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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 397 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/protein+gel/10%25+Criterion+TGX+Stain-Free+Protein+Gel/pmc12828604-94-8-12
    Average 96 stars, based on 397 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

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    Membrane:

    Article Title: FAK Inhibition Remodels the Metastatic ECM and Restores CD8⁺ T Cell Trafficking and Immunosurveillance
    Article Snippet: After centrifugation for 15 min, 4 ° C, 15000 x g, protein concentration of supernatant was determined with Pierce TM Bradford Protein Assay (Cat #23200, ThermoFisher Scientific). .. 15 μg protein per sample was separated on 8-16% protein gel (Cat #4568106, Biorad) and transferred onto a nitrocellulose membrane. ..

    Article Title: B cells promote atrial fibrillation via autoantibodies.
    Article Snippet: Masahiro Yamazoe, Kenneth K. Y. Ting, I-Hsiu Lee , Aneesh Bapat , Andrew Lewis, Ling Xiao , Fadi E. Pulous , Kyle Mentkowski , Alexandre Paccalet, Noor Momin , Hana Seung , Theresa Dolejsi, Nina Kumowski, Maximilian J. Schloss, Yoshiko Iwamoto, Gustavo Ramos , Kenneth Chan, Charalambos Antoniades, Barbara Casadei , Filip K. Swirski , Patrick T. Ellinor , Kamila Naxerova , Steffen Pabel , Maarten Hulsmans & Matthias Nahrendorf

    Article Title: Supporting Information for Steric pressure between glycosylated transmembrane proteins inhibits internalization by endocytosis Authors
    Article Snippet: All protein samples were resolved on a pre-cast SDS-PAGE gel (Bio-Rad Mini-PROTEAN TGX polyacrylamide gel). .. The protein gel was transferred onto a nitrocellulose membrane with Bio-Rad’s Trans-Blot Turbo Transfer System at 1.5 Amps for 10 minutes. ..

    Article Title: Identification of the Notch ligand DLK1 as an immunotherapeutic target and regulator of tumor cell plasticity and chemoresistance in adrenocortical carcinoma
    Article Snippet: Protein concentration was determined by the DC TM Protein Assay Reagents Package Kit (Bio-Rad, #5000116). .. 20 μg of protein lysates were resolved on 4–15% Protein Gel (Bio-Rad, #5671084) and transferred to nitrocellulose membrane. .. The membranes were blocked in 5% blotting grade blocker (Bio-Rad, #1706404XTU) in TBS with 0.1% Tween-20 and then incubated with the indicated primary antibodies.

    Article Title: B cells promote atrial fibrillation via autoantibodies
    Article Snippet: .. Lysates of 20 μg were subjected to electrophoresis using the 4–15% protein gel (Bio-Rad) and blotted to a nitrocellulose membrane using the Trans-Blot Turbo transfer system (Bio-Rad). .. Anti-p2808 RyR2 antibody (1:1,000, Badrilla, A010-30), anti-RyR2 antibody (1:15,000, ThermoFisher, PA5-87416), anti-GAPDH antibody (1:5,000, Cell Signaling, 2118), anti-phospholamban Ser16 (1:1,000, ThermoFisher, PA5-117226), anti-phospholamban (1:1,000, ThemoFisher, PA5-119803) and HRP-conjugated secondary antibodies (1:5,000, Cell Signaling, 7074) were used.

    Blocking Assay:

    Article Title: TSG-6 Activated MSC-derived Extracellular Vesicles Present Altered micro-RNA Contents and Ameliorate the Inflammatory Phenotype of Macrophages in Vitro.
    Article Snippet: 1 3 Page 3 of 20 42 Inflammation (2026) 49:42 μl of RIPA Lysis and Extraction Buffer supplemented with 100× phosphatase and protease inhibitor cocktail, diluted to a final concentration of 1× in RIPA buffer (Thermo Fisher Scientific, 89901 and 78444).) and protein content was quantified by BCA assay (Thermo Fisher Scientific, 23225). .. EV protein samples (10 μg) were combined with 4X Laemmli buffer and 10% β-mercaptoethanol (Sigma Aldrich, 444203), heated on a heat block (95 °C, 5 min), and loaded onto a Mini-PROTEAN TGX 7.5% protein gel (Bio-Rad, 4568024) with a protein ladder (Thermo Fisher Scientific, 26617), in SDS-PAGE running buffer. .. Gel electrophoresis was run on Mini-PROTEAN Tetra Cells (Bio-Rad) and blots were transferred onto a 0.2 μm polyvinylidene difluoride (PVDF) Transfer-Blot Turbo Transfer Pack membrane (Bio-Rad, 1704156) in a Trans-Blot turbo transfer system (Bio-Rad, 1704150).

    Article Title: TSG-6 Activated MSC-derived Extracellular Vesicles Present Altered micro-RNA Contents and Ameliorate the Inflammatory Phenotype of Macrophages in Vitro
    Article Snippet: MSC-EVs were harvested as described above and the resulting pellets were lysed in 100 μl of RIPA Lysis and Extraction Buffer supplemented with 100× phosphatase and protease inhibitor cocktail, diluted to a final concentration of 1× in RIPA buffer (Thermo Fisher Scientific, 89901 and 78444).) and protein content was quantified by BCA assay (Thermo Fisher Scientific, 23225). .. EV protein samples (10 μg) were combined with 4X Laemmli buffer and 10% β-mercaptoethanol (Sigma Aldrich, 444203), heated on a heat block (95 °C, 5 min), and loaded onto a Mini-PROTEAN TGX 7.5% protein gel (Bio-Rad, 4568024) with a protein ladder (Thermo Fisher Scientific, 26617), in SDS-PAGE running buffer. .. Gel electrophoresis was run on Mini-PROTEAN Tetra Cells (Bio-Rad) and blots were transferred onto a 0.2 μm polyvinylidene difluoride (PVDF) Transfer-Blot Turbo Transfer Pack membrane (Bio-Rad, 1704156) in a Trans-Blot turbo transfer system (Bio-Rad, 1704150).

    SDS Page:

    Article Title: TSG-6 Activated MSC-derived Extracellular Vesicles Present Altered micro-RNA Contents and Ameliorate the Inflammatory Phenotype of Macrophages in Vitro.
    Article Snippet: 1 3 Page 3 of 20 42 Inflammation (2026) 49:42 μl of RIPA Lysis and Extraction Buffer supplemented with 100× phosphatase and protease inhibitor cocktail, diluted to a final concentration of 1× in RIPA buffer (Thermo Fisher Scientific, 89901 and 78444).) and protein content was quantified by BCA assay (Thermo Fisher Scientific, 23225). .. EV protein samples (10 μg) were combined with 4X Laemmli buffer and 10% β-mercaptoethanol (Sigma Aldrich, 444203), heated on a heat block (95 °C, 5 min), and loaded onto a Mini-PROTEAN TGX 7.5% protein gel (Bio-Rad, 4568024) with a protein ladder (Thermo Fisher Scientific, 26617), in SDS-PAGE running buffer. .. Gel electrophoresis was run on Mini-PROTEAN Tetra Cells (Bio-Rad) and blots were transferred onto a 0.2 μm polyvinylidene difluoride (PVDF) Transfer-Blot Turbo Transfer Pack membrane (Bio-Rad, 1704156) in a Trans-Blot turbo transfer system (Bio-Rad, 1704150).

    Article Title: TSG-6 Activated MSC-derived Extracellular Vesicles Present Altered micro-RNA Contents and Ameliorate the Inflammatory Phenotype of Macrophages in Vitro
    Article Snippet: MSC-EVs were harvested as described above and the resulting pellets were lysed in 100 μl of RIPA Lysis and Extraction Buffer supplemented with 100× phosphatase and protease inhibitor cocktail, diluted to a final concentration of 1× in RIPA buffer (Thermo Fisher Scientific, 89901 and 78444).) and protein content was quantified by BCA assay (Thermo Fisher Scientific, 23225). .. EV protein samples (10 μg) were combined with 4X Laemmli buffer and 10% β-mercaptoethanol (Sigma Aldrich, 444203), heated on a heat block (95 °C, 5 min), and loaded onto a Mini-PROTEAN TGX 7.5% protein gel (Bio-Rad, 4568024) with a protein ladder (Thermo Fisher Scientific, 26617), in SDS-PAGE running buffer. .. Gel electrophoresis was run on Mini-PROTEAN Tetra Cells (Bio-Rad) and blots were transferred onto a 0.2 μm polyvinylidene difluoride (PVDF) Transfer-Blot Turbo Transfer Pack membrane (Bio-Rad, 1704156) in a Trans-Blot turbo transfer system (Bio-Rad, 1704150).

    Electrophoresis:

    Article Title: B cells promote atrial fibrillation via autoantibodies.
    Article Snippet: Masahiro Yamazoe, Kenneth K. Y. Ting, I-Hsiu Lee , Aneesh Bapat , Andrew Lewis, Ling Xiao , Fadi E. Pulous , Kyle Mentkowski , Alexandre Paccalet, Noor Momin , Hana Seung , Theresa Dolejsi, Nina Kumowski, Maximilian J. Schloss, Yoshiko Iwamoto, Gustavo Ramos , Kenneth Chan, Charalambos Antoniades, Barbara Casadei , Filip K. Swirski , Patrick T. Ellinor , Kamila Naxerova , Steffen Pabel , Maarten Hulsmans & Matthias Nahrendorf

    Article Title: B cells promote atrial fibrillation via autoantibodies
    Article Snippet: .. Lysates of 20 μg were subjected to electrophoresis using the 4–15% protein gel (Bio-Rad) and blotted to a nitrocellulose membrane using the Trans-Blot Turbo transfer system (Bio-Rad). .. Anti-p2808 RyR2 antibody (1:1,000, Badrilla, A010-30), anti-RyR2 antibody (1:15,000, ThermoFisher, PA5-87416), anti-GAPDH antibody (1:5,000, Cell Signaling, 2118), anti-phospholamban Ser16 (1:1,000, ThermoFisher, PA5-117226), anti-phospholamban (1:1,000, ThemoFisher, PA5-119803) and HRP-conjugated secondary antibodies (1:5,000, Cell Signaling, 7074) were used.



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    Bio-Rad mini protean tgx stain free protein gel
    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.
    Mini Protean Tgx Stain Free Protein Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/protein+gel/MINI-PROTEAN+TGX/pmc13091216-163-38-44
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    Nobilis Therapeutics myofibrillar 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.
    Myofibrillar Protein Gels, supplied by Nobilis Therapeutics, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/protein+gel/gels+myofibrillar+protein/10__1016_slash_j__jfutfo__2026__05__034-376-22-29
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    96
    Bio-Rad criteriontm tgxtm precast 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.
    Criteriontm Tgxtm Precast 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