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Sangon Biotech d glucose
D Glucose, supplied by Sangon Biotech, 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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Article Title: Structure-adaptive dual-function poly-T sequences enable a homogeneous label-free colorimetric sensing platform.
Article Snippet: Compared with the extensive research on G-rich nucleic acids, the catalytic properties of T-rich sequences have received limited attention.. Herein, the peroxidase-like activity of poly-T sequences was investigated, and the results demonstrated that the poly-T sequences can display peroxidase-like activity with acetic acid as an activator, and the catalytic efficiency is positively correlated with sequence length.. Based on this, we constructed a novel homogeneous colorimetric sensing platform with melamine as the target.

Article Title: Methods for preparing pantoic acid, pantothenic acid and panthenol as well as salts thereof
Article Snippet: Casein Tryptone, yeast powder, D-(+)-glucose, potassium dihydrogen phosphate, sodium chloride, calcium chloride, ammonium chloride, D-calcium pantothenate, β-alanine, IPTG, thiamine and kanamycin sulfate were all purchased from Shanghai Sangon Biotech.

Article Title: High Q-factor all-dielectric terahertz metasurface biosensor with sensitivity enhanced via resonance-to-fingerprint peak matching
Article Snippet: A high quality factor (Q-factor) dual-band all-dielectric terahertz metasurface-based biosensor has been proposed and fabricated, with one resonance occurring in proximity to the fingerprint peak of D-(+)-glucose.. The alldielectric terahertz metasurface exhibits exceptional resonance characteristics, with Q-factors as high as 140 and 108 for its two distinct resonance peaks, which are significantly higher than those of traditional metasurfaces.. To evaluate its biosensing capabilities, the device was employed to detect D-(+)-glucose solutions across a concentration gradient spanning from 0.05 mmol/L to 0.5 mmol/L.

Article Title: Engineering Kluyveromyces marxianus for 3-hydroxypropionic acid production at elevated temperature from Jerusalem artichoke tubers and crude glycerol
Article Snippet: All compounds and biological reagents used in this study meet or exceed analytical grade purity specifications. d -glucose, glycerol, restriction endonucleases ( Eco RI, Not I), T4 DNA ligase, and yeast nitrogen base without amino acids (YNB) were purchased from Sangon Biotech Co., Ltd. (Shanghai, China).

Article Title: <scp>UCMSCs</scp> ‐Derived Exosomal <scp>circHIPK3</scp> Restrains Oxidative Stress and Inflammation by Downregulating the Stability of <scp>HMGB1 mRNA</scp> via Recruiting <scp>UPF1</scp> in Diabetes Foot Ulcer
Article Snippet: For HG stimulation, HUVECs and HDMECs were treated with D- glucose (20 mM, Sangon Biotech) for 72 h as per the manufacturer's instructions [27].

Article Title: Engineering Kluyveromyces marxianus for 3-hydroxypropionic acid production at elevated temperature from Jerusalem artichoke tubers and crude glycerol
Article Snippet: D-glucose, glycerol, restriction endonucleases (EcoRI, NotI), T4 DNA ligase, and yeast nitrogen base without amino acids (YNB) were purchased from Sangon Biotech Co., Ltd. (Shanghai, China).

Article Title: A wearable paper-based SGR/MCC microneedle array sensor for continuous glucose monitoring.
Article Snippet: D-(+)-Glucose and Propidium iodide (PI) were obtained from Sangon Biotech Co., Ltd. (Shanghai, China).

Injection:

Article Title: Hepatic GPR110 contributes to sex disparity in the development of MASH through oestrogen receptor α-dependent signalling.
Article Snippet: Metabolic dysfunction-associated steatohepatitis (MASH) is an important phase in the progression of metabolic dysfunction-associated steatotic liver disease to end-stage liver diseases, posing an increasing threat to public health worldwide with limited treatment options.. Here we show that GPR110 is a liver-selective G-protein-coupled receptor closely associated with MASH in a sex-specific manner.. Hepatocyte-specific Gpr110 knockout protects against MASH in female, but not male mice.



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Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) <t>HSP72,</t> 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.
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Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) <t>HSP72,</t> 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.
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Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) <t>HSP72,</t> 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.
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Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) <t>HSP72,</t> 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.
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Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) <t>HSP72,</t> 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.
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Relative HSP abundances in whole skeletal muscle homogenates from young adults and older adults pre and post HIT exercise. Representative Westen blots of (A) <t>HSP72,</t> 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.
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In vitro evaluation of CDT-induced immunogenic cell death (ICD), dendritic cell (DC) maturation, and T cell activation . ( A ) Schematic illustration of CDT-triggered ICD and associated damage-associated molecular pattern (DAMP) release. ( B, C ) Bioluminescence images and quantitative analysis of extracellular ATP release from 4T1 cells after different treatments. ( D, E ) Quantitative analysis and CLSM images of HMGB1 release. ( F ) CLSM images showing CRT surface exposure in 4T1 cells after different treatments. ( G ) Schematic illustration of the co-culture system used to evaluate DC maturation and subsequent T cell activation. Immature DCs (iDCs) were isolated from bone marrow, and CD8 + T cells were isolated from the lymph nodes and spleens of naïve BALB/c mice. ( H, I ) Representative flow cytometric plots and quantitative analysis of mature DCs, defined as CD11c + CD80 + D86 + cells, after 24 h incubation with differently treated 4T1 cells, showing enhanced DC maturation in the SHINE group. ( J, K ) Representative flow cytometric plots and quantification of CD69 + cells among CD8 + T cells. ( L, M ) Representative flow cytometric plots and quantification of CD25 + cells among CD8 + T cells. ( N, O ) Quantification of granzyme B and perforin expression in CD8 + T cells, indicating enhanced T cell activation and effector function following SHINE treatment. ( P ) Schematic illustration of the in vitro tumor-killing assay. CDT-pretreated 4T1-Luc cells (CDT only) and CDT-pretreated 4T1-Luc cells co-cultured with effector CD8 + T cells at an effector-to-target (E:T) ratio of 5:1 were used to evaluate the additional contribution of immunotherapy. After 24 <t>h,</t> <t>D-luciferin</t> (150 μg mL −1 ) was added to quantify live tumor cells by luciferase activity. ( Q, R ) Bioluminescence images and quantitative analysis of surviving 4T1-Luc cells after treatment with CDT alone or combined CDT + immunotherapy at different concentrations, showing that addition of immunotherapy further enhanced tumor cell killing. M, MnO 2 @PEG; MR, MnO 2 @R848; MP, MnO 2 @aPD-L1; SHINE, MnO 2 @R848@aPD-L1. Data are presented as mean ± SD ( n = 3 ; n = 4 for (R)). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Panels A, G, and P created with BioRender.com .
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In vitro evaluation of CDT-induced immunogenic cell death (ICD), dendritic cell (DC) maturation, and T cell activation . ( A ) Schematic illustration of CDT-triggered ICD and associated damage-associated molecular pattern (DAMP) release. ( B, C ) Bioluminescence images and quantitative analysis of extracellular ATP release from 4T1 cells after different treatments. ( D, E ) Quantitative analysis and CLSM images of HMGB1 release. ( F ) CLSM images showing CRT surface exposure in 4T1 cells after different treatments. ( G ) Schematic illustration of the co-culture system used to evaluate DC maturation and subsequent T cell activation. Immature DCs (iDCs) were isolated from bone marrow, and CD8 + T cells were isolated from the lymph nodes and spleens of naïve BALB/c mice. ( H, I ) Representative flow cytometric plots and quantitative analysis of mature DCs, defined as CD11c + CD80 + D86 + cells, after 24 h incubation with differently treated 4T1 cells, showing enhanced DC maturation in the SHINE group. ( J, K ) Representative flow cytometric plots and quantification of CD69 + cells among CD8 + T cells. ( L, M ) Representative flow cytometric plots and quantification of CD25 + cells among CD8 + T cells. ( N, O ) Quantification of granzyme B and perforin expression in CD8 + T cells, indicating enhanced T cell activation and effector function following SHINE treatment. ( P ) Schematic illustration of the in vitro tumor-killing assay. CDT-pretreated 4T1-Luc cells (CDT only) and CDT-pretreated 4T1-Luc cells co-cultured with effector CD8 + T cells at an effector-to-target (E:T) ratio of 5:1 were used to evaluate the additional contribution of immunotherapy. After 24 <t>h,</t> <t>D-luciferin</t> (150 μg mL −1 ) was added to quantify live tumor cells by luciferase activity. ( Q, R ) Bioluminescence images and quantitative analysis of surviving 4T1-Luc cells after treatment with CDT alone or combined CDT + immunotherapy at different concentrations, showing that addition of immunotherapy further enhanced tumor cell killing. M, MnO 2 @PEG; MR, MnO 2 @R848; MP, MnO 2 @aPD-L1; SHINE, MnO 2 @R848@aPD-L1. Data are presented as mean ± SD ( n = 3 ; n = 4 for (R)). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Panels A, G, and P created with BioRender.com .
D Glucose, supplied by Sangon Biotech, 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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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: Details of antibodies used are as follows: HSP72 (1 in 500 mouse monoclonal, SMC100A; StressMarq Biosciences, Victoria, Canada); HSP27 (1 in 1000 mouse monoclonal, G3.1 ab2790; Abcam, Cambridge, UK); pHSP27 Ser15 (1 in 2000 monoclonal rabbit, ab76313; Abcam), pHSP27 Ser82 (1 in 2000 polyclonal mouse, ADI-SPA-524; Enzo Biochem, Farmingdale, NY, USA), αB-crystallin (1 in 1000 mouse monoclonal, SPA-222; StressGen Biotechnologies), pαB-crystallin Ser59 (1 in 1000 rabbit polyclonal, SPA-227; StressGen Biotechnologies).

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: Details of antibodies used are as follows: HSP72 (1 in 500 mouse monoclonal, SMC100A; StressMarq Biosciences, Victoria, Canada); HSP27 (1 in 1000 mouse monoclonal, G3.1 ab2790; Abcam, Cambridge, UK); pHSP27 Ser15 (1 in 2000 monoclonal rabbit, ab76313; Abcam), pHSP27 Ser82 (1 in 2000 polyclonal mouse, ADI-SPA-524; Enzo Biochem, Farmingdale, NY, USA), αB-crystallin (1 in 1000 mouse monoclonal, SPA-222; StressGen Biotechnologies), pαB-crystallin Ser59 (1 in 1000 rabbit polyclonal, SPA-227; StressGen Biotechnologies).

Techniques: Staining, Membrane, Comparison

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.

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 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.

Article Snippet: Details of antibodies used are as follows: HSP72 (1 in 500 mouse monoclonal, SMC100A; StressMarq Biosciences, Victoria, Canada); HSP27 (1 in 1000 mouse monoclonal, G3.1 ab2790; Abcam, Cambridge, UK); pHSP27 Ser15 (1 in 2000 monoclonal rabbit, ab76313; Abcam), pHSP27 Ser82 (1 in 2000 polyclonal mouse, ADI-SPA-524; Enzo Biochem, Farmingdale, NY, USA), αB-crystallin (1 in 1000 mouse monoclonal, SPA-222; StressGen Biotechnologies), pαB-crystallin Ser59 (1 in 1000 rabbit polyclonal, SPA-227; StressGen Biotechnologies).

Techniques:

In vitro evaluation of CDT-induced immunogenic cell death (ICD), dendritic cell (DC) maturation, and T cell activation . ( A ) Schematic illustration of CDT-triggered ICD and associated damage-associated molecular pattern (DAMP) release. ( B, C ) Bioluminescence images and quantitative analysis of extracellular ATP release from 4T1 cells after different treatments. ( D, E ) Quantitative analysis and CLSM images of HMGB1 release. ( F ) CLSM images showing CRT surface exposure in 4T1 cells after different treatments. ( G ) Schematic illustration of the co-culture system used to evaluate DC maturation and subsequent T cell activation. Immature DCs (iDCs) were isolated from bone marrow, and CD8 + T cells were isolated from the lymph nodes and spleens of naïve BALB/c mice. ( H, I ) Representative flow cytometric plots and quantitative analysis of mature DCs, defined as CD11c + CD80 + D86 + cells, after 24 h incubation with differently treated 4T1 cells, showing enhanced DC maturation in the SHINE group. ( J, K ) Representative flow cytometric plots and quantification of CD69 + cells among CD8 + T cells. ( L, M ) Representative flow cytometric plots and quantification of CD25 + cells among CD8 + T cells. ( N, O ) Quantification of granzyme B and perforin expression in CD8 + T cells, indicating enhanced T cell activation and effector function following SHINE treatment. ( P ) Schematic illustration of the in vitro tumor-killing assay. CDT-pretreated 4T1-Luc cells (CDT only) and CDT-pretreated 4T1-Luc cells co-cultured with effector CD8 + T cells at an effector-to-target (E:T) ratio of 5:1 were used to evaluate the additional contribution of immunotherapy. After 24 h, D-luciferin (150 μg mL −1 ) was added to quantify live tumor cells by luciferase activity. ( Q, R ) Bioluminescence images and quantitative analysis of surviving 4T1-Luc cells after treatment with CDT alone or combined CDT + immunotherapy at different concentrations, showing that addition of immunotherapy further enhanced tumor cell killing. M, MnO 2 @PEG; MR, MnO 2 @R848; MP, MnO 2 @aPD-L1; SHINE, MnO 2 @R848@aPD-L1. Data are presented as mean ± SD ( n = 3 ; n = 4 for (R)). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Panels A, G, and P created with BioRender.com .

Journal: Bioactive Materials

Article Title: GSH-responsive nanovaccine triggers immunogenic cell death and potent memory T cell immunity for durable, recurrence-free tumor eradication

doi: 10.1016/j.bioactmat.2026.04.025

Figure Lengend Snippet: In vitro evaluation of CDT-induced immunogenic cell death (ICD), dendritic cell (DC) maturation, and T cell activation . ( A ) Schematic illustration of CDT-triggered ICD and associated damage-associated molecular pattern (DAMP) release. ( B, C ) Bioluminescence images and quantitative analysis of extracellular ATP release from 4T1 cells after different treatments. ( D, E ) Quantitative analysis and CLSM images of HMGB1 release. ( F ) CLSM images showing CRT surface exposure in 4T1 cells after different treatments. ( G ) Schematic illustration of the co-culture system used to evaluate DC maturation and subsequent T cell activation. Immature DCs (iDCs) were isolated from bone marrow, and CD8 + T cells were isolated from the lymph nodes and spleens of naïve BALB/c mice. ( H, I ) Representative flow cytometric plots and quantitative analysis of mature DCs, defined as CD11c + CD80 + D86 + cells, after 24 h incubation with differently treated 4T1 cells, showing enhanced DC maturation in the SHINE group. ( J, K ) Representative flow cytometric plots and quantification of CD69 + cells among CD8 + T cells. ( L, M ) Representative flow cytometric plots and quantification of CD25 + cells among CD8 + T cells. ( N, O ) Quantification of granzyme B and perforin expression in CD8 + T cells, indicating enhanced T cell activation and effector function following SHINE treatment. ( P ) Schematic illustration of the in vitro tumor-killing assay. CDT-pretreated 4T1-Luc cells (CDT only) and CDT-pretreated 4T1-Luc cells co-cultured with effector CD8 + T cells at an effector-to-target (E:T) ratio of 5:1 were used to evaluate the additional contribution of immunotherapy. After 24 h, D-luciferin (150 μg mL −1 ) was added to quantify live tumor cells by luciferase activity. ( Q, R ) Bioluminescence images and quantitative analysis of surviving 4T1-Luc cells after treatment with CDT alone or combined CDT + immunotherapy at different concentrations, showing that addition of immunotherapy further enhanced tumor cell killing. M, MnO 2 @PEG; MR, MnO 2 @R848; MP, MnO 2 @aPD-L1; SHINE, MnO 2 @R848@aPD-L1. Data are presented as mean ± SD ( n = 3 ; n = 4 for (R)). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Panels A, G, and P created with BioRender.com .

Article Snippet: Tumor cell viability was assessed by adding D-luciferin (Caliper Life Sciences, Hopkinton, Massachusetts, USA; 150 μg mL −1 ) and quantifying bioluminescence using an IVIS Lumina XR system (PerkinElmer, Inc., Waltham, Massachusetts, USA).

Techniques: In Vitro, Activation Assay, Co-Culture Assay, Isolation, Incubation, Expressing, Cell Culture, Luciferase, Activity Assay