hsp72 (StressMarq)
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Structured Review
StressMarq
hsp72
Hsp72, supplied by StressMarq, used in various techniques. Bioz Stars score: 93/100, based on 107 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hsp72/HSP70+Antibody/pmc12828604-96-7-14
Average 93 stars, based on 107 article reviews
Hsp72, supplied by StressMarq, used in various techniques. Bioz Stars score: 93/100, based on 107 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hsp72/HSP70+Antibody/pmc12828604-96-7-14
Average 93 stars, based on 107 article reviews
hsp72 - by Bioz Stars,
2026-10
93/100 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
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
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
Figure Legend Snippet: HSP abundances in type I and II skeletal fibers from older adults pre- and post HIT exercise. Relative protein abundances of (A and B) HSP72, (C and D) HSP27, (E and F) pHSP27 Ser15, (G and H) αB-crystallin, and (I and J) pαB-crystallin Ser59 in fibers from old pre and old post HIT exercise. All fibers are expressed relative to the average old pre type I fibers or relative pre type II depending on fiber type. The same color is assigned to the same Individual, consistent in both graphs and all figures. * p < 0.05 and ** p < 0.01 indicated significant difference in paired t -test (except pHSP27 Ser15 Wilcoxon match-pair rank test). Representative blots are shown in . HIT = high-intensity training; HSP = heat shock protein; pαB-crystallin Ser59 = phospho-αB-crystallin at Serine59; pHSP27 Ser15 = phospho-HSP27 at Serine15.
Techniques Used:
Related Articles
Purification:Article Title: Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers. Article Snippet: 6 Noni T. Larkins, Robyn M. Murphy & Graham D. Lamb 7 8 Department of Zoology, La Trobe University, Melbourne, Victoria, 3086, Australia 9 10 11 Corresponding author: 12 Prof. Graham D. Lamb 13 Department of Zoology, La Trobe University, Melbourne, Victoria, 3086, Australia 14 Telephone: +61-3-9479 2249 15 Facsimile: +61-3-9479 1551 16 E-mail: g.lamb@latrobe.edu.au 17 18 19 Short page title: HSP binding in skeletal muscle fibers 20 21 Articles in PresS.. Am J Physiol Cell Physiol (July 3, 2012). doi:10.1152/ajpcell.00180.2012 Recombinant:Article Title: Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers. Article Snippet: 6 Noni T. Larkins, Robyn M. Murphy & Graham D. Lamb 7 8 Department of Zoology, La Trobe University, Melbourne, Victoria, 3086, Australia 9 10 11 Corresponding author: 12 Prof. Graham D. Lamb 13 Department of Zoology, La Trobe University, Melbourne, Victoria, 3086, Australia 14 Telephone: +61-3-9479 2249 15 Facsimile: +61-3-9479 1551 16 E-mail: g.lamb@latrobe.edu.au 17 18 19 Short page title: HSP binding in skeletal muscle fibers 20 21 Articles in PresS.. Am J Physiol Cell Physiol (July 3, 2012). doi:10.1152/ajpcell.00180.2012 other:Article Title: Astaxanthin supplementation impacts the cellular HSP expression profile during passive heating Article Snippet: Article Title: Heat shock protein 72 supports extracellular matrix production in metastatic mammary tumors. Article Snippet: This study identified tumorigenic processes most dependent on murine HSP72 in the MMTV-PyMT mammary tumor model, which give rise to spontaneous mammary tumors that exhibit HSP72dependent metastasis to the lung.. RNA-seq expression profiling of Hspa1a/Hspa1b (Hsp72) WT and Hsp72 -/primary mammary tumors discovered significantly lower expression of genes encoding components of the extracellular matrix (ECM) in Hsp72 knockout mammary tumors compared to WT controls.. In vitro studies found that genetic or chemical inhibition of HSP72 activity in cultured collagenJo ur na l P r -p ro of expressing human or murine cells also reduces mRNA and protein levels of COL1A1 and several other ECM-encoding genes. Saline:Article Title: Targeting Heat Shock Proteins Mitigates Ventilator Induced Diaphragm Muscle Dysfunction in an Age-Dependent Manner Article Snippet: Separated proteins were transferred to poly(vinylidene difluoride) membranes (Immobilon-P, Millipore). .. Membranes were blocked with 3% non-fat milk powder in Tris-buffered saline containing Tween 20 for 1 h and incubated overnight at 4°C with Incubation:Article Title: Targeting Heat Shock Proteins Mitigates Ventilator Induced Diaphragm Muscle Dysfunction in an Age-Dependent Manner Article Snippet: Separated proteins were transferred to poly(vinylidene difluoride) membranes (Immobilon-P, Millipore). .. Membranes were blocked with 3% non-fat milk powder in Tris-buffered saline containing Tween 20 for 1 h and incubated overnight at 4°C with |
