , region Q2). b CD8 + T lymphocytes (CD3 + CD8 + , region Q2). c MHC-I molecules (CD3 + MHC-I, region Q2). d . MHC-II molecules (CD3 + MHC-II, region Q2)
    Brilliant Violet 785 Anti Mouse I A I E Mhc Ii, supplied by BioLegend, used in various techniques. Bioz Stars score: 94/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    BioLegend fitc anti mouse i a i e
    Flow cytometry strategy. Detection of T lymphocyte subpopulation and <t>MHC</t> molecules using flow cytometry technique (CD3 gated), a <t>CD4</t> + T lymphocytes (CD3 + CD4 + , region Q2). b CD8 + T lymphocytes (CD3 + CD8 + , region Q2). c MHC-I molecules (CD3 + MHC-I, region Q2). d . MHC-II molecules (CD3 + MHC-II, region Q2)
    Fitc Anti Mouse I A I E, supplied by BioLegend, used in various techniques. Bioz Stars score: 94/100, based on 88 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Developmental Studies Hybridoma Bank mouse anti myosin heavy chain myhc
    Flow cytometry strategy. Detection of T lymphocyte subpopulation and <t>MHC</t> molecules using flow cytometry technique (CD3 gated), a <t>CD4</t> + T lymphocytes (CD3 + CD4 + , region Q2). b CD8 + T lymphocytes (CD3 + CD8 + , region Q2). c MHC-I molecules (CD3 + MHC-I, region Q2). d . MHC-II molecules (CD3 + MHC-II, region Q2)
    Mouse Anti Myosin Heavy Chain Myhc, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 88/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore mouse anti myosin heavy chain
    Immunostaining of embryonic <t>myosin,</t> myosin <t>heavy</t> <t>chain,</t> and LaminAC+ nuclei in the fiber interior. (A) Sections of the excised defect site were stained with embryonic myosin (eMHC; red), human-specific LaminAC (cyan), and DAPI (blue). Inset ( left) : concentrations of eMHC were found in the center of the implanted fibers. Dotted line denotes fiber boundary. Inset (right) : Example of colocalizing eMHC+ and human LaminAC+ cell in fibers with induced ASCs. Images depict fibers at 4 weeks. (B) Sections of the excised defect site were stained with myosin heavy chain (MHC; red), human-specific LaminAC (cyan), and DAPI (blue). Inset: concentrations of MHC were found in the center of the implanted fibers. Dotted line denotes fiber boundary. Images depict fibers at 12 weeks. (C) Sections of the excised defect site were stained with laminin (red), human-specific LaminAC (cyan), and DAPI (blue). Inset: concentrations of laminin+ cells with human nuclei were found in the center of the implanted fibers. Dotted line denotes fiber boundary. Image depicts uninduced fibers at 4 weeks. (D) Quantification of the number of eMHC+ and MHC+ cells inside fibers among the three groups ( n =9–15). There were significantly more eMHC+ cells at 1 month in fibers with uninduced ASCs than in acellular fibers. There was no significant difference in eMHC expression among groups at 3 months. There were significantly more MHC+ cells at both 1 month and 3 months in fibers with uninduced ASCs than in acellular fibers. (E) Sections of the excised defect site were stained for <t>mouse</t> CD31 (red) and DAPI (blue). Inset: host vascular infiltration was found in the interior of the implanted fibers in all groups at 3 months. Dotted line denotes fiber boundary. *p
    Mouse Anti Myosin Heavy Chain, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 126 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore mouse igg2b monoclonal anti mhc type i
    Effects of Parkin knockout on muscle contractility and phenotype A , in situ specific force of the TA muscle of Park2 −/− and Park2 +/+ expressed as a function of the stimulation frequency ( n = 5 or 6). B , representative immunolabeling for <t>type</t> I (blue), type IIa (red) and type IIb (green) <t>MHC</t> of a gastrocnemius cross‐section of Park2 −/− (right) and Park2 +/+ (left) mice. Type IIx fibre, unstained on these images, shown in black. Laminin was also immunolabelled to highlight fibre borders (green line surrounding each muscle fibre). C , quantification of the overall fibre size of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). D , quantification of the fibre size distribution of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). E , quantification of the average fibre size for each fibre type of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). F , quantification of the fibre type proportion the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). Statistical analyses for data shown in ( A ), ( D ), ( E ) and ( F ) were performed using a two‐way ANOVA. Corrections for multiple comparisons were performed by controlling for the false discovery rate using the two‐stage method of Benjamini and Krieger and Yekutieli (with q
    Mouse Igg2b Monoclonal Anti Mhc Type I, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexafluor 700 anti mouse mhc ii
    Effects of Parkin knockout on muscle contractility and phenotype A , in situ specific force of the TA muscle of Park2 −/− and Park2 +/+ expressed as a function of the stimulation frequency ( n = 5 or 6). B , representative immunolabeling for <t>type</t> I (blue), type IIa (red) and type IIb (green) <t>MHC</t> of a gastrocnemius cross‐section of Park2 −/− (right) and Park2 +/+ (left) mice. Type IIx fibre, unstained on these images, shown in black. Laminin was also immunolabelled to highlight fibre borders (green line surrounding each muscle fibre). C , quantification of the overall fibre size of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). D , quantification of the fibre size distribution of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). E , quantification of the average fibre size for each fibre type of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). F , quantification of the fibre type proportion the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). Statistical analyses for data shown in ( A ), ( D ), ( E ) and ( F ) were performed using a two‐way ANOVA. Corrections for multiple comparisons were performed by controlling for the false discovery rate using the two‐stage method of Benjamini and Krieger and Yekutieli (with q
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    Thermo Fisher apc anti mouse mhc ii
    Effects of Parkin knockout on muscle contractility and phenotype A , in situ specific force of the TA muscle of Park2 −/− and Park2 +/+ expressed as a function of the stimulation frequency ( n = 5 or 6). B , representative immunolabeling for <t>type</t> I (blue), type IIa (red) and type IIb (green) <t>MHC</t> of a gastrocnemius cross‐section of Park2 −/− (right) and Park2 +/+ (left) mice. Type IIx fibre, unstained on these images, shown in black. Laminin was also immunolabelled to highlight fibre borders (green line surrounding each muscle fibre). C , quantification of the overall fibre size of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). D , quantification of the fibre size distribution of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). E , quantification of the average fibre size for each fibre type of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). F , quantification of the fibre type proportion the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). Statistical analyses for data shown in ( A ), ( D ), ( E ) and ( F ) were performed using a two‐way ANOVA. Corrections for multiple comparisons were performed by controlling for the false discovery rate using the two‐stage method of Benjamini and Krieger and Yekutieli (with q
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    Image Search Results


    Immunochemistry of muscles treated with rHyal- sk in the presence and absence of GET. Skeletal muscle FFPE sections were stained at 3h (d0), d7 and d14 after treatment with monoclonal antibodies specific for macrophages ( A , F4/80) and dendritic cells ( B , MHC-II; C , CD11c). Positive control samples were muscles treated with LPS. Negative control samples included skeletal muscle harvested from untreated mice. All sections were counterstained with hematoxylin and analysed by optical microscopy. 20× magnification. Scale bars, 50 μm. rHyal- sk , recombinant Hyal from Fidia Farmaceutici; bHyal, bovine Hyal from Sigma-Aldrich; Hyal + GET, electrotransfer after Hyal injection; LPS, lipopolysaccharide injection; NEG CTRL, untreated muscle.

    Journal: Cancers

    Article Title: In Vivo Evaluation of a New Recombinant Hyaluronidase to Improve Gene Electro-Transfer Protocols for DNA-Based Drug Delivery against Cancer

    doi: 10.3390/cancers10110405

    Figure Lengend Snippet: Immunochemistry of muscles treated with rHyal- sk in the presence and absence of GET. Skeletal muscle FFPE sections were stained at 3h (d0), d7 and d14 after treatment with monoclonal antibodies specific for macrophages ( A , F4/80) and dendritic cells ( B , MHC-II; C , CD11c). Positive control samples were muscles treated with LPS. Negative control samples included skeletal muscle harvested from untreated mice. All sections were counterstained with hematoxylin and analysed by optical microscopy. 20× magnification. Scale bars, 50 μm. rHyal- sk , recombinant Hyal from Fidia Farmaceutici; bHyal, bovine Hyal from Sigma-Aldrich; Hyal + GET, electrotransfer after Hyal injection; LPS, lipopolysaccharide injection; NEG CTRL, untreated muscle.

    Article Snippet: Sections were incubated in a humid chamber overnight at 4 °C with the following primary antibodies used at 1:50 dilution in blocking buffer: anti-mouse F4/80 clone BM8, anti-mouse MHC class II clone M5/114.15.2, and anti-mouse CD11c, clone N418 (eBioscience, San Diego, CA, USA).

    Techniques: Formalin-fixed Paraffin-Embedded, Staining, Positive Control, Negative Control, Mouse Assay, Microscopy, Recombinant, Electrotransfer, Injection

    MS induces a muscle type switch to slow-twitch fibers After crush injury and MS treatment, the quadriceps was retrieved and analyzed by western blot or histology. We found that the expression of muscle proteins was increased after MS treatment. (A) Desmin nearly doubled its expression levels, and (B) a specific increase in MyH type 1 could be detected. (C) No significant difference in MyH type 2 was found by WB. (D, E, F) Staining was performed with anti-myosin-heavy-chain-slowtwitch/FITC-anti-mouse-IgM (green), anti-myosin-heavy-chain-fast-twitch/Cy3-antimouse-IgG (red), and DAPI (blue). When compared with intact control quadriceps, no fiber type change was found in injured muscle without MS stimulation. (E) On the other hand, a shift to type 1 fibers was verified in MS-treated samples. (F) MyH type 1 expression was up to 3-fold higher in MS-treated samples than in native muscle. (G) As expected, a relative decrease in MyH type 2 was detected. +MS indicates magnetic stimulation treatment, whereas -MS represents the unstimulated controls (* P

    Journal: Muscle & nerve

    Article Title: Magnetic stimulation supports muscle and nerve regeneration after trauma in mice

    doi: 10.1002/mus.24780

    Figure Lengend Snippet: MS induces a muscle type switch to slow-twitch fibers After crush injury and MS treatment, the quadriceps was retrieved and analyzed by western blot or histology. We found that the expression of muscle proteins was increased after MS treatment. (A) Desmin nearly doubled its expression levels, and (B) a specific increase in MyH type 1 could be detected. (C) No significant difference in MyH type 2 was found by WB. (D, E, F) Staining was performed with anti-myosin-heavy-chain-slowtwitch/FITC-anti-mouse-IgM (green), anti-myosin-heavy-chain-fast-twitch/Cy3-antimouse-IgG (red), and DAPI (blue). When compared with intact control quadriceps, no fiber type change was found in injured muscle without MS stimulation. (E) On the other hand, a shift to type 1 fibers was verified in MS-treated samples. (F) MyH type 1 expression was up to 3-fold higher in MS-treated samples than in native muscle. (G) As expected, a relative decrease in MyH type 2 was detected. +MS indicates magnetic stimulation treatment, whereas -MS represents the unstimulated controls (* P

    Article Snippet: The primary antibodies were mouse anti-Desmin (1:500, BD Biosciences), mouse anti-myosin-heavy-chain (1:50, DSHB, Yowa), mouse anti-myosin-heavy-chain I (1:25, DSHB, Yowa), mouse anti-myosin-heavy-chain II (1:25, DSHB, Yowa), mouse PGP9.5-Neuronal Marker (1:2000, Abcam), anti-neurofilament 68 (1:1000, Sigma), rabbit anti-Agrin (1:200, Santa Cruz), and monoclonal anti-GAPDH (1:2000, Sigma).

    Techniques: Mass Spectrometry, Western Blot, Expressing, Staining

    Myosin heavy chain (MyHC) expression in parental C2C12 cells and C2C12-derived cells permanently expressing Wnt4. Parental C2C12 cells (a, b, e, and f) and W4-08 cells (c, d, g, and h) were cultured for 2 days in proliferation medium containing 10% fetal bovine serum (a–d), or in differentiation medium containing 2% horse serum (e–h), and then immunohistochemically stained with anti-MyHC antibodies, followed by counterstaining with DAPI. Spontaneous expression of slow-type MyHC was evident in W4-08 cells in proliferation medium and intensified in differentiation medium, although the proliferation rates were greatly reduced compared to those of the parental C2C12 cells, as observed in the reduced number of nuclei (blue).

    Journal: International Journal of Cell Biology

    Article Title: Interaction of Wnt Signaling with BMP/Smad Signaling during the Transition from Cell Proliferation to Myogenic Differentiation in Mouse Myoblast-Derived Cells

    doi: 10.1155/2013/616294

    Figure Lengend Snippet: Myosin heavy chain (MyHC) expression in parental C2C12 cells and C2C12-derived cells permanently expressing Wnt4. Parental C2C12 cells (a, b, e, and f) and W4-08 cells (c, d, g, and h) were cultured for 2 days in proliferation medium containing 10% fetal bovine serum (a–d), or in differentiation medium containing 2% horse serum (e–h), and then immunohistochemically stained with anti-MyHC antibodies, followed by counterstaining with DAPI. Spontaneous expression of slow-type MyHC was evident in W4-08 cells in proliferation medium and intensified in differentiation medium, although the proliferation rates were greatly reduced compared to those of the parental C2C12 cells, as observed in the reduced number of nuclei (blue).

    Article Snippet: After three washes with PBS, cells were immunohistochemically stained as previously described [ ], using anti-fast myosin heavy chain (M4276, Sigma-Aldrich, Saint Louis, MO, USA), anti-slow myosin heavy chain (M8421, Sigma-Aldrich), anti-troponin T (MAB1487, clone TT-98, Abnova, Walnut, CA, USA), anti-β-catenin (C2206, Sigma-Aldrich), anti-phospho-Smad1/5, and anti-phospho- (Ser10) histone H3 (382159, Calbiochem, Millipore) antibodies at 1 : 100, 1 : 200, 1 : 40, 1 : 200, 1 : 1000, and 1 : 500 dilutions, respectively.

    Techniques: Expressing, Derivative Assay, Cell Culture, Staining

    rHcSTP-1 suppressed both major histocompatibility complex (MHC) class-I and II on goat monocytes. Monocytes were cultured in the presence of control buffer, HisTag protein (pET32a), and multiple concentrations of rHcSTP-1 for 24 h. MHC-II expression was measured by flow cytometric analysis and calculated as the percentage of mean fluorescence intensity (MFI). (A) Histogram corresponds to one representative of three independent experiments. (B,C) Stagger offset showing expression level of MHCs on monocytes. (D,E) Bar graphs represent the MFI ± SD of controls. The data are representative of three independent experiments (*** p

    Journal: Frontiers in Immunology

    Article Title: The Serine/Threonine-Protein Phosphatase 1 From Haemonchus contortus Is Actively Involved in Suppressive Regulatory Roles on Immune Functions of Goat Peripheral Blood Mononuclear Cells

    doi: 10.3389/fimmu.2018.01627

    Figure Lengend Snippet: rHcSTP-1 suppressed both major histocompatibility complex (MHC) class-I and II on goat monocytes. Monocytes were cultured in the presence of control buffer, HisTag protein (pET32a), and multiple concentrations of rHcSTP-1 for 24 h. MHC-II expression was measured by flow cytometric analysis and calculated as the percentage of mean fluorescence intensity (MFI). (A) Histogram corresponds to one representative of three independent experiments. (B,C) Stagger offset showing expression level of MHCs on monocytes. (D,E) Bar graphs represent the MFI ± SD of controls. The data are representative of three independent experiments (*** p

    Article Snippet: The purified monocytes were incubated in 24-well culture plates with different concentrations of rHcSTP-1 (treatment group) or pET32a protein and PBS (control group) at 37°C for 24 h. Subsequently, the monocytes were marked with monoclonal antibodies MHC-I (MCA2189A647, AbDserotec, Bio-Rad, USA) and MHC-II (MCA2225PE, AbDserotec), followed by flow cytometric analysis at FACS Calibur cytometer (BD Biosciences, San Jose, CA, USA) (Figure A).

    Techniques: Cell Culture, Expressing, Flow Cytometry, Fluorescence

    Effect of Lf on myoblast differentiation. (A) Myoblasts were cultured in differentiation medium containing Lf at various concentrations for six days. (B) Myoblasts were cultured in differentiation medium in the presence of Lf for six days (6 days) or in differentiation medium in the presence of Lf for one day and in the absence of Lf for the next 5 days (1 day). (A and B) The expression of MyHC and β-actin was analyzed by western blots. (C) Myoblasts were cultured in differentiation medium containing Lf (50 µg/ml). cDNA was synthesized and genes were amplified by polymerase chain reaction. (D) Myoblasts were transfected with control siRNA (siControl) or LRP1 siRNA (siLRP1) and were differentiated in the presence of Lf (50 µg/ml) for three days. The expression of MyHC, LRP1, and GAPDH was analyzed by western blotting. (E) (Upper panel) Fixed cells were reacted with anti-MyHC antibody and a fluorescence-labeled secondary antibody (green). The nuclei were stained with DAPI (blue). (Lower panel) The fusion index was calculated. Statistically significant differences were determined by one-way ANOVA and Tukey's post-hoc test. *P

    Journal: Molecular Medicine Reports

    Article Title: Lactoferrin promotes murine C2C12 myoblast proliferation and differentiation and myotube hypertrophy

    doi: 10.3892/mmr.2018.8603

    Figure Lengend Snippet: Effect of Lf on myoblast differentiation. (A) Myoblasts were cultured in differentiation medium containing Lf at various concentrations for six days. (B) Myoblasts were cultured in differentiation medium in the presence of Lf for six days (6 days) or in differentiation medium in the presence of Lf for one day and in the absence of Lf for the next 5 days (1 day). (A and B) The expression of MyHC and β-actin was analyzed by western blots. (C) Myoblasts were cultured in differentiation medium containing Lf (50 µg/ml). cDNA was synthesized and genes were amplified by polymerase chain reaction. (D) Myoblasts were transfected with control siRNA (siControl) or LRP1 siRNA (siLRP1) and were differentiated in the presence of Lf (50 µg/ml) for three days. The expression of MyHC, LRP1, and GAPDH was analyzed by western blotting. (E) (Upper panel) Fixed cells were reacted with anti-MyHC antibody and a fluorescence-labeled secondary antibody (green). The nuclei were stained with DAPI (blue). (Lower panel) The fusion index was calculated. Statistically significant differences were determined by one-way ANOVA and Tukey's post-hoc test. *P

    Article Snippet: The supernatants were subjected to SDS-polyacrylamide gel electrophoresis, followed by western blot analysis with the following primary antibodies: rabbit polyclonal anti-p-ERK1/2 (Thr202/Thr204; Cell Signaling Technology, Inc., Danvers, MA, USA), anti-ERK1/2 (Cell Signaling Technology, Inc.), rabbit monoclonal anti-LRP1 (Abcam, Cambridge, UK), mouse monoclonal anti-MyHC (clone MF20; Developmental Studies Hybridoma Bank, University of Iowa, Iowa city, IA, USA), and anti-β-actin (Abgent, San Diego, CA, USA).

    Techniques: Cell Culture, Expressing, Western Blot, Synthesized, Amplification, Polymerase Chain Reaction, Transfection, Fluorescence, Labeling, Staining

    The timing of the cardiac differentiation program is altered in TBX5-depleted embryos ( A ) RT-PCR analysis of the expression of heart-specific isoforms of MHC, troponin and tropomyosin; and skeletal muscle-specific genes MyoD and muscle actin, throughout early and mid-tadpole stages of development in CMO (‘C’) and T5MO (‘T’) stage-matched embryos. All samples are derived from a single batch of eggs, and identical results were achieved in at least two independent sets of experiments for each marker. EF1-Alpha was used as a loading control for all RT-PCR reactions. ( B–I ) Images depicting embryos injected with (B–E) CMO, or (F–I) T5MO and immunostained for Tmy, showing delayed expression of Tmy in the hearts of T5MO embryos. Shown are representative sibling embryos imaged at the indicated stages. White arrows denote expression of Tmy within the heart. ( J–Q ) Images of living cardiac actin:GFP transgenic embryos, showing a delay in the onset of cardiac actin expression in the heart. Representative sibling embryos obtained from a single batch of embryos were injected with (J – M) CMO or (N – Q) T5MO and imaged at the indicated stages. Shown is a representative pair of embryos, while identical results were observed in over 50 embryos. White arrows denote expression of GFP within the heart field.

    Journal: Development (Cambridge, England)

    Article Title: TBX5 is required for embryonic cardiac cell cycle progression

    doi: 10.1242/dev.02420

    Figure Lengend Snippet: The timing of the cardiac differentiation program is altered in TBX5-depleted embryos ( A ) RT-PCR analysis of the expression of heart-specific isoforms of MHC, troponin and tropomyosin; and skeletal muscle-specific genes MyoD and muscle actin, throughout early and mid-tadpole stages of development in CMO (‘C’) and T5MO (‘T’) stage-matched embryos. All samples are derived from a single batch of eggs, and identical results were achieved in at least two independent sets of experiments for each marker. EF1-Alpha was used as a loading control for all RT-PCR reactions. ( B–I ) Images depicting embryos injected with (B–E) CMO, or (F–I) T5MO and immunostained for Tmy, showing delayed expression of Tmy in the hearts of T5MO embryos. Shown are representative sibling embryos imaged at the indicated stages. White arrows denote expression of Tmy within the heart. ( J–Q ) Images of living cardiac actin:GFP transgenic embryos, showing a delay in the onset of cardiac actin expression in the heart. Representative sibling embryos obtained from a single batch of embryos were injected with (J – M) CMO or (N – Q) T5MO and imaged at the indicated stages. Shown is a representative pair of embryos, while identical results were observed in over 50 embryos. White arrows denote expression of GFP within the heart field.

    Article Snippet: Cryostat sections (14 μm) were rinsed with wash buffer (PBS with 1% Triton and 1% heat inactivated calf serum), and incubated at 4°C overnight, as indicated, with mouse anti-tropomyosin 1:50, mouse anti-troponin 1:20, mouse anti-fibrillin 1:50 (all from Developmental Studies Hybridoma Bank), mouse anti-MHC (Abcam) rabbit anti-fibronectin 1:50 (Sigma), rabbit anti- Beta-catenin all at 1:1000 (Sigma), rabbit anti-phosphohistone H3 1:50 (Upstate) and rabbit anti-cleaved caspase 3 1:50 (Cell Signaling).

    Techniques: Reverse Transcription Polymerase Chain Reaction, Expressing, Derivative Assay, Marker, Injection, Transgenic Assay

    TBX5 depletion leads to a disruption in cardiac myofibril structure Cardiomyocyte structure in transverse sections through the hearts of (A,C,E,G) CMO or (B,D,F,H) T5MO stage 37 embryos, as detected by immunostaining for ( A , B ) cardiac troponin T (cTNT), ( C , D ) MHC, ( E , F ) actin or ( G , H ) Tmy. (I,K,M) Stage 37 CMO or (J,L,N) T5MO embryos double-immunostained for tropomyosin (green) and ( I , J ) fibronectin, ( K , L ) fibrillin or ( M , N ) β-catenin, all shown in red. Note increase in fibrillin staining on the walls of the chamber of T5MO hearts relative to CMO (compare panel K to L, white arrows) and ectoptic expression of fibronectin, shown by white arrow, in the dorsal portion of the heart in panel J relative to panel I. ( O , P ) High magnification confocal images of hearts from (O) CMO or (P) T5MO stage 37 embryos. Note that formation of organized cardiac muscle bundles in T5MO hearts is limited to a single cluster adjacent to the cardiac lumen. ( Q – S ) Representative transmission electron micrographs of transverse images of stage 37 embryos taken from (Q) CMO cardiac tissue or (R) T5MO cardiac tissue adjacent to the pericardial cavity and (S) T5MO cardiac tissue adjacent to the cardiac lumen. Cardiac muscle fibrils are shown pseudo-colored in yellow. Note that sarcomeres in T5MO hearts can only be identified adjacent to the cardiac lumen (compare R with S) and only found in concentric arrays. By contrast, CMO-derived hearts show both longitudinal and concentric arrays (compare Q with S). High-magnification TEM images reveal the ultrastructures of ( T ) CMO and ( U ) T5MO cardiac sarcomeres. Arrows denote A-bands. Note the smaller, non-continuous A-bands in the T5MO-derived sarcomeres (U). ( V ) Traces of the heart sections from CMO and T5MO embryos imaged by TEM are depicted schematically. Yellow circles represent the location of TEM imaging. Scale bars: 50 μm in A–N; 2 μm in Q–S; 0.2 μm in T,U.

    Journal: Development (Cambridge, England)

    Article Title: TBX5 is required for embryonic cardiac cell cycle progression

    doi: 10.1242/dev.02420

    Figure Lengend Snippet: TBX5 depletion leads to a disruption in cardiac myofibril structure Cardiomyocyte structure in transverse sections through the hearts of (A,C,E,G) CMO or (B,D,F,H) T5MO stage 37 embryos, as detected by immunostaining for ( A , B ) cardiac troponin T (cTNT), ( C , D ) MHC, ( E , F ) actin or ( G , H ) Tmy. (I,K,M) Stage 37 CMO or (J,L,N) T5MO embryos double-immunostained for tropomyosin (green) and ( I , J ) fibronectin, ( K , L ) fibrillin or ( M , N ) β-catenin, all shown in red. Note increase in fibrillin staining on the walls of the chamber of T5MO hearts relative to CMO (compare panel K to L, white arrows) and ectoptic expression of fibronectin, shown by white arrow, in the dorsal portion of the heart in panel J relative to panel I. ( O , P ) High magnification confocal images of hearts from (O) CMO or (P) T5MO stage 37 embryos. Note that formation of organized cardiac muscle bundles in T5MO hearts is limited to a single cluster adjacent to the cardiac lumen. ( Q – S ) Representative transmission electron micrographs of transverse images of stage 37 embryos taken from (Q) CMO cardiac tissue or (R) T5MO cardiac tissue adjacent to the pericardial cavity and (S) T5MO cardiac tissue adjacent to the cardiac lumen. Cardiac muscle fibrils are shown pseudo-colored in yellow. Note that sarcomeres in T5MO hearts can only be identified adjacent to the cardiac lumen (compare R with S) and only found in concentric arrays. By contrast, CMO-derived hearts show both longitudinal and concentric arrays (compare Q with S). High-magnification TEM images reveal the ultrastructures of ( T ) CMO and ( U ) T5MO cardiac sarcomeres. Arrows denote A-bands. Note the smaller, non-continuous A-bands in the T5MO-derived sarcomeres (U). ( V ) Traces of the heart sections from CMO and T5MO embryos imaged by TEM are depicted schematically. Yellow circles represent the location of TEM imaging. Scale bars: 50 μm in A–N; 2 μm in Q–S; 0.2 μm in T,U.

    Article Snippet: Cryostat sections (14 μm) were rinsed with wash buffer (PBS with 1% Triton and 1% heat inactivated calf serum), and incubated at 4°C overnight, as indicated, with mouse anti-tropomyosin 1:50, mouse anti-troponin 1:20, mouse anti-fibrillin 1:50 (all from Developmental Studies Hybridoma Bank), mouse anti-MHC (Abcam) rabbit anti-fibronectin 1:50 (Sigma), rabbit anti- Beta-catenin all at 1:1000 (Sigma), rabbit anti-phosphohistone H3 1:50 (Upstate) and rabbit anti-cleaved caspase 3 1:50 (Cell Signaling).

    Techniques: Immunostaining, Staining, Expressing, Transmission Assay, Derivative Assay, Transmission Electron Microscopy, Imaging

    MiR-17/20a enhances NK cell recognition by suppressing the expression of MHC class I

    Journal: Cancer immunology research

    Article Title: Restoration of MiR-17/20a in Solid Tumor Cells Enhances the Natural Killer Cell Antitumor Activity by Targeting Mekk2

    doi: 10.1158/2326-6066.CIR-13-0162

    Figure Lengend Snippet: MiR-17/20a enhances NK cell recognition by suppressing the expression of MHC class I

    Article Snippet: Cells were pretreated with the FcγR-blocking mAb (eBioscience, San Diego, CA, USA) on ice for 10 minutes, followed by treatment with anti-mouse MHC class I (H-2D/H-2K, eBioscience, San Diego, CA, USA) or H-2D mAb (BioLegend, San Diego, CA, USA) on ice for 30 minutes.

    Techniques: Expressing

    MiR-17/20a suppresses the expression of MHC class I via the Erk5 signal pathway by targeting Mekk2

    Journal: Cancer immunology research

    Article Title: Restoration of MiR-17/20a in Solid Tumor Cells Enhances the Natural Killer Cell Antitumor Activity by Targeting Mekk2

    doi: 10.1158/2326-6066.CIR-13-0162

    Figure Lengend Snippet: MiR-17/20a suppresses the expression of MHC class I via the Erk5 signal pathway by targeting Mekk2

    Article Snippet: Cells were pretreated with the FcγR-blocking mAb (eBioscience, San Diego, CA, USA) on ice for 10 minutes, followed by treatment with anti-mouse MHC class I (H-2D/H-2K, eBioscience, San Diego, CA, USA) or H-2D mAb (BioLegend, San Diego, CA, USA) on ice for 30 minutes.

    Techniques: Expressing

    Stromal-derived factors inhibit DC RALDH expression. (a and b) BM from C57BL/6 mice was cultured with GM-CSF alone or in the presence of SNs derived from primary mouse skin lines (skin), 3T3 fibroblasts, or EL-4 cells. After 3 d, LPS was added and, 18 h later, cells were stained with ALD and CD11c to measure DC RALDH activity. (a) A representative contour plot depicting the expression of CD11c and ALD is shown with inset values indicating the percentage of CD11c + DCs that are ALD + . (b) BM was differentiated, as in a, with SNs at various concentrations. Bar graphs show the mean percentages of CD11c + DCs that are ALD + with SD. Data were pooled from between 2 and 18 experiments. (c) DCs were differentiated from BM with GM-CSF alone or in the presence of skin SN. Cells were treated with LPS at day 3. 16–18 h later, DCs were purified with anti-CD11c or MHC class II microbeads and analyzed for RALDH2 expression by real-time qPCR. RALDH2 expression was normalized to GAPDH. Shown is relative expression of RALDH2 by skin SN versus control DCs, with each dot representing an individual experiment and horizontal bars the pooled mean. (d) DCs were differentiated from BM with GM-CSF alone, or in the presence of skin SN. After 3 d, LPS was added and, 18 h later, MHC class II + DCs were purified, pulsed with NP 366–374 -peptide, and used to stimulate CFSE-labeled CD8 + F5 T cells. 4 d later, the expression of CCR9 and PSL was analyzed by flow cytometry. Dot plots show the expression of homing receptors versus CFSE on live (PI − ) TCR + cells. Inset values are the mean percentage of dividing T cells positive for each receptor pooled from between 7 and 17 experiments. (e) CD8 + F5 T cells were activated as in d. After 4 d, T cells were labeled with CFSE or CTO, pooled at a 1:1 ratio, and transferred into congenic B6.Ly5.1 recipients (∼2 × 10 6 /recipient) that had been primed with oxazolone and challenged on the ear. After 16–18 h, the relative frequency of donor (CD45.2 + ) T cells primed by control versus skin SN-conditioned DCs at the various sites was determined by flow cytometry. A representative contour plot gated on live (PI − ) CD45.2 + donor T cells is shown, where control T cells are labeled with CTO and skin SN DC-primed T cells with CFSE. Inset is the mean frequency of each population pooled from three independent experiments.

    Journal: The Journal of Experimental Medicine

    Article Title: Prostaglandin E2 suppresses the differentiation of retinoic acid-producing dendritic cells in mice and humans

    doi: 10.1084/jem.20101967

    Figure Lengend Snippet: Stromal-derived factors inhibit DC RALDH expression. (a and b) BM from C57BL/6 mice was cultured with GM-CSF alone or in the presence of SNs derived from primary mouse skin lines (skin), 3T3 fibroblasts, or EL-4 cells. After 3 d, LPS was added and, 18 h later, cells were stained with ALD and CD11c to measure DC RALDH activity. (a) A representative contour plot depicting the expression of CD11c and ALD is shown with inset values indicating the percentage of CD11c + DCs that are ALD + . (b) BM was differentiated, as in a, with SNs at various concentrations. Bar graphs show the mean percentages of CD11c + DCs that are ALD + with SD. Data were pooled from between 2 and 18 experiments. (c) DCs were differentiated from BM with GM-CSF alone or in the presence of skin SN. Cells were treated with LPS at day 3. 16–18 h later, DCs were purified with anti-CD11c or MHC class II microbeads and analyzed for RALDH2 expression by real-time qPCR. RALDH2 expression was normalized to GAPDH. Shown is relative expression of RALDH2 by skin SN versus control DCs, with each dot representing an individual experiment and horizontal bars the pooled mean. (d) DCs were differentiated from BM with GM-CSF alone, or in the presence of skin SN. After 3 d, LPS was added and, 18 h later, MHC class II + DCs were purified, pulsed with NP 366–374 -peptide, and used to stimulate CFSE-labeled CD8 + F5 T cells. 4 d later, the expression of CCR9 and PSL was analyzed by flow cytometry. Dot plots show the expression of homing receptors versus CFSE on live (PI − ) TCR + cells. Inset values are the mean percentage of dividing T cells positive for each receptor pooled from between 7 and 17 experiments. (e) CD8 + F5 T cells were activated as in d. After 4 d, T cells were labeled with CFSE or CTO, pooled at a 1:1 ratio, and transferred into congenic B6.Ly5.1 recipients (∼2 × 10 6 /recipient) that had been primed with oxazolone and challenged on the ear. After 16–18 h, the relative frequency of donor (CD45.2 + ) T cells primed by control versus skin SN-conditioned DCs at the various sites was determined by flow cytometry. A representative contour plot gated on live (PI − ) CD45.2 + donor T cells is shown, where control T cells are labeled with CTO and skin SN DC-primed T cells with CFSE. Inset is the mean frequency of each population pooled from three independent experiments.

    Article Snippet: For in vitro proliferation assays, DCs were subsequently enriched with anti-CD11c or anti–MHC class II microbeads (Miltenyi Biotec).

    Techniques: Derivative Assay, Expressing, Mouse Assay, Cell Culture, Staining, Activity Assay, Purification, Real-time Polymerase Chain Reaction, Labeling, Flow Cytometry, Cytometry

    Increased expression of GATA-6 in obstruction-induced BSM hypertrophy in men with BPH. A: RNA was extracted from healthy (N) and BPH (B) human BSM tissues and subjected to RT-PCR for GATA-6 ( upper panel ) and GAPDH (lower panel) as control. B: Densitometric analysis of bands from A reported as GATA-6 expression relative to GAPDH. C: Nuclear protein was extracted from the same samples and subjected to immunoblotting. D: Densitometric analysis of bands in C presented as GATA-6 ( upper panel in C ) expression relative to nuclear protein p97 ( lower panel in C ). Data are from individual patients. E: Immunofluorescence images of endogenous GATA-6 in human BSM from healthy men ( upper panel ) and patients with BPH ( lower panel ). Human BSM tissue was stained with anti-GATA-6 polyclonal antibody (1:100) followed by FITC-conjugated secondary antibody. The smooth muscle tissues were also stained with Cy3-conjugated smooth muscle myosin heavy-chain 1. Slides were mounted in VectaShield medium containing DAPI to counterstain nuclei. Original magnification, ×63. Scale bars = 20 μm.

    Journal: The American Journal of Pathology

    Article Title: Transcriptional Repression of Caveolin-1 (CAV1) Gene Expression by GATA-6 in Bladder Smooth Muscle Hypertrophy in Mice and Human Beings

    doi: 10.1016/j.ajpath.2011.01.038

    Figure Lengend Snippet: Increased expression of GATA-6 in obstruction-induced BSM hypertrophy in men with BPH. A: RNA was extracted from healthy (N) and BPH (B) human BSM tissues and subjected to RT-PCR for GATA-6 ( upper panel ) and GAPDH (lower panel) as control. B: Densitometric analysis of bands from A reported as GATA-6 expression relative to GAPDH. C: Nuclear protein was extracted from the same samples and subjected to immunoblotting. D: Densitometric analysis of bands in C presented as GATA-6 ( upper panel in C ) expression relative to nuclear protein p97 ( lower panel in C ). Data are from individual patients. E: Immunofluorescence images of endogenous GATA-6 in human BSM from healthy men ( upper panel ) and patients with BPH ( lower panel ). Human BSM tissue was stained with anti-GATA-6 polyclonal antibody (1:100) followed by FITC-conjugated secondary antibody. The smooth muscle tissues were also stained with Cy3-conjugated smooth muscle myosin heavy-chain 1. Slides were mounted in VectaShield medium containing DAPI to counterstain nuclei. Original magnification, ×63. Scale bars = 20 μm.

    Article Snippet: The primary antibodies used were rabbit polyclonal anti–caveolin-1 conjugated with Cy3 (C3990) and mouse monoclonal antibody to smooth muscle myosin heavy-chain I (M7786) (both from Sigma-Aldrich, St. Louis, MO), and goat polyclonal antibody to SM22 (ab10135) and rabbit polyclonal antibody to GATA-6 (ab22600) (both from Abcam, Inc.).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Immunofluorescence, Staining

    Confocal microscopy of a live anesthetized mouse intradermally injected in the ear with anti-MHC class II reveals a significant decrease in the density of MHC class II + cells when locally irradiated. Two hours after intradermal injection of APC-conjugated

    Journal:

    Article Title: Migration of Skin Dendritic Cells in Response to Ionizing Radiation Exposure

    doi: 10.1667/RR1600.1

    Figure Lengend Snippet: Confocal microscopy of a live anesthetized mouse intradermally injected in the ear with anti-MHC class II reveals a significant decrease in the density of MHC class II + cells when locally irradiated. Two hours after intradermal injection of APC-conjugated

    Article Snippet: Fluorescein isothiocyanate (FITC)-conjugated anti-mouse MHC class II (I-A/I-E), FITC-conjugated anti-rat IgG2b , phycoerythrin (PE)-conjugated internal anti-mouse Langerin (CD207), allophycocyanin (APC)-conjugated anti-mouse F4/80, and APC-conjugated anti-mouse MHC class II (I-A/I-E) were purchased from eBioscience (San Diego, CA).

    Techniques: Confocal Microscopy, Injection, Irradiation

    Flow cytometry strategy. Detection of T lymphocyte subpopulation and MHC molecules using flow cytometry technique (CD3 gated), a CD4 + T lymphocytes (CD3 + CD4 + , region Q2). b CD8 + T lymphocytes (CD3 + CD8 + , region Q2). c MHC-I molecules (CD3 + MHC-I, region Q2). d . MHC-II molecules (CD3 + MHC-II, region Q2)

    Journal: BMC Infectious Diseases

    Article Title: Protective immunity against acute toxoplasmosis in BALB/c mice induced by a DNA vaccine encoding Toxoplasma gondii elongation factor 1-alpha

    doi: 10.1186/s12879-015-1220-5

    Figure Lengend Snippet: Flow cytometry strategy. Detection of T lymphocyte subpopulation and MHC molecules using flow cytometry technique (CD3 gated), a CD4 + T lymphocytes (CD3 + CD4 + , region Q2). b CD8 + T lymphocytes (CD3 + CD8 + , region Q2). c MHC-I molecules (CD3 + MHC-I, region Q2). d . MHC-II molecules (CD3 + MHC-II, region Q2)

    Article Snippet: Splenocyte suspensions (1 × 106 cells/ml) were dually stained with anti-mouse CD3e-FITC + anti-mouse CD8-PE, anti-mouse CD3e-FITC + anti-mouse CD4-PE, anti-mouse CD3e-FITC + anti-mouse MHC-I-PE or anti-mouse CD3e-FITC + anti-mouse MHC-II-PE (eBioscience, San Diego, CA, USA) for 30 min at 4 °C in the dark.

    Techniques: Flow Cytometry, Cytometry

    Immunostaining of embryonic myosin, myosin heavy chain, and LaminAC+ nuclei in the fiber interior. (A) Sections of the excised defect site were stained with embryonic myosin (eMHC; red), human-specific LaminAC (cyan), and DAPI (blue). Inset ( left) : concentrations of eMHC were found in the center of the implanted fibers. Dotted line denotes fiber boundary. Inset (right) : Example of colocalizing eMHC+ and human LaminAC+ cell in fibers with induced ASCs. Images depict fibers at 4 weeks. (B) Sections of the excised defect site were stained with myosin heavy chain (MHC; red), human-specific LaminAC (cyan), and DAPI (blue). Inset: concentrations of MHC were found in the center of the implanted fibers. Dotted line denotes fiber boundary. Images depict fibers at 12 weeks. (C) Sections of the excised defect site were stained with laminin (red), human-specific LaminAC (cyan), and DAPI (blue). Inset: concentrations of laminin+ cells with human nuclei were found in the center of the implanted fibers. Dotted line denotes fiber boundary. Image depicts uninduced fibers at 4 weeks. (D) Quantification of the number of eMHC+ and MHC+ cells inside fibers among the three groups ( n =9–15). There were significantly more eMHC+ cells at 1 month in fibers with uninduced ASCs than in acellular fibers. There was no significant difference in eMHC expression among groups at 3 months. There were significantly more MHC+ cells at both 1 month and 3 months in fibers with uninduced ASCs than in acellular fibers. (E) Sections of the excised defect site were stained for mouse CD31 (red) and DAPI (blue). Inset: host vascular infiltration was found in the interior of the implanted fibers in all groups at 3 months. Dotted line denotes fiber boundary. *p

    Journal: Cell Transplantation

    Article Title: Adipose-derived Stem/Stromal Cells on Electrospun Fibrin Microfiber Bundles Enable Moderate Muscle Reconstruction in a Volumetric Muscle Loss Model

    doi: 10.1177/0963689718805370

    Figure Lengend Snippet: Immunostaining of embryonic myosin, myosin heavy chain, and LaminAC+ nuclei in the fiber interior. (A) Sections of the excised defect site were stained with embryonic myosin (eMHC; red), human-specific LaminAC (cyan), and DAPI (blue). Inset ( left) : concentrations of eMHC were found in the center of the implanted fibers. Dotted line denotes fiber boundary. Inset (right) : Example of colocalizing eMHC+ and human LaminAC+ cell in fibers with induced ASCs. Images depict fibers at 4 weeks. (B) Sections of the excised defect site were stained with myosin heavy chain (MHC; red), human-specific LaminAC (cyan), and DAPI (blue). Inset: concentrations of MHC were found in the center of the implanted fibers. Dotted line denotes fiber boundary. Images depict fibers at 12 weeks. (C) Sections of the excised defect site were stained with laminin (red), human-specific LaminAC (cyan), and DAPI (blue). Inset: concentrations of laminin+ cells with human nuclei were found in the center of the implanted fibers. Dotted line denotes fiber boundary. Image depicts uninduced fibers at 4 weeks. (D) Quantification of the number of eMHC+ and MHC+ cells inside fibers among the three groups ( n =9–15). There were significantly more eMHC+ cells at 1 month in fibers with uninduced ASCs than in acellular fibers. There was no significant difference in eMHC expression among groups at 3 months. There were significantly more MHC+ cells at both 1 month and 3 months in fibers with uninduced ASCs than in acellular fibers. (E) Sections of the excised defect site were stained for mouse CD31 (red) and DAPI (blue). Inset: host vascular infiltration was found in the interior of the implanted fibers in all groups at 3 months. Dotted line denotes fiber boundary. *p

    Article Snippet: Primary antibodies included rabbit anti-mouse CCR7 (2.6 μg/ml; Abcam, Cambridge, UK), rabbit anti-human LaminAC (1.1 μg/ml; Abcam), mouse anti-human LaminAC (1:20; Abcam), mouse anti-embryonic myosin (4 μg/ml; DSHB), mouse anti-myosin heavy chain (24.3 μg/ml; Sigma-Aldrich), rabbit anti-laminin (4.5 μg/ml; Sigma-Aldrich), and rat anti-mouse CD31 (0.3 μg/ml; BD Biosciences).

    Techniques: Immunostaining, Staining, Expressing

    Effects of Parkin knockout on muscle contractility and phenotype A , in situ specific force of the TA muscle of Park2 −/− and Park2 +/+ expressed as a function of the stimulation frequency ( n = 5 or 6). B , representative immunolabeling for type I (blue), type IIa (red) and type IIb (green) MHC of a gastrocnemius cross‐section of Park2 −/− (right) and Park2 +/+ (left) mice. Type IIx fibre, unstained on these images, shown in black. Laminin was also immunolabelled to highlight fibre borders (green line surrounding each muscle fibre). C , quantification of the overall fibre size of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). D , quantification of the fibre size distribution of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). E , quantification of the average fibre size for each fibre type of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). F , quantification of the fibre type proportion the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). Statistical analyses for data shown in ( A ), ( D ), ( E ) and ( F ) were performed using a two‐way ANOVA. Corrections for multiple comparisons were performed by controlling for the false discovery rate using the two‐stage method of Benjamini and Krieger and Yekutieli (with q

    Journal: The Journal of Physiology

    Article Title: Protective role of Parkin in skeletal muscle contractile and mitochondrial function

    doi: 10.1113/JP275604

    Figure Lengend Snippet: Effects of Parkin knockout on muscle contractility and phenotype A , in situ specific force of the TA muscle of Park2 −/− and Park2 +/+ expressed as a function of the stimulation frequency ( n = 5 or 6). B , representative immunolabeling for type I (blue), type IIa (red) and type IIb (green) MHC of a gastrocnemius cross‐section of Park2 −/− (right) and Park2 +/+ (left) mice. Type IIx fibre, unstained on these images, shown in black. Laminin was also immunolabelled to highlight fibre borders (green line surrounding each muscle fibre). C , quantification of the overall fibre size of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). D , quantification of the fibre size distribution of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). E , quantification of the average fibre size for each fibre type of the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). F , quantification of the fibre type proportion the gastrocnemius muscle of Park2 −/− and Park2 +/+ mice ( n = 6 or 7). Statistical analyses for data shown in ( A ), ( D ), ( E ) and ( F ) were performed using a two‐way ANOVA. Corrections for multiple comparisons were performed by controlling for the false discovery rate using the two‐stage method of Benjamini and Krieger and Yekutieli (with q

    Article Snippet: These sections were then blocked using goat serum (10% in PBS) and incubated for 1 h at room temperature with a primary antibody cocktail: mouse IgG2b monoclonal anti‐MHC type I (BA‐F8; dilution 1:25), mouse IgG1 monoclonal anti‐MHC type IIa (SC‐71; dilution 1:200), mouse IgM monoclonal anti‐MHC type IIb (BF‐ F3; dilution 1:200) and rabbit IgG polyclonal anti‐laminin (L9393; Sigma‐Aldrich; dilution 1:750).

    Techniques: Knock-Out, In Situ, Immunolabeling, Mouse Assay