antibodies against ryr3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc antibodies against ryr3
    Antibodies Against Ryr3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti ryr1 antibodies  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ryr1 antibodies
    Dihydropyridine receptor alpha 1 (DHPRα1) and <t>ryanodine</t> <t>receptor</t> <t>1</t> <t>(RyR1)</t> localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.
    Anti Ryr1 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "The Effects of Aging on Sarcoplasmic Reticulum-Related Factors in the Skeletal Muscle of Mice"

    Article Title: The Effects of Aging on Sarcoplasmic Reticulum-Related Factors in the Skeletal Muscle of Mice

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms25042148

    Dihydropyridine receptor alpha 1 (DHPRα1) and ryanodine receptor 1 (RyR1) localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.
    Figure Legend Snippet: Dihydropyridine receptor alpha 1 (DHPRα1) and ryanodine receptor 1 (RyR1) localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.

    Techniques Used: Muscles, Staining, Standard Deviation

    rabbit monoclonal nti ryr1 antibodies  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc rabbit monoclonal nti ryr1 antibodies
    Rabbit Monoclonal Nti Ryr1 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ryr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ryr2
    Ryr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ryr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ryr2
    Antibodies used in this study
    Ryr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Sexual dimorphism in bidirectional SR-mitochondria crosstalk in ventricular cardiomyocytes"

    Article Title: Sexual dimorphism in bidirectional SR-mitochondria crosstalk in ventricular cardiomyocytes

    Journal: Basic Research in Cardiology

    doi: 10.1007/s00395-023-00988-1

    Antibodies used in this study
    Figure Legend Snippet: Antibodies used in this study

    Techniques Used: Western Blot

    COX7RP overexpression reduces spontaneous SR Ca 2+ release and mito-ROS in male ventricular myocytes under β-adrenergic stimulation. Conversely, COX7RP knock-down increases Ca 2+ waves and mito-ROS in females. A , B Representative Ca 2+ traces ( A ) and pooled data ( B ) for spontaneous Ca 2+ waves (SCW) latency in male (M), female (F), male overexpressing COX7RP (M + COX), and female expressing shRNA COX7RP (F + shC) ventricular cardiomyocytes (VCMs) exposed to 50 nmol/L isoproterenol (ISO, 5 min) after cessation of field stimulation (1 Hz). Mean ± SEM, n = 58–64, N = 6–9 preparations, * p < 0.05, p values were calculated using two-level random intercept model. C Pooled data for normalized fluorescence of mitochondria matrix ROS biosensor MLS-HyPer-7. Mean ± SEM, n = 29–42 VCMs, N = 6–9 animals, * p < 0.05, p values were calculated using two-level random intercept model. D Adenovirus–mediated expression of COX7RP in males and shRNA COX7RP in females alter RyR2 oxidation levels in rat VMs exposed to isoproterenol (ISO, 50 nmol/L) paced at 1 Hz for 5 min cultured for 48 h after infection (10 MOI). Immunoprecipitated RyR2s from M and F cultured VCM samples were probed with Anti-DNP antibody to detect amount of oxidized cysteines. E Pooled DNP optical density normalized to corresponding RyR2 signal. Mean ± SEM, N = 3 M, N = 4 F. * p < 0.05, Student’s t -test
    Figure Legend Snippet: COX7RP overexpression reduces spontaneous SR Ca 2+ release and mito-ROS in male ventricular myocytes under β-adrenergic stimulation. Conversely, COX7RP knock-down increases Ca 2+ waves and mito-ROS in females. A , B Representative Ca 2+ traces ( A ) and pooled data ( B ) for spontaneous Ca 2+ waves (SCW) latency in male (M), female (F), male overexpressing COX7RP (M + COX), and female expressing shRNA COX7RP (F + shC) ventricular cardiomyocytes (VCMs) exposed to 50 nmol/L isoproterenol (ISO, 5 min) after cessation of field stimulation (1 Hz). Mean ± SEM, n = 58–64, N = 6–9 preparations, * p < 0.05, p values were calculated using two-level random intercept model. C Pooled data for normalized fluorescence of mitochondria matrix ROS biosensor MLS-HyPer-7. Mean ± SEM, n = 29–42 VCMs, N = 6–9 animals, * p < 0.05, p values were calculated using two-level random intercept model. D Adenovirus–mediated expression of COX7RP in males and shRNA COX7RP in females alter RyR2 oxidation levels in rat VMs exposed to isoproterenol (ISO, 50 nmol/L) paced at 1 Hz for 5 min cultured for 48 h after infection (10 MOI). Immunoprecipitated RyR2s from M and F cultured VCM samples were probed with Anti-DNP antibody to detect amount of oxidized cysteines. E Pooled DNP optical density normalized to corresponding RyR2 signal. Mean ± SEM, N = 3 M, N = 4 F. * p < 0.05, Student’s t -test

    Techniques Used: Over Expression, Expressing, shRNA, Fluorescence, Cell Culture, Infection, Immunoprecipitation

    rabbit α ryr2 ser2814  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit α ryr2 ser2814
    Rabbit α Ryr2 Ser2814, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96/100 stars

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    rabbit α ryr2 ser2808  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit α ryr2 ser2808
    Rabbit α Ryr2 Ser2808, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ryr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ryr2
    Ryr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    total ryr1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total ryr1
    Illustration of DAB stained myofiber cross-sections (20x magnification) showing ( A ) total AMPK, ( B ) pAMPKThr 172 and ( C ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). No fiber type-specific differences in total AMPK were observed; Illustration of DAB stained consecutive myofiber cross-sections showing ( D ) total <t>RyR1,</t> ( E ) pRyR1Ser 2843 and ( F ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). As displayed in ( D, F ) total <t>RyR1</t> density was considerably lower in type I compared to type II myofibers. ( G ) Assessment of total RyR1 density in type I and II myofibers at baseline, 15 min, 30 min and 60 min post resistance exercise. Type II myofibers displayed significantly higher RyR1 densities than type I myofibers (p<0.01). Total RyR1 did not change over the time-course in type I and II myofibers. *headed bars display significant differences between myofibers types (p<0.01).
    Total Ryr1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Intense Resistance Exercise Induces Early and Transient Increases in Ryanodine Receptor 1 Phosphorylation in Human Skeletal Muscle"

    Article Title: Intense Resistance Exercise Induces Early and Transient Increases in Ryanodine Receptor 1 Phosphorylation in Human Skeletal Muscle

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0049326

    Illustration of DAB stained myofiber cross-sections (20x magnification) showing ( A ) total AMPK, ( B ) pAMPKThr 172 and ( C ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). No fiber type-specific differences in total AMPK were observed; Illustration of DAB stained consecutive myofiber cross-sections showing ( D ) total RyR1, ( E ) pRyR1Ser 2843 and ( F ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). As displayed in ( D, F ) total RyR1 density was considerably lower in type I compared to type II myofibers. ( G ) Assessment of total RyR1 density in type I and II myofibers at baseline, 15 min, 30 min and 60 min post resistance exercise. Type II myofibers displayed significantly higher RyR1 densities than type I myofibers (p<0.01). Total RyR1 did not change over the time-course in type I and II myofibers. *headed bars display significant differences between myofibers types (p<0.01).
    Figure Legend Snippet: Illustration of DAB stained myofiber cross-sections (20x magnification) showing ( A ) total AMPK, ( B ) pAMPKThr 172 and ( C ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). No fiber type-specific differences in total AMPK were observed; Illustration of DAB stained consecutive myofiber cross-sections showing ( D ) total RyR1, ( E ) pRyR1Ser 2843 and ( F ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). As displayed in ( D, F ) total RyR1 density was considerably lower in type I compared to type II myofibers. ( G ) Assessment of total RyR1 density in type I and II myofibers at baseline, 15 min, 30 min and 60 min post resistance exercise. Type II myofibers displayed significantly higher RyR1 densities than type I myofibers (p<0.01). Total RyR1 did not change over the time-course in type I and II myofibers. *headed bars display significant differences between myofibers types (p<0.01).

    Techniques Used: Staining

    ( A ) pRyR1Ser 2843 -stained myofiber cross-section at baseline (PRE) (20x magnification). ( B ) Consecutive myofiber cross-section specifically stained for type I MyHC1 (A4.840) assigning type I (dark) and type II (unstained) myofibers. ( C ) pRyR1Ser 2843 -stained myofiber cross-section in type I and type II myofibers 30 min post exercise. ( D ) Consecutive myofiber cross-section of displaying type I (dark) and type II (unstained) myofibers ( E ) Densitometry analysis of pRyR1Ser 172 staining in type I and II myofibers cross-sections at baseline as well as 15, 30 and 60 min after resistance exercise. Significantly (p<0.01) increased levels 15 and 30 min post exercise compared to baseline levels in type II (§) and up to 60 min in type I (#) myofibers. ( F ) Western blotting analysis of pRyR1Ser 2843 (n = 7). pRyR1Ser 2843 (band size is observed at 270 kDa according to ) was analyzed PRE, 15, 30 and 60 min following exercise in comparison to total RyR1 levels. Myosin heavy chain (MyHC1, 220 kDa) served as an additional internal loading control. ( § ) pRyR1Ser 2843 significantly different towards baseline levels at 15 min (p<0.05) and 30 min (p<0.01) after resistance exercise.
    Figure Legend Snippet: ( A ) pRyR1Ser 2843 -stained myofiber cross-section at baseline (PRE) (20x magnification). ( B ) Consecutive myofiber cross-section specifically stained for type I MyHC1 (A4.840) assigning type I (dark) and type II (unstained) myofibers. ( C ) pRyR1Ser 2843 -stained myofiber cross-section in type I and type II myofibers 30 min post exercise. ( D ) Consecutive myofiber cross-section of displaying type I (dark) and type II (unstained) myofibers ( E ) Densitometry analysis of pRyR1Ser 172 staining in type I and II myofibers cross-sections at baseline as well as 15, 30 and 60 min after resistance exercise. Significantly (p<0.01) increased levels 15 and 30 min post exercise compared to baseline levels in type II (§) and up to 60 min in type I (#) myofibers. ( F ) Western blotting analysis of pRyR1Ser 2843 (n = 7). pRyR1Ser 2843 (band size is observed at 270 kDa according to ) was analyzed PRE, 15, 30 and 60 min following exercise in comparison to total RyR1 levels. Myosin heavy chain (MyHC1, 220 kDa) served as an additional internal loading control. ( § ) pRyR1Ser 2843 significantly different towards baseline levels at 15 min (p<0.05) and 30 min (p<0.01) after resistance exercise.

    Techniques Used: Staining, Western Blot

    ( A ) pAMPKThr 172 -stained myofiber cross-section at baseline (PRE) (20x magnification). ( B ) Consecutive myofiber cross-section specifically stained for pRyR1Ser 2843 at baseline ( C ) pAMPKThr 172 -stained myofiber cross-section 30 min post exercise showing increased staining intensities compared to baseline condition. ( D ) Consecutive myofiber cross-section of showing increased staining intensities compared to baseline. ( E ) Distribution of combined phosphorylation levels of pAMPKThr 172 and pRyR1Ser 2843 within a population of single myofibers of one representative subject at baseline and 30 min post exercise. Each data point reflects the values of pAMPKThr 172 and pRyR1Ser 2843 within a single myofiber to the specified time point. The scatter plot reveals a heterogeneous distribution of combined phosphorylation levels of AMPK and RyR1 within single myofibers at baseline (○). 30 min post exercise the majority of myofibers offered significantly, however gradually increased pAMPKThr 172 and pRyR1ASer 2843 phosphorylation levels (•).
    Figure Legend Snippet: ( A ) pAMPKThr 172 -stained myofiber cross-section at baseline (PRE) (20x magnification). ( B ) Consecutive myofiber cross-section specifically stained for pRyR1Ser 2843 at baseline ( C ) pAMPKThr 172 -stained myofiber cross-section 30 min post exercise showing increased staining intensities compared to baseline condition. ( D ) Consecutive myofiber cross-section of showing increased staining intensities compared to baseline. ( E ) Distribution of combined phosphorylation levels of pAMPKThr 172 and pRyR1Ser 2843 within a population of single myofibers of one representative subject at baseline and 30 min post exercise. Each data point reflects the values of pAMPKThr 172 and pRyR1Ser 2843 within a single myofiber to the specified time point. The scatter plot reveals a heterogeneous distribution of combined phosphorylation levels of AMPK and RyR1 within single myofibers at baseline (○). 30 min post exercise the majority of myofibers offered significantly, however gradually increased pAMPKThr 172 and pRyR1ASer 2843 phosphorylation levels (•).

    Techniques Used: Staining

    anti ryanodine receptor 1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ryanodine receptor 1
    Comparison of muscle fibers and primary myotubes via immunostaining. (a) Anti-desmin, (b) anti-myosin heavy chain, (c) anti-Mitofusin 2, and (d) <t>anti-ryanodine</t> <t>receptor</t> 1. Muscle fibers and primary myotubes show typical cross-striated pattern for desmin and myosin staining. Nuclei were counterstained with DAPI. Scale bar corresponds to 50 μ m.
    Anti Ryanodine Receptor 1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Primary Murine Myotubes as a Model for Investigating Muscular Dystrophy"

    Article Title: Primary Murine Myotubes as a Model for Investigating Muscular Dystrophy

    Journal: BioMed Research International

    doi: 10.1155/2015/594751

    Comparison of muscle fibers and primary myotubes via immunostaining. (a) Anti-desmin, (b) anti-myosin heavy chain, (c) anti-Mitofusin 2, and (d) anti-ryanodine receptor 1. Muscle fibers and primary myotubes show typical cross-striated pattern for desmin and myosin staining. Nuclei were counterstained with DAPI. Scale bar corresponds to 50 μ m.
    Figure Legend Snippet: Comparison of muscle fibers and primary myotubes via immunostaining. (a) Anti-desmin, (b) anti-myosin heavy chain, (c) anti-Mitofusin 2, and (d) anti-ryanodine receptor 1. Muscle fibers and primary myotubes show typical cross-striated pattern for desmin and myosin staining. Nuclei were counterstained with DAPI. Scale bar corresponds to 50 μ m.

    Techniques Used: Immunostaining, Staining

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    Cell Signaling Technology Inc antibodies against ryr3
    Antibodies Against Ryr3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc anti ryr1 antibodies
    Dihydropyridine receptor alpha 1 (DHPRα1) and <t>ryanodine</t> <t>receptor</t> <t>1</t> <t>(RyR1)</t> localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.
    Anti Ryr1 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit monoclonal nti ryr1 antibodies
    Dihydropyridine receptor alpha 1 (DHPRα1) and <t>ryanodine</t> <t>receptor</t> <t>1</t> <t>(RyR1)</t> localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.
    Rabbit Monoclonal Nti Ryr1 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc ryr2
    Dihydropyridine receptor alpha 1 (DHPRα1) and <t>ryanodine</t> <t>receptor</t> <t>1</t> <t>(RyR1)</t> localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.
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    Cell Signaling Technology Inc rabbit α ryr2 ser2814
    Dihydropyridine receptor alpha 1 (DHPRα1) and <t>ryanodine</t> <t>receptor</t> <t>1</t> <t>(RyR1)</t> localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.
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    Cell Signaling Technology Inc rabbit α ryr2 ser2808
    Dihydropyridine receptor alpha 1 (DHPRα1) and <t>ryanodine</t> <t>receptor</t> <t>1</t> <t>(RyR1)</t> localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.
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    Illustration of DAB stained myofiber cross-sections (20x magnification) showing ( A ) total AMPK, ( B ) pAMPKThr 172 and ( C ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). No fiber type-specific differences in total AMPK were observed; Illustration of DAB stained consecutive myofiber cross-sections showing ( D ) total <t>RyR1,</t> ( E ) pRyR1Ser 2843 and ( F ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). As displayed in ( D, F ) total <t>RyR1</t> density was considerably lower in type I compared to type II myofibers. ( G ) Assessment of total RyR1 density in type I and II myofibers at baseline, 15 min, 30 min and 60 min post resistance exercise. Type II myofibers displayed significantly higher RyR1 densities than type I myofibers (p<0.01). Total RyR1 did not change over the time-course in type I and II myofibers. *headed bars display significant differences between myofibers types (p<0.01).
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    Cell Signaling Technology Inc anti ryanodine receptor 1
    Comparison of muscle fibers and primary myotubes via immunostaining. (a) Anti-desmin, (b) anti-myosin heavy chain, (c) anti-Mitofusin 2, and (d) <t>anti-ryanodine</t> <t>receptor</t> 1. Muscle fibers and primary myotubes show typical cross-striated pattern for desmin and myosin staining. Nuclei were counterstained with DAPI. Scale bar corresponds to 50 μ m.
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    Image Search Results


    Dihydropyridine receptor alpha 1 (DHPRα1) and ryanodine receptor 1 (RyR1) localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.

    Journal: International Journal of Molecular Sciences

    Article Title: The Effects of Aging on Sarcoplasmic Reticulum-Related Factors in the Skeletal Muscle of Mice

    doi: 10.3390/ijms25042148

    Figure Lengend Snippet: Dihydropyridine receptor alpha 1 (DHPRα1) and ryanodine receptor 1 (RyR1) localization. Cross-sections of the gastrocnemius ( a , c , e , g ) and soleus ( b , d , f , h ) muscles were stained with anti-DHPRα1 ( a – d ) or anti-RyR1 ( e – h ) antibodies. Asterisks indicate normal immunoreactivity (IR) in the cytoplasm and subsarcolemma of DHPRα1 or RyR1 ( a , b , d – f , h ). Arrows indicate muscle fiber with ectopic DHPRα1 or RyR1 IR ( c , g ). Scale bar = 50 μm. The number of muscle fibers with ectopic DHPRα1 or RyR1 IR was measured in the gastrocnemius ( i , k ) and soleus ( j , l ) muscles. Data are presented as mean ± standard deviation, n = 8 per group. Significant differences between young and old mice were determined using Student’s t -test. *** p < 0.0001. n.s.: not significant. All data are represented as dots in the graph. GAS, gastrocnemius muscle; SOL, soleus muscle; 3M, 3-month-old mice; 24M, 24-month-old mice.

    Article Snippet: The sections were then bleached with 3% H 2 O 2 , rinsed with PBS, and incubated in PBS containing 1% normal goat serum and 0.3% Triton X-100 at 4 °C for 1 h. The sections were then incubated with mouse monoclonal anti-DHPRα1 antibodies (MA3-920; Thermo Fisher Scientific, Waltham, MA, USA; 1:100) or rabbit polyclonal anti-SERCA1 antibodies (22361-1-AP; Proteintech, Rosemont, IL, USA; 1:500), anti-SERCA2 antibodies (ab3625; Abcam, Cambridge, MA, USA; 1:500), anti-RyR1 antibodies (D4E1, #8153; Cell Signaling Technology, Danvers, MA, USA; 1:100), anti-JPH1 antibodies (40-5100; Thermo Fisher Scientific, Waltham, MA, USA; 1:250), anti-JPH2 antibodies (40-5300; Thermo Fisher Scientific, Waltham, MA, USA; 1:50), or anti-MMP2 antibodies (GTX104577; GeneTex, Irvine, CA, USA; 1:50) in PBS containing 0.3% Triton X-100 at 4 °C for 24 h. Subsequently, the sections were incubated with biotinylated anti-mouse or rabbit immunoglobulin G (Vectastain ABC kit; Vector Laboratories, Burlingame, CA, USA) diluted at 1:1000 in PBS for 1 h at 25 °C, followed by incubation with avidin-biotin complex (Vectastain ABC kit) for 1 h at 4 °C.

    Techniques: Muscles, Staining, Standard Deviation

    Illustration of DAB stained myofiber cross-sections (20x magnification) showing ( A ) total AMPK, ( B ) pAMPKThr 172 and ( C ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). No fiber type-specific differences in total AMPK were observed; Illustration of DAB stained consecutive myofiber cross-sections showing ( D ) total RyR1, ( E ) pRyR1Ser 2843 and ( F ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). As displayed in ( D, F ) total RyR1 density was considerably lower in type I compared to type II myofibers. ( G ) Assessment of total RyR1 density in type I and II myofibers at baseline, 15 min, 30 min and 60 min post resistance exercise. Type II myofibers displayed significantly higher RyR1 densities than type I myofibers (p<0.01). Total RyR1 did not change over the time-course in type I and II myofibers. *headed bars display significant differences between myofibers types (p<0.01).

    Journal: PLoS ONE

    Article Title: Intense Resistance Exercise Induces Early and Transient Increases in Ryanodine Receptor 1 Phosphorylation in Human Skeletal Muscle

    doi: 10.1371/journal.pone.0049326

    Figure Lengend Snippet: Illustration of DAB stained myofiber cross-sections (20x magnification) showing ( A ) total AMPK, ( B ) pAMPKThr 172 and ( C ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). No fiber type-specific differences in total AMPK were observed; Illustration of DAB stained consecutive myofiber cross-sections showing ( D ) total RyR1, ( E ) pRyR1Ser 2843 and ( F ) corresponding MyHC1 staining displaying type I myofibers (black) and type II myofibers (unstained). As displayed in ( D, F ) total RyR1 density was considerably lower in type I compared to type II myofibers. ( G ) Assessment of total RyR1 density in type I and II myofibers at baseline, 15 min, 30 min and 60 min post resistance exercise. Type II myofibers displayed significantly higher RyR1 densities than type I myofibers (p<0.01). Total RyR1 did not change over the time-course in type I and II myofibers. *headed bars display significant differences between myofibers types (p<0.01).

    Article Snippet: Membranes were incubated overnight at 4°C with rabbit polyclonal total AMPK and phosphorylated AMPKThr 172 antibodies (Cell Signaling, Beverly, MA, USA; dilution 1∶1000) total RyR1 and RyR1Ser 2843 antibodies (Abcam, Cambridge, UK; dilution 1∶500 total RyR1 and 1∶750 pRyR1 Ser 2843 ).

    Techniques: Staining

    ( A ) pRyR1Ser 2843 -stained myofiber cross-section at baseline (PRE) (20x magnification). ( B ) Consecutive myofiber cross-section specifically stained for type I MyHC1 (A4.840) assigning type I (dark) and type II (unstained) myofibers. ( C ) pRyR1Ser 2843 -stained myofiber cross-section in type I and type II myofibers 30 min post exercise. ( D ) Consecutive myofiber cross-section of displaying type I (dark) and type II (unstained) myofibers ( E ) Densitometry analysis of pRyR1Ser 172 staining in type I and II myofibers cross-sections at baseline as well as 15, 30 and 60 min after resistance exercise. Significantly (p<0.01) increased levels 15 and 30 min post exercise compared to baseline levels in type II (§) and up to 60 min in type I (#) myofibers. ( F ) Western blotting analysis of pRyR1Ser 2843 (n = 7). pRyR1Ser 2843 (band size is observed at 270 kDa according to ) was analyzed PRE, 15, 30 and 60 min following exercise in comparison to total RyR1 levels. Myosin heavy chain (MyHC1, 220 kDa) served as an additional internal loading control. ( § ) pRyR1Ser 2843 significantly different towards baseline levels at 15 min (p<0.05) and 30 min (p<0.01) after resistance exercise.

    Journal: PLoS ONE

    Article Title: Intense Resistance Exercise Induces Early and Transient Increases in Ryanodine Receptor 1 Phosphorylation in Human Skeletal Muscle

    doi: 10.1371/journal.pone.0049326

    Figure Lengend Snippet: ( A ) pRyR1Ser 2843 -stained myofiber cross-section at baseline (PRE) (20x magnification). ( B ) Consecutive myofiber cross-section specifically stained for type I MyHC1 (A4.840) assigning type I (dark) and type II (unstained) myofibers. ( C ) pRyR1Ser 2843 -stained myofiber cross-section in type I and type II myofibers 30 min post exercise. ( D ) Consecutive myofiber cross-section of displaying type I (dark) and type II (unstained) myofibers ( E ) Densitometry analysis of pRyR1Ser 172 staining in type I and II myofibers cross-sections at baseline as well as 15, 30 and 60 min after resistance exercise. Significantly (p<0.01) increased levels 15 and 30 min post exercise compared to baseline levels in type II (§) and up to 60 min in type I (#) myofibers. ( F ) Western blotting analysis of pRyR1Ser 2843 (n = 7). pRyR1Ser 2843 (band size is observed at 270 kDa according to ) was analyzed PRE, 15, 30 and 60 min following exercise in comparison to total RyR1 levels. Myosin heavy chain (MyHC1, 220 kDa) served as an additional internal loading control. ( § ) pRyR1Ser 2843 significantly different towards baseline levels at 15 min (p<0.05) and 30 min (p<0.01) after resistance exercise.

    Article Snippet: Membranes were incubated overnight at 4°C with rabbit polyclonal total AMPK and phosphorylated AMPKThr 172 antibodies (Cell Signaling, Beverly, MA, USA; dilution 1∶1000) total RyR1 and RyR1Ser 2843 antibodies (Abcam, Cambridge, UK; dilution 1∶500 total RyR1 and 1∶750 pRyR1 Ser 2843 ).

    Techniques: Staining, Western Blot

    ( A ) pAMPKThr 172 -stained myofiber cross-section at baseline (PRE) (20x magnification). ( B ) Consecutive myofiber cross-section specifically stained for pRyR1Ser 2843 at baseline ( C ) pAMPKThr 172 -stained myofiber cross-section 30 min post exercise showing increased staining intensities compared to baseline condition. ( D ) Consecutive myofiber cross-section of showing increased staining intensities compared to baseline. ( E ) Distribution of combined phosphorylation levels of pAMPKThr 172 and pRyR1Ser 2843 within a population of single myofibers of one representative subject at baseline and 30 min post exercise. Each data point reflects the values of pAMPKThr 172 and pRyR1Ser 2843 within a single myofiber to the specified time point. The scatter plot reveals a heterogeneous distribution of combined phosphorylation levels of AMPK and RyR1 within single myofibers at baseline (○). 30 min post exercise the majority of myofibers offered significantly, however gradually increased pAMPKThr 172 and pRyR1ASer 2843 phosphorylation levels (•).

    Journal: PLoS ONE

    Article Title: Intense Resistance Exercise Induces Early and Transient Increases in Ryanodine Receptor 1 Phosphorylation in Human Skeletal Muscle

    doi: 10.1371/journal.pone.0049326

    Figure Lengend Snippet: ( A ) pAMPKThr 172 -stained myofiber cross-section at baseline (PRE) (20x magnification). ( B ) Consecutive myofiber cross-section specifically stained for pRyR1Ser 2843 at baseline ( C ) pAMPKThr 172 -stained myofiber cross-section 30 min post exercise showing increased staining intensities compared to baseline condition. ( D ) Consecutive myofiber cross-section of showing increased staining intensities compared to baseline. ( E ) Distribution of combined phosphorylation levels of pAMPKThr 172 and pRyR1Ser 2843 within a population of single myofibers of one representative subject at baseline and 30 min post exercise. Each data point reflects the values of pAMPKThr 172 and pRyR1Ser 2843 within a single myofiber to the specified time point. The scatter plot reveals a heterogeneous distribution of combined phosphorylation levels of AMPK and RyR1 within single myofibers at baseline (○). 30 min post exercise the majority of myofibers offered significantly, however gradually increased pAMPKThr 172 and pRyR1ASer 2843 phosphorylation levels (•).

    Article Snippet: Membranes were incubated overnight at 4°C with rabbit polyclonal total AMPK and phosphorylated AMPKThr 172 antibodies (Cell Signaling, Beverly, MA, USA; dilution 1∶1000) total RyR1 and RyR1Ser 2843 antibodies (Abcam, Cambridge, UK; dilution 1∶500 total RyR1 and 1∶750 pRyR1 Ser 2843 ).

    Techniques: Staining

    Comparison of muscle fibers and primary myotubes via immunostaining. (a) Anti-desmin, (b) anti-myosin heavy chain, (c) anti-Mitofusin 2, and (d) anti-ryanodine receptor 1. Muscle fibers and primary myotubes show typical cross-striated pattern for desmin and myosin staining. Nuclei were counterstained with DAPI. Scale bar corresponds to 50 μ m.

    Journal: BioMed Research International

    Article Title: Primary Murine Myotubes as a Model for Investigating Muscular Dystrophy

    doi: 10.1155/2015/594751

    Figure Lengend Snippet: Comparison of muscle fibers and primary myotubes via immunostaining. (a) Anti-desmin, (b) anti-myosin heavy chain, (c) anti-Mitofusin 2, and (d) anti-ryanodine receptor 1. Muscle fibers and primary myotubes show typical cross-striated pattern for desmin and myosin staining. Nuclei were counterstained with DAPI. Scale bar corresponds to 50 μ m.

    Article Snippet: Cells were incubated for one hour at room temperature with the following primary antibodies: anti-desmin (D33, DAKO, Denmark), anti-myosin heavy chain (MAB4470, R&D, USA), anti-ryanodine Receptor 1 (D4E1, Cell signaling, USA), anti-Mitofusin 2 (ab56889, Abcam, USA), anti-lamin A/C (NCL-LAM-A/C, Novocastra, UK).

    Techniques: Immunostaining, Staining