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criterion tgx stain  (Bio-Rad)


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    Structured Review

    Bio-Rad criterion tgx stain
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Criterion Tgx Stain, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 399 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/criterion+tgx+stain+free+gel/10%25+Criterion+TGX+Stain-Free+Protein+Gel/pmc12828604-94-8-12
    Average 96 stars, based on 399 article reviews
    criterion tgx stain - by Bioz Stars, 2026-09
    96/100 stars

    Images

    1) Product Images from "Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals"

    Article Title: Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals

    Journal: Journal of Sport and Health Science

    doi: 10.1016/j.jshs.2025.101111

    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see Methods). Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Figure Legend Snippet: Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see Methods). Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Techniques Used: Staining, Membrane

    HSP abundances in type I and II skeletal muscle fibers from young and older adults. (A, C, and F) The MHC isoform present was determined in individual muscle fiber segments from the vastus lateralis and, following pooling into type I and type II groups from a given biopsy, were analyzed by Westen blotting. Westen blots of (A) HSP72, (C) HSP27 and pHSP27 Ser15, (F) αB-crystallin and pαB-crystallin Ser59, with MHC isoforms in groups of fibers. Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Calibration curves of mixed muscle homogenates are indicated. Relative protein abundances of (B) HSP72, (D) HSP27, (E) pHSP27 Ser15, (G) αB-crystallin, and (H) pαB-crystallin Ser59 in fibers from young (circle) and older adults (square) type I fibers (no outline) and type II fibers (outline). All fibers are expressed relative to the average older adult’s type I fibers. The same color is assigned to the same individual and is consistent with (data are presented as mean ± SD). * p < 0.05 and ** p < 0.01, mixed effect model Univariant using either Tukey’s or Games-Horwell’s multiple comparison test (see Methods). HIT = high-intensity training; HSP = heat shock protein; MHC = myosin heavy chain; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Figure Legend Snippet: HSP abundances in type I and II skeletal muscle fibers from young and older adults. (A, C, and F) The MHC isoform present was determined in individual muscle fiber segments from the vastus lateralis and, following pooling into type I and type II groups from a given biopsy, were analyzed by Westen blotting. Westen blots of (A) HSP72, (C) HSP27 and pHSP27 Ser15, (F) αB-crystallin and pαB-crystallin Ser59, with MHC isoforms in groups of fibers. Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Calibration curves of mixed muscle homogenates are indicated. Relative protein abundances of (B) HSP72, (D) HSP27, (E) pHSP27 Ser15, (G) αB-crystallin, and (H) pαB-crystallin Ser59 in fibers from young (circle) and older adults (square) type I fibers (no outline) and type II fibers (outline). All fibers are expressed relative to the average older adult’s type I fibers. The same color is assigned to the same individual and is consistent with (data are presented as mean ± SD). * p < 0.05 and ** p < 0.01, mixed effect model Univariant using either Tukey’s or Games-Horwell’s multiple comparison test (see Methods). HIT = high-intensity training; HSP = heat shock protein; MHC = myosin heavy chain; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Techniques Used: Staining, Membrane, Comparison

    Related Articles

    Staining:

    Article Title: Comparative lipidomics of iPSC-derived microglia protocols reveal lipid droplet and immune differences mediated by media composition.
    Article Snippet: Image analysis was performed using Columbus version 2.5.2 (PerkinElmer, Waltham, MA, USA) after imaging on CX7, or using Fiji (Schindelin et al., 2012) for confocal imaging on the Nikon Ti-Eclipse. .. Cells were lysed with LSB and samples denatured for 5 min at 95 ◦ C and shortly centrifuged before loading onto a 4–15% Criterion TGX Stain-free gel (BIO-RAD, 5678085). .. Gels were run at 90V for 30 min, followed by 45 min at 150V before transfer using the Trans-Blot Turbo RTA Midi 0.45 μm LF PVDF Transfer kit (BIO-RAD, 1704275) and the Trans-blot Turbo Transfer System (BIO-RAD, 1704150).

    Article Title: Comparative lipidomics of iPSC-derived microglia protocols reveal lipid droplet and immune differences mediated by media composition
    Article Snippet: Image analysis was performed using Columbus version 2.5.2 (PerkinElmer, Waltham, MA, USA) after imaging on CX7, or using Fiji ( ) for confocal imaging on the Nikon Ti-Eclipse. .. Cells were lysed with LSB and samples denatured for 5 min at 95°C and shortly centrifuged before loading onto a 4–15% Criterion TGX Stain-free gel (BIO-RAD, 5678085). .. Gels were run at 90V for 30 min, followed by 45 min at 150V before transfer using the Trans-Blot Turbo RTA Midi 0.45 μm LF PVDF Transfer kit (BIO-RAD, 1704275) and the Trans -blot Turbo Transfer System (BIO-RAD, 1704150).

    Article Title: Loss of the Coronary Artery Disease Risk Gene Leiomodin1 in Vascular Smooth Muscle Cells Triggers Rapid Onset Coronary Atherosclerosis
    Article Snippet: Aortas were isolated, cleaned, and lysed in RIPA buffer (Sigma-Aldrich #R0278) supplemented with protease inhibitor cocktail (Roche #04693159001) and PMSF (Sigma-Aldrich #10837091001). .. Protein concentrations were determined using the Protein Assay Kit II (Bio-Rad #5000112), and an average of 5 μg of protein was mixed with Laemmli Sample Buffer (Bio-Rad #1610747), boiled, cooled on ice for 10 minutes, and separated on a 4% to 15% Criterion TGX stain-free gel (Bio-Rad #5678083) using Tris-Glycine-SDS Buffer (10X, Bio Basic #A0030). .. Proteins were transferred onto PVDF membranes (Bio-Rad #1620177) using the Trans-Blot Turbo Transfer System (Bio-Rad #1704150) with the Trans-Blot Turbo Transfer Pack (Bio-Rad #1704275).

    Article Title: Early intestinal barrier changes in A53T transgenic Parkinson's disease mice.
    Article Snippet: Protein concentrations were determined using the Bio-Rad DC Protein Assay Kit (BioRad Laboratories, Hercules, USA) according to the manufacturer’s instructions. .. Approximately 10 μg of protein extract was loaded onto a 26-well Criterion TGX Stain-Free gel (Bio-Rad Laboratories, Hercules, USA) and subjected to electrophoresis at 50 mV for 5 min, followed by 100 mV for 60 min. Proteins were transferred to PVDF membranes for 1 h at 100 mV. ..

    Article Title: The Neurolipid Atlas: a lipidomics resource for neurodegenerative diseases
    Article Snippet: .. The samples were shortly vortexed and loaded onto 4–15% Criterion TGX stain-free gel (Bio-Rad, 5678085). .. After running the gel (90 V for 30 min followed by 150 V for 45 min), the gel was transferred to a low-fluorescence (LF) PVDF membrane using the Trans-Blot Turbo RTA Midi 0.45-μm LF PVDF transfer kit (Bio-Rad, 1704275).

    Article Title: Early intestinal barrier changes in A53T transgenic Parkinson’s disease mice
    Article Snippet: Protein concentrations were determined using the Bio-Rad DC Protein Assay Kit (Bio-Rad Laboratories, Hercules, USA) according to the manufacturer’s instructions. .. Approximately 10 μg of protein extract was loaded onto a 26-well Criterion TGX Stain-Free gel (Bio-Rad Laboratories, Hercules, USA) and subjected to electrophoresis at 50 mV for 5 min, followed by 100 mV for 60 min. Proteins were transferred to PVDF membranes for 1 h at 100 mV. ..

    Article Title: Challenges in mimicking hypoxia: insights into HIF-regulated MiRNA expression induced by DMOG and CoCl 2
    Article Snippet: .. Following the normalization of the protein concentrations, the lysates were mixed with an equal volume of 6X Laemmli sample buffer (12% SDS, 60% glycerol, 0.06% bromophenol blue, 375 mM Tris-HCl pH = 6.8) and incubated for 5 min at 95 °C prior to separation by SDS-PAGE on a 4–15% Criterion TGX Stain-Free Gel (Bio-Rad, Hercules, CA, USA). .. Following SDS-PAGE, the proteins were transferred to polyvinylidene fluoride membranes (Bio-Rad) using the wet electroblotting method (300 mA, 4 °C, 90 min for one gel and 180 min for two gels).

    Article Title: De novo design of potent inhibitors of clostridial family toxins.
    Article Snippet: .. These samples underwent SDS- PAGE using a Criterion TGX stain free gel (BioRad) at 200 V for 30 min before being stained with coomassie blue. ..

    Electrophoresis:

    Article Title: Early intestinal barrier changes in A53T transgenic Parkinson's disease mice.
    Article Snippet: Protein concentrations were determined using the Bio-Rad DC Protein Assay Kit (BioRad Laboratories, Hercules, USA) according to the manufacturer’s instructions. .. Approximately 10 μg of protein extract was loaded onto a 26-well Criterion TGX Stain-Free gel (Bio-Rad Laboratories, Hercules, USA) and subjected to electrophoresis at 50 mV for 5 min, followed by 100 mV for 60 min. Proteins were transferred to PVDF membranes for 1 h at 100 mV. ..

    Article Title: Early intestinal barrier changes in A53T transgenic Parkinson’s disease mice
    Article Snippet: Protein concentrations were determined using the Bio-Rad DC Protein Assay Kit (Bio-Rad Laboratories, Hercules, USA) according to the manufacturer’s instructions. .. Approximately 10 μg of protein extract was loaded onto a 26-well Criterion TGX Stain-Free gel (Bio-Rad Laboratories, Hercules, USA) and subjected to electrophoresis at 50 mV for 5 min, followed by 100 mV for 60 min. Proteins were transferred to PVDF membranes for 1 h at 100 mV. ..

    Incubation:

    Article Title: Challenges in mimicking hypoxia: insights into HIF-regulated MiRNA expression induced by DMOG and CoCl 2
    Article Snippet: .. Following the normalization of the protein concentrations, the lysates were mixed with an equal volume of 6X Laemmli sample buffer (12% SDS, 60% glycerol, 0.06% bromophenol blue, 375 mM Tris-HCl pH = 6.8) and incubated for 5 min at 95 °C prior to separation by SDS-PAGE on a 4–15% Criterion TGX Stain-Free Gel (Bio-Rad, Hercules, CA, USA). .. Following SDS-PAGE, the proteins were transferred to polyvinylidene fluoride membranes (Bio-Rad) using the wet electroblotting method (300 mA, 4 °C, 90 min for one gel and 180 min for two gels).

    SDS Page:

    Article Title: Challenges in mimicking hypoxia: insights into HIF-regulated MiRNA expression induced by DMOG and CoCl 2
    Article Snippet: .. Following the normalization of the protein concentrations, the lysates were mixed with an equal volume of 6X Laemmli sample buffer (12% SDS, 60% glycerol, 0.06% bromophenol blue, 375 mM Tris-HCl pH = 6.8) and incubated for 5 min at 95 °C prior to separation by SDS-PAGE on a 4–15% Criterion TGX Stain-Free Gel (Bio-Rad, Hercules, CA, USA). .. Following SDS-PAGE, the proteins were transferred to polyvinylidene fluoride membranes (Bio-Rad) using the wet electroblotting method (300 mA, 4 °C, 90 min for one gel and 180 min for two gels).

    Article Title: De novo design of potent inhibitors of clostridial family toxins.
    Article Snippet: .. These samples underwent SDS- PAGE using a Criterion TGX stain free gel (BioRad) at 200 V for 30 min before being stained with coomassie blue. ..



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    96
    Bio-Rad criterion gels
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
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    96
    Bio-Rad criterion tgx stain free protein gels
    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see <t>Methods).</t> <t>Stain-free</t> gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
    Criterion Tgx Stain Free Protein Gels, supplied by Bio-Rad, 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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    Image Search Results


    Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see Methods). Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Journal: Journal of Sport and Health Science

    Article Title: Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals

    doi: 10.1016/j.jshs.2025.101111

    Figure Lengend Snippet: Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) HSP72, HSP27, and αB-crystallin and (B) phosphorylated HSP27 Ser15 (pHSP27 Ser15) and pαB-crystallin Ser59 in whole muscle homogenates from the vastus lateralis of the same individuals. Calibration curves of mixed muscle homogenates are indicated and were used to determine the relative number of given proteins (see Methods). Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Relative abundances of (C) HSP72, (D) HSP27, (E) pHSP27 Ser15, (F) αB-crystallin, and (G) pαB-crystallin Ser59 from young (circle) and older adults Pre (square) and older adults Post (triangle) HIT exercise are shown relative to average Old (pre) on a given gel (data are presented as mean ± SD). Individuals indicated by the number of symbols ( n : 5–7), with the same color assigned to the same individual and consistent across all graphs. * p ≤ 0.05 indicates Brown-Forsye and Welch’s and post hoc analysis using Games-Horwell. HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Article Snippet: Total protein was separated on 10% or 4%–15% Criterion TGX stain-free gels (Bio-Rad Laboratories) and run for 45 min at 200 V. Using a wet transfer protocol, protein was transferred to nitrocellulose membranes at 100 V for 30 min. Membranes were incubated in Miser TM solution (ThermoFisher Scientific) and blocked in 5% skim milk powder in tris-buffered saline-tween (TBST).

    Techniques: Staining, Membrane

    HSP abundances in type I and II skeletal muscle fibers from young and older adults. (A, C, and F) The MHC isoform present was determined in individual muscle fiber segments from the vastus lateralis and, following pooling into type I and type II groups from a given biopsy, were analyzed by Westen blotting. Westen blots of (A) HSP72, (C) HSP27 and pHSP27 Ser15, (F) αB-crystallin and pαB-crystallin Ser59, with MHC isoforms in groups of fibers. Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Calibration curves of mixed muscle homogenates are indicated. Relative protein abundances of (B) HSP72, (D) HSP27, (E) pHSP27 Ser15, (G) αB-crystallin, and (H) pαB-crystallin Ser59 in fibers from young (circle) and older adults (square) type I fibers (no outline) and type II fibers (outline). All fibers are expressed relative to the average older adult’s type I fibers. The same color is assigned to the same individual and is consistent with (data are presented as mean ± SD). * p < 0.05 and ** p < 0.01, mixed effect model Univariant using either Tukey’s or Games-Horwell’s multiple comparison test (see Methods). HIT = high-intensity training; HSP = heat shock protein; MHC = myosin heavy chain; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Journal: Journal of Sport and Health Science

    Article Title: Exercise attenuates stress-related signaling as sensed by higher phosphorylation of small heat shock proteins in skeletal muscle from older individuals

    doi: 10.1016/j.jshs.2025.101111

    Figure Lengend Snippet: HSP abundances in type I and II skeletal muscle fibers from young and older adults. (A, C, and F) The MHC isoform present was determined in individual muscle fiber segments from the vastus lateralis and, following pooling into type I and type II groups from a given biopsy, were analyzed by Westen blotting. Westen blots of (A) HSP72, (C) HSP27 and pHSP27 Ser15, (F) αB-crystallin and pαB-crystallin Ser59, with MHC isoforms in groups of fibers. Stain-free gels are indicative of total protein loading, and molecular weights are indicated by markers collected under white light capture without moving the membrane between that and chemiluminescence detection. Calibration curves of mixed muscle homogenates are indicated. Relative protein abundances of (B) HSP72, (D) HSP27, (E) pHSP27 Ser15, (G) αB-crystallin, and (H) pαB-crystallin Ser59 in fibers from young (circle) and older adults (square) type I fibers (no outline) and type II fibers (outline). All fibers are expressed relative to the average older adult’s type I fibers. The same color is assigned to the same individual and is consistent with (data are presented as mean ± SD). * p < 0.05 and ** p < 0.01, mixed effect model Univariant using either Tukey’s or Games-Horwell’s multiple comparison test (see Methods). HIT = high-intensity training; HSP = heat shock protein; MHC = myosin heavy chain; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.

    Article Snippet: Total protein was separated on 10% or 4%–15% Criterion TGX stain-free gels (Bio-Rad Laboratories) and run for 45 min at 200 V. Using a wet transfer protocol, protein was transferred to nitrocellulose membranes at 100 V for 30 min. Membranes were incubated in Miser TM solution (ThermoFisher Scientific) and blocked in 5% skim milk powder in tris-buffered saline-tween (TBST).

    Techniques: Staining, Membrane, Comparison