hdac Search Results


hdac4  (Sino Biological)
90
Sino Biological hdac4
Hdac4, supplied by Sino Biological, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/10__1021_slash_acs__jmedchem__8b00393-394-7-15?v=Sino+Biological
Average 90 stars, based on 1 article reviews
hdac4 - by Bioz Stars, 2026-08
90/100 stars
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hdac2 staining  (Boster Bio)
93
Boster Bio hdac2 staining
<t>HDAC2</t> immunohistochemistry. Lung tissue slices from each treatment group were immunostained for HDAC2. Magnification, ×200. (A) Control, (B) COPD, (C) budesonide, (D) TCHM + budesonide and (E) theophylline + budesonide groups. One representative image from each group is shown (n=8). HDAC2, histone deacetylase 2; COPD, chronic obstructive pulmonary disease; TCHM, traditional Chinese herbal medicine.
Hdac2 Staining, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/pmc05795500-99-35-42?v=Boster+Bio
Average 93 stars, based on 1 article reviews
hdac2 staining - by Bioz Stars, 2026-08
93/100 stars
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rabbit anti α tubulin  (Rockland Immunochemicals)
93
Rockland Immunochemicals rabbit anti α tubulin
BMP signaling in CCN2/CTGF treated HTM-N cells in vitro . (A, B) Verification of BMP signaling activity in HMT-N cells in vitro . Immunoreactivity of pSmad1/5/8 (green) in HMT-N cells was increased after the treatment with 10 ng/mL BMP-4 (A) and 10 ng/mL BMP-7 (B) . Nuclei were stained with Dapi (blue). n = 3 (C) Western blot analysis of pSmad1/5/8 in the cytoplasmic fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after the treatment with BMP-4 for. (n = 5). GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (D) Western blot analysis of pSmad1/5/8 in the nuclear fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after 1 h with both treatments (n = 5). LaminB1 was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (E) Real-time RT-PCR analysis of Bmp-4 and Bmp-7 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Bmp-4 and Bmp-7 was significantly reduced after the treatment with CCN2/CTGF ( Bmp-4 : control n = 4, 50 ng/mL CCN2/CTGF n = 3, 100 ng/mL CCN2/CTGF n = 3; Bmp-7 : control n = 5, 50 ng/mL CCN2/CTGF n = 4, 100 ng/mL CCN2/CTGF n = 3). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (F) Real-time RT-PCR analyses of Smad6 , Smad7 , and Id2 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Smad6 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (n = 6). mRNA expression of Smad7 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression of Id2 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (G) Western blot analyses of BMP-7 after the treatment with 5 ng/mL, 25 ng/mL, 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. Protein synthesis of BMP-7 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 4, 5 ng/mL CCN2/CTGF: n = 3, 25 ng/mL CCN2/CTGF: n = 3, 50 ng/mL CCN2/CTGF: n = 3, 100 ng/mL CCN2/CTGF: n = 3). Mean value of wildtype animals (control) was set to 1. <t>α</t> <t>-Tubulin</t> was used to normalize protein synthesis. For statistical analysis the Kruskal–Wallis test was used. (H) Western blot analysis of pSmad1/5/8 after the treatment with 10 ng/mL BMP-4, 60 ng/mL Noggin and 10 ng/mL BMP-4, and 50 ng/mL CCN2/CTGF and 10 ng/mL BMP-4 in HTM-N cells. pSmad1/5/8 protein synthesis was increased after the treatment with BMP-4 (n = 5), compared to untreated control cells and significantly reduced after the treatment with the combination of Noggin and BMP-4 (n = 5) and the combination of CCN2/CTGF and BMP-4 (n = 5), compared to the treatment with BMP-4 only. Mean value of wildtype animals (control) was set to 1. GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. For statistical analysis the One-way ANOVA test was used. * p ≤ 0.05, ** p < 0.01, *** p < 0.001.
Rabbit Anti α Tubulin, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/pmc10210157-259-51-54?v=Rockland+Immunochemicals
Average 93 stars, based on 1 article reviews
rabbit anti α tubulin - by Bioz Stars, 2026-08
93/100 stars
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histone h3  (Rockland Immunochemicals)
88
Rockland Immunochemicals histone h3
BMP signaling in CCN2/CTGF treated HTM-N cells in vitro . (A, B) Verification of BMP signaling activity in HMT-N cells in vitro . Immunoreactivity of pSmad1/5/8 (green) in HMT-N cells was increased after the treatment with 10 ng/mL BMP-4 (A) and 10 ng/mL BMP-7 (B) . Nuclei were stained with Dapi (blue). n = 3 (C) Western blot analysis of pSmad1/5/8 in the cytoplasmic fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after the treatment with BMP-4 for. (n = 5). GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (D) Western blot analysis of pSmad1/5/8 in the nuclear fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after 1 h with both treatments (n = 5). LaminB1 was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (E) Real-time RT-PCR analysis of Bmp-4 and Bmp-7 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Bmp-4 and Bmp-7 was significantly reduced after the treatment with CCN2/CTGF ( Bmp-4 : control n = 4, 50 ng/mL CCN2/CTGF n = 3, 100 ng/mL CCN2/CTGF n = 3; Bmp-7 : control n = 5, 50 ng/mL CCN2/CTGF n = 4, 100 ng/mL CCN2/CTGF n = 3). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (F) Real-time RT-PCR analyses of Smad6 , Smad7 , and Id2 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Smad6 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (n = 6). mRNA expression of Smad7 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression of Id2 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (G) Western blot analyses of BMP-7 after the treatment with 5 ng/mL, 25 ng/mL, 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. Protein synthesis of BMP-7 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 4, 5 ng/mL CCN2/CTGF: n = 3, 25 ng/mL CCN2/CTGF: n = 3, 50 ng/mL CCN2/CTGF: n = 3, 100 ng/mL CCN2/CTGF: n = 3). Mean value of wildtype animals (control) was set to 1. <t>α</t> <t>-Tubulin</t> was used to normalize protein synthesis. For statistical analysis the Kruskal–Wallis test was used. (H) Western blot analysis of pSmad1/5/8 after the treatment with 10 ng/mL BMP-4, 60 ng/mL Noggin and 10 ng/mL BMP-4, and 50 ng/mL CCN2/CTGF and 10 ng/mL BMP-4 in HTM-N cells. pSmad1/5/8 protein synthesis was increased after the treatment with BMP-4 (n = 5), compared to untreated control cells and significantly reduced after the treatment with the combination of Noggin and BMP-4 (n = 5) and the combination of CCN2/CTGF and BMP-4 (n = 5), compared to the treatment with BMP-4 only. Mean value of wildtype animals (control) was set to 1. GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. For statistical analysis the One-way ANOVA test was used. * p ≤ 0.05, ** p < 0.01, *** p < 0.001.
Histone H3, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/pmc05923265-311-16-19?v=Rockland+Immunochemicals
Average 88 stars, based on 1 article reviews
histone h3 - by Bioz Stars, 2026-08
88/100 stars
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antibodies against hdac4  (Proteintech)
95
Proteintech antibodies against hdac4
BMP signaling in CCN2/CTGF treated HTM-N cells in vitro . (A, B) Verification of BMP signaling activity in HMT-N cells in vitro . Immunoreactivity of pSmad1/5/8 (green) in HMT-N cells was increased after the treatment with 10 ng/mL BMP-4 (A) and 10 ng/mL BMP-7 (B) . Nuclei were stained with Dapi (blue). n = 3 (C) Western blot analysis of pSmad1/5/8 in the cytoplasmic fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after the treatment with BMP-4 for. (n = 5). GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (D) Western blot analysis of pSmad1/5/8 in the nuclear fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after 1 h with both treatments (n = 5). LaminB1 was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (E) Real-time RT-PCR analysis of Bmp-4 and Bmp-7 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Bmp-4 and Bmp-7 was significantly reduced after the treatment with CCN2/CTGF ( Bmp-4 : control n = 4, 50 ng/mL CCN2/CTGF n = 3, 100 ng/mL CCN2/CTGF n = 3; Bmp-7 : control n = 5, 50 ng/mL CCN2/CTGF n = 4, 100 ng/mL CCN2/CTGF n = 3). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (F) Real-time RT-PCR analyses of Smad6 , Smad7 , and Id2 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Smad6 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (n = 6). mRNA expression of Smad7 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression of Id2 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (G) Western blot analyses of BMP-7 after the treatment with 5 ng/mL, 25 ng/mL, 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. Protein synthesis of BMP-7 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 4, 5 ng/mL CCN2/CTGF: n = 3, 25 ng/mL CCN2/CTGF: n = 3, 50 ng/mL CCN2/CTGF: n = 3, 100 ng/mL CCN2/CTGF: n = 3). Mean value of wildtype animals (control) was set to 1. <t>α</t> <t>-Tubulin</t> was used to normalize protein synthesis. For statistical analysis the Kruskal–Wallis test was used. (H) Western blot analysis of pSmad1/5/8 after the treatment with 10 ng/mL BMP-4, 60 ng/mL Noggin and 10 ng/mL BMP-4, and 50 ng/mL CCN2/CTGF and 10 ng/mL BMP-4 in HTM-N cells. pSmad1/5/8 protein synthesis was increased after the treatment with BMP-4 (n = 5), compared to untreated control cells and significantly reduced after the treatment with the combination of Noggin and BMP-4 (n = 5) and the combination of CCN2/CTGF and BMP-4 (n = 5), compared to the treatment with BMP-4 only. Mean value of wildtype animals (control) was set to 1. GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. For statistical analysis the One-way ANOVA test was used. * p ≤ 0.05, ** p < 0.01, *** p < 0.001.
Antibodies Against Hdac4, supplied by Proteintech, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/pm40143630-105-8-11?v=Proteintech
Average 95 stars, based on 1 article reviews
antibodies against hdac4 - by Bioz Stars, 2026-08
95/100 stars
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hdac4 expression vector  (OriGene)
93
OriGene hdac4 expression vector
Soleus muscle morphometric analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed <t>HDAC4.</t> (A) Representative immunofluorescence photomicrographs of soleus muscle, laminin (green) and DAPI (blue, used for nuclei identification) (scale bar 100 μm) and hematoxylin–eosin staining (scale bar 50 μm). The asterisk corresponds to the same fiber in both HE and immunofluorescence technique. (B) Soleus muscle mass, (C) whole muscle CSA, (D) fiber CSA and (E) fiber distribution from EV, <t>pCMVHDAC4,</t> Imm/pCMVHDAC4 and Imm + Leu/pCMVHDAC4 groups. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001 ( n = 5 per group).
Hdac4 Expression Vector, supplied by OriGene, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/pmc12138493-37-11-17?v=OriGene
Average 93 stars, based on 1 article reviews
hdac4 expression vector - by Bioz Stars, 2026-08
93/100 stars
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hdac2 levels  (Shanghai Korain Biotech Co Ltd)
94
Shanghai Korain Biotech Co Ltd hdac2 levels
Soleus muscle morphometric analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed <t>HDAC4.</t> (A) Representative immunofluorescence photomicrographs of soleus muscle, laminin (green) and DAPI (blue, used for nuclei identification) (scale bar 100 μm) and hematoxylin–eosin staining (scale bar 50 μm). The asterisk corresponds to the same fiber in both HE and immunofluorescence technique. (B) Soleus muscle mass, (C) whole muscle CSA, (D) fiber CSA and (E) fiber distribution from EV, <t>pCMVHDAC4,</t> Imm/pCMVHDAC4 and Imm + Leu/pCMVHDAC4 groups. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001 ( n = 5 per group).
Hdac2 Levels, supplied by Shanghai Korain Biotech Co Ltd, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/med_rxiv__64898__2026__04__05__26348641-80-0-13?v=Shanghai+Korain+Biotech+Co+Ltd
Average 94 stars, based on 1 article reviews
hdac2 levels - by Bioz Stars, 2026-08
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и наборов fluorogenic hdac  (BPS Bioscience)
93
BPS Bioscience и наборов fluorogenic hdac
Soleus muscle morphometric analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed <t>HDAC4.</t> (A) Representative immunofluorescence photomicrographs of soleus muscle, laminin (green) and DAPI (blue, used for nuclei identification) (scale bar 100 μm) and hematoxylin–eosin staining (scale bar 50 μm). The asterisk corresponds to the same fiber in both HE and immunofluorescence technique. (B) Soleus muscle mass, (C) whole muscle CSA, (D) fiber CSA and (E) fiber distribution from EV, <t>pCMVHDAC4,</t> Imm/pCMVHDAC4 and Imm + Leu/pCMVHDAC4 groups. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001 ( n = 5 per group).
и наборов Fluorogenic Hdac, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/10__17650_slash_2313___805x___2022___9___4___5___150-4152-15-25?v=BPS+Bioscience
Average 93 stars, based on 1 article reviews
и наборов fluorogenic hdac - by Bioz Stars, 2026-08
93/100 stars
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rabbit anti phospho hdac4  (Rockland Immunochemicals)
90
Rockland Immunochemicals rabbit anti phospho hdac4
Soleus muscle morphometric analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed <t>HDAC4.</t> (A) Representative immunofluorescence photomicrographs of soleus muscle, laminin (green) and DAPI (blue, used for nuclei identification) (scale bar 100 μm) and hematoxylin–eosin staining (scale bar 50 μm). The asterisk corresponds to the same fiber in both HE and immunofluorescence technique. (B) Soleus muscle mass, (C) whole muscle CSA, (D) fiber CSA and (E) fiber distribution from EV, <t>pCMVHDAC4,</t> Imm/pCMVHDAC4 and Imm + Leu/pCMVHDAC4 groups. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001 ( n = 5 per group).
Rabbit Anti Phospho Hdac4, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/10__1074_slash_jbc__m115__657775-86-40-53?v=Rockland+Immunochemicals
Average 90 stars, based on 1 article reviews
rabbit anti phospho hdac4 - by Bioz Stars, 2026-08
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fluorogenic hdac substrates  (BPS Bioscience)
90
BPS Bioscience fluorogenic hdac substrates
Soleus muscle morphometric analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed <t>HDAC4.</t> (A) Representative immunofluorescence photomicrographs of soleus muscle, laminin (green) and DAPI (blue, used for nuclei identification) (scale bar 100 μm) and hematoxylin–eosin staining (scale bar 50 μm). The asterisk corresponds to the same fiber in both HE and immunofluorescence technique. (B) Soleus muscle mass, (C) whole muscle CSA, (D) fiber CSA and (E) fiber distribution from EV, <t>pCMVHDAC4,</t> Imm/pCMVHDAC4 and Imm + Leu/pCMVHDAC4 groups. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001 ( n = 5 per group).
Fluorogenic Hdac Substrates, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/pmc04917448-112-23-6?v=BPS+Bioscience
Average 90 stars, based on 1 article reviews
fluorogenic hdac substrates - by Bioz Stars, 2026-08
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antigen recovery  (Boster Bio)
91
Boster Bio antigen recovery
Soleus muscle morphometric analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed <t>HDAC4.</t> (A) Representative immunofluorescence photomicrographs of soleus muscle, laminin (green) and DAPI (blue, used for nuclei identification) (scale bar 100 μm) and hematoxylin–eosin staining (scale bar 50 μm). The asterisk corresponds to the same fiber in both HE and immunofluorescence technique. (B) Soleus muscle mass, (C) whole muscle CSA, (D) fiber CSA and (E) fiber distribution from EV, <t>pCMVHDAC4,</t> Imm/pCMVHDAC4 and Imm + Leu/pCMVHDAC4 groups. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001 ( n = 5 per group).
Antigen Recovery, supplied by Boster Bio, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/10__3727_slash_096504016x14732510786564-98-0-13?v=Boster+Bio
Average 91 stars, based on 1 article reviews
antigen recovery - by Bioz Stars, 2026-08
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anti hdac4  (Proteintech)
93
Proteintech anti hdac4
Soleus muscle morphometric analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed <t>HDAC4.</t> (A) Representative immunofluorescence photomicrographs of soleus muscle, laminin (green) and DAPI (blue, used for nuclei identification) (scale bar 100 μm) and hematoxylin–eosin staining (scale bar 50 μm). The asterisk corresponds to the same fiber in both HE and immunofluorescence technique. (B) Soleus muscle mass, (C) whole muscle CSA, (D) fiber CSA and (E) fiber distribution from EV, <t>pCMVHDAC4,</t> Imm/pCMVHDAC4 and Imm + Leu/pCMVHDAC4 groups. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001 ( n = 5 per group).
Anti Hdac4, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hdac/pmc09672882-68-0-20?v=Proteintech
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anti hdac4 - by Bioz Stars, 2026-08
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Image Search Results


HDAC2 immunohistochemistry. Lung tissue slices from each treatment group were immunostained for HDAC2. Magnification, ×200. (A) Control, (B) COPD, (C) budesonide, (D) TCHM + budesonide and (E) theophylline + budesonide groups. One representative image from each group is shown (n=8). HDAC2, histone deacetylase 2; COPD, chronic obstructive pulmonary disease; TCHM, traditional Chinese herbal medicine.

Journal: Experimental and Therapeutic Medicine

Article Title: Jinwei Tang modulates HDAC2 expression in a rat model of COPD

doi: 10.3892/etm.2018.5707

Figure Lengend Snippet: HDAC2 immunohistochemistry. Lung tissue slices from each treatment group were immunostained for HDAC2. Magnification, ×200. (A) Control, (B) COPD, (C) budesonide, (D) TCHM + budesonide and (E) theophylline + budesonide groups. One representative image from each group is shown (n=8). HDAC2, histone deacetylase 2; COPD, chronic obstructive pulmonary disease; TCHM, traditional Chinese herbal medicine.

Article Snippet: Following washing, biotinylated secondary antibodies (cat. no. 85-6643; 1:100 dilution; Invitrogen; Thermo Fisher Scientifc, Inc.) were allowed to react at room temperature for 15 min followed by binding to horseradish peroxidase-avidin conjugation for 15 min. HDAC2 staining was visualized by DAB development (Wuhan Boster Biological Technology, Ltd.).

Techniques: Immunohistochemistry, Control, Histone Deacetylase Assay

Levels of HDAC2, IL-8 and TNF-α in rat lung tissue (mean ± standard deviation, n=8).

Journal: Experimental and Therapeutic Medicine

Article Title: Jinwei Tang modulates HDAC2 expression in a rat model of COPD

doi: 10.3892/etm.2018.5707

Figure Lengend Snippet: Levels of HDAC2, IL-8 and TNF-α in rat lung tissue (mean ± standard deviation, n=8).

Article Snippet: Following washing, biotinylated secondary antibodies (cat. no. 85-6643; 1:100 dilution; Invitrogen; Thermo Fisher Scientifc, Inc.) were allowed to react at room temperature for 15 min followed by binding to horseradish peroxidase-avidin conjugation for 15 min. HDAC2 staining was visualized by DAB development (Wuhan Boster Biological Technology, Ltd.).

Techniques: Standard Deviation, Control

Correlation of HDAC2 with IL-8 or TNF-α. Correlation between HADC2 and (A) TNF-α and (B) IL-8. HDAC2, histone deacetylase 2; IL, interleukin; TNF, tumor necrosis factor.

Journal: Experimental and Therapeutic Medicine

Article Title: Jinwei Tang modulates HDAC2 expression in a rat model of COPD

doi: 10.3892/etm.2018.5707

Figure Lengend Snippet: Correlation of HDAC2 with IL-8 or TNF-α. Correlation between HADC2 and (A) TNF-α and (B) IL-8. HDAC2, histone deacetylase 2; IL, interleukin; TNF, tumor necrosis factor.

Article Snippet: Following washing, biotinylated secondary antibodies (cat. no. 85-6643; 1:100 dilution; Invitrogen; Thermo Fisher Scientifc, Inc.) were allowed to react at room temperature for 15 min followed by binding to horseradish peroxidase-avidin conjugation for 15 min. HDAC2 staining was visualized by DAB development (Wuhan Boster Biological Technology, Ltd.).

Techniques: Histone Deacetylase Assay

BMP signaling in CCN2/CTGF treated HTM-N cells in vitro . (A, B) Verification of BMP signaling activity in HMT-N cells in vitro . Immunoreactivity of pSmad1/5/8 (green) in HMT-N cells was increased after the treatment with 10 ng/mL BMP-4 (A) and 10 ng/mL BMP-7 (B) . Nuclei were stained with Dapi (blue). n = 3 (C) Western blot analysis of pSmad1/5/8 in the cytoplasmic fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after the treatment with BMP-4 for. (n = 5). GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (D) Western blot analysis of pSmad1/5/8 in the nuclear fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after 1 h with both treatments (n = 5). LaminB1 was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (E) Real-time RT-PCR analysis of Bmp-4 and Bmp-7 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Bmp-4 and Bmp-7 was significantly reduced after the treatment with CCN2/CTGF ( Bmp-4 : control n = 4, 50 ng/mL CCN2/CTGF n = 3, 100 ng/mL CCN2/CTGF n = 3; Bmp-7 : control n = 5, 50 ng/mL CCN2/CTGF n = 4, 100 ng/mL CCN2/CTGF n = 3). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (F) Real-time RT-PCR analyses of Smad6 , Smad7 , and Id2 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Smad6 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (n = 6). mRNA expression of Smad7 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression of Id2 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (G) Western blot analyses of BMP-7 after the treatment with 5 ng/mL, 25 ng/mL, 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. Protein synthesis of BMP-7 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 4, 5 ng/mL CCN2/CTGF: n = 3, 25 ng/mL CCN2/CTGF: n = 3, 50 ng/mL CCN2/CTGF: n = 3, 100 ng/mL CCN2/CTGF: n = 3). Mean value of wildtype animals (control) was set to 1. α -Tubulin was used to normalize protein synthesis. For statistical analysis the Kruskal–Wallis test was used. (H) Western blot analysis of pSmad1/5/8 after the treatment with 10 ng/mL BMP-4, 60 ng/mL Noggin and 10 ng/mL BMP-4, and 50 ng/mL CCN2/CTGF and 10 ng/mL BMP-4 in HTM-N cells. pSmad1/5/8 protein synthesis was increased after the treatment with BMP-4 (n = 5), compared to untreated control cells and significantly reduced after the treatment with the combination of Noggin and BMP-4 (n = 5) and the combination of CCN2/CTGF and BMP-4 (n = 5), compared to the treatment with BMP-4 only. Mean value of wildtype animals (control) was set to 1. GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. For statistical analysis the One-way ANOVA test was used. * p ≤ 0.05, ** p < 0.01, *** p < 0.001.

Journal: Frontiers in Molecular Biosciences

Article Title: CCN2/CTGF tip the balance of growth factors towards TGF-β2 in primary open-angle glaucoma

doi: 10.3389/fmolb.2023.1045411

Figure Lengend Snippet: BMP signaling in CCN2/CTGF treated HTM-N cells in vitro . (A, B) Verification of BMP signaling activity in HMT-N cells in vitro . Immunoreactivity of pSmad1/5/8 (green) in HMT-N cells was increased after the treatment with 10 ng/mL BMP-4 (A) and 10 ng/mL BMP-7 (B) . Nuclei were stained with Dapi (blue). n = 3 (C) Western blot analysis of pSmad1/5/8 in the cytoplasmic fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after the treatment with BMP-4 for. (n = 5). GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (D) Western blot analysis of pSmad1/5/8 in the nuclear fraction of HTM-N cells after the treatment with 10 ng/mL BMP-4 or BMP-7 for 1 h. Protein synthesis of pSmad1/5/8 was significantly increased after 1 h with both treatments (n = 5). LaminB1 was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. For statistical analysis unpaired two-tailed t -test was used. (E) Real-time RT-PCR analysis of Bmp-4 and Bmp-7 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Bmp-4 and Bmp-7 was significantly reduced after the treatment with CCN2/CTGF ( Bmp-4 : control n = 4, 50 ng/mL CCN2/CTGF n = 3, 100 ng/mL CCN2/CTGF n = 3; Bmp-7 : control n = 5, 50 ng/mL CCN2/CTGF n = 4, 100 ng/mL CCN2/CTGF n = 3). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (F) Real-time RT-PCR analyses of Smad6 , Smad7 , and Id2 after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. mRNA expression of Smad6 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (n = 6). mRNA expression of Smad7 was significantly increased after the treatment with 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression of Id2 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 4). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (G) Western blot analyses of BMP-7 after the treatment with 5 ng/mL, 25 ng/mL, 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h in HMT-N cells. Protein synthesis of BMP-7 was significantly reduced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 4, 5 ng/mL CCN2/CTGF: n = 3, 25 ng/mL CCN2/CTGF: n = 3, 50 ng/mL CCN2/CTGF: n = 3, 100 ng/mL CCN2/CTGF: n = 3). Mean value of wildtype animals (control) was set to 1. α -Tubulin was used to normalize protein synthesis. For statistical analysis the Kruskal–Wallis test was used. (H) Western blot analysis of pSmad1/5/8 after the treatment with 10 ng/mL BMP-4, 60 ng/mL Noggin and 10 ng/mL BMP-4, and 50 ng/mL CCN2/CTGF and 10 ng/mL BMP-4 in HTM-N cells. pSmad1/5/8 protein synthesis was increased after the treatment with BMP-4 (n = 5), compared to untreated control cells and significantly reduced after the treatment with the combination of Noggin and BMP-4 (n = 5) and the combination of CCN2/CTGF and BMP-4 (n = 5), compared to the treatment with BMP-4 only. Mean value of wildtype animals (control) was set to 1. GAPDH was used to normalize protein synthesis. Data represented as mean ± SD. For statistical analysis the One-way ANOVA test was used. * p ≤ 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: Specific antibodies were used as follows: rabbit anti-pSmad1/5/8 (1:1,000, Cell Signaling Technology, Danvers, MA, United States; RRID:AB_331671), goat anti-BMP7 (1:500, Santa Cruz Biotechnology; RRID:AB_2227926), goat anti-BMP4 (1:500, Santa Cruz Biotechnology; RRID:AB_2243391), rabbit anti-Gremlin (1:200, Santa Cruz Biotechnology; RRID:AB_2279266), rabbit anti-TGF- β1 (1:200, Promega), rabbit anti- TGF- β2 (1:200; Santa Cruz Biotechnology), rabbit anti-α-Tubulin (1:2500, Rockland; RRID:AB_2612816), rabbit anti-pSmad2 (1:200, Cell Signaling Technology; RRID:AB_390732), rabbit anti-pSmad3 (1:200, Cell Signaling Technology; RRID:AB_2193207), rabbit anti-GAPDH-HRP (1:5,000, Cell Signaling Technology; RRID:AB_1642205), rabbit anti-LaminB1 (1:1,000; Cell signaling Technology; Cat# 13435, RRID:AB_2737428), chicken anti-goat (HRP, 1:2000, Santa Cruz Biotechnology), chicken anti-goat (AP, 1:2000, Santa Cruz Biotechnology), chicken anti-rabbit (HRP, 1:2000 Cell Signaling Technology) and chicken anti-rabbit (AP, 1:2000, Santa Cruz Biotechnology). α -Tubulin, GAPDH and total protein staining with Coomassie were used as loading control to normalize the signal intensity of the Western blots.

Techniques: In Vitro, Activity Assay, Staining, Western Blot, Two Tailed Test, Quantitative RT-PCR, Expressing

TGF-β signaling in CCN2/CTGF treated HTM-N cells in vitro and in βB1-CTGF1 mice in vivo . (A) Real-time RT-PCR analyses of Tgf-b1 , Tgf-b2 and Ccn2/Ctgf in HTM-N cells after the treatment with 5 ng/mL, 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h. mRNA expression of Tgf-b1 was significantly increased after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 8, 5 ng/mL CCN2/CTGF: n = 8, 50 ng/mL CCN2/CTGF: n = 6, 100 ng/mL CCN2/CTGF: n = 3). Tgf-b2 mRNA was significantly enhanced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 5, 5 ng/mL CCN2/CTGF: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 5). mRNA expression of Ccn2/Ctgf was significantly increased after the treatment with 5 ng/mL and 50 ng/mL CCN2/CTGF (control: n = 6, 5 ng/mL CCN2/CTGF: n = 6, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 6). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (B) Western blot analysis of TGF-β1 and TGF-β2 in HTM-N cells after the treatment with 5 ng/mL, 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h. Protein synthesis of TGF-β1 was significantly increased after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (n = 4). The protein synthesis of TGF-β2 was significantly enhanced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 6, 5 ng/mL CCN2/CTGF: n = 8, 50 ng/mL CCN2/CTGF: n = 6, 100 ng/mL CCN2/CTGF: n = 5). Right panel shows representative Western Blots for the proteins. Mean value of untreated control cells was set at 1. α -Tubulin was used to normalize protein synthesis. For statistical analysis the Kruskal–Wallis test was used. (C) Real-time RT-PCR analysis of Tgf-b1 and Tgf-b2 in the anterior eye segment of 2-month-old βB1-CTGF1 mice and wildtype littermates. mRNA expression of Tgf-b2 was significantly increased in βB1-CTGF mice, compared to wildtype littermates ( Tgf-b1 : WT: n = 8, TG: n = 6; Tgf-b2 : WT: n = 19, TG: n = 19). For statistical analysis the Mann-Whitney test was used. mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. (D) Western blot analysis of TGF-β2 in the anterior eye segment of 2-month-old βB1-CTGF mice and wildtype littermates. Protein synthesis of TGF-β2 was significantly increased in βB1-CTGF1 mice, compared to wildtype littermates (TGF-β2: WT: n = 6, TG: n = 6). Right panel shows a representative Western blot. α -Tubulin was used to normalize protein synthesis. For statistical analysis the Mann-Whitney test was used. (E) Immunohistochemical staining of TGF-β2 (red) in the anterior chamber of 2-month-old βB1-CTGF1 mice and wildtype littermates. Immunoreactivity of TGF-β2 was increased in the TM of βB1-CTGF mice1, in comparison to wildtype mice. Nuclei were stained with Dapi (blue). n = 5 (F) Western blot analysis of the phosphorylation of Smad2 and Smad3. Protein synthesis of pSmad2 and pSmad3 was significantly increased in βB1-CTGF mice, compared to wildtype littermates (pSMAD2: WT: n = 6, TG: n = 6; pSmad3: WT: n = 7, TG: n = 7). Right panel shows representative Western Blots for both proteins. α -Tubulin was used to normalize protein synthesis. For statistical analysis the Mann-Whitney test was used. (G) Immunohistochemical staining of pSmad2 (red) in the anterior chamber angle of 2-month-old βB1-CTGF1 mice and wildtype littermates. Immunoreactivity of pSmad2 is increased in the TM of βB1-CTGF1 mice, in comparison to wildtype mice. Nuclei were stained with Dapi (blue). Data represented as mean ± SD. CB: ciliary body, I: iris, C: cornea, TM: trabecular meshwork. n = 5. * p ≤ 0.05, ** p < 0.01, *** p < 0.001.

Journal: Frontiers in Molecular Biosciences

Article Title: CCN2/CTGF tip the balance of growth factors towards TGF-β2 in primary open-angle glaucoma

doi: 10.3389/fmolb.2023.1045411

Figure Lengend Snippet: TGF-β signaling in CCN2/CTGF treated HTM-N cells in vitro and in βB1-CTGF1 mice in vivo . (A) Real-time RT-PCR analyses of Tgf-b1 , Tgf-b2 and Ccn2/Ctgf in HTM-N cells after the treatment with 5 ng/mL, 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h. mRNA expression of Tgf-b1 was significantly increased after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 8, 5 ng/mL CCN2/CTGF: n = 8, 50 ng/mL CCN2/CTGF: n = 6, 100 ng/mL CCN2/CTGF: n = 3). Tgf-b2 mRNA was significantly enhanced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 5, 5 ng/mL CCN2/CTGF: n = 5, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 5). mRNA expression of Ccn2/Ctgf was significantly increased after the treatment with 5 ng/mL and 50 ng/mL CCN2/CTGF (control: n = 6, 5 ng/mL CCN2/CTGF: n = 6, 50 ng/mL CCN2/CTGF: n = 5, 100 ng/mL CCN2/CTGF: n = 6). mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. For statistical analysis the Kruskal–Wallis test was used. (B) Western blot analysis of TGF-β1 and TGF-β2 in HTM-N cells after the treatment with 5 ng/mL, 50 ng/mL and 100 ng/mL CCN2/CTGF for 24 h. Protein synthesis of TGF-β1 was significantly increased after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (n = 4). The protein synthesis of TGF-β2 was significantly enhanced after the treatment with 50 ng/mL and 100 ng/mL CCN2/CTGF (control: n = 6, 5 ng/mL CCN2/CTGF: n = 8, 50 ng/mL CCN2/CTGF: n = 6, 100 ng/mL CCN2/CTGF: n = 5). Right panel shows representative Western Blots for the proteins. Mean value of untreated control cells was set at 1. α -Tubulin was used to normalize protein synthesis. For statistical analysis the Kruskal–Wallis test was used. (C) Real-time RT-PCR analysis of Tgf-b1 and Tgf-b2 in the anterior eye segment of 2-month-old βB1-CTGF1 mice and wildtype littermates. mRNA expression of Tgf-b2 was significantly increased in βB1-CTGF mice, compared to wildtype littermates ( Tgf-b1 : WT: n = 8, TG: n = 6; Tgf-b2 : WT: n = 19, TG: n = 19). For statistical analysis the Mann-Whitney test was used. mRNA expression was normalized to Gnb2l, and mean value of untreated control cells was set to 1. (D) Western blot analysis of TGF-β2 in the anterior eye segment of 2-month-old βB1-CTGF mice and wildtype littermates. Protein synthesis of TGF-β2 was significantly increased in βB1-CTGF1 mice, compared to wildtype littermates (TGF-β2: WT: n = 6, TG: n = 6). Right panel shows a representative Western blot. α -Tubulin was used to normalize protein synthesis. For statistical analysis the Mann-Whitney test was used. (E) Immunohistochemical staining of TGF-β2 (red) in the anterior chamber of 2-month-old βB1-CTGF1 mice and wildtype littermates. Immunoreactivity of TGF-β2 was increased in the TM of βB1-CTGF mice1, in comparison to wildtype mice. Nuclei were stained with Dapi (blue). n = 5 (F) Western blot analysis of the phosphorylation of Smad2 and Smad3. Protein synthesis of pSmad2 and pSmad3 was significantly increased in βB1-CTGF mice, compared to wildtype littermates (pSMAD2: WT: n = 6, TG: n = 6; pSmad3: WT: n = 7, TG: n = 7). Right panel shows representative Western Blots for both proteins. α -Tubulin was used to normalize protein synthesis. For statistical analysis the Mann-Whitney test was used. (G) Immunohistochemical staining of pSmad2 (red) in the anterior chamber angle of 2-month-old βB1-CTGF1 mice and wildtype littermates. Immunoreactivity of pSmad2 is increased in the TM of βB1-CTGF1 mice, in comparison to wildtype mice. Nuclei were stained with Dapi (blue). Data represented as mean ± SD. CB: ciliary body, I: iris, C: cornea, TM: trabecular meshwork. n = 5. * p ≤ 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: Specific antibodies were used as follows: rabbit anti-pSmad1/5/8 (1:1,000, Cell Signaling Technology, Danvers, MA, United States; RRID:AB_331671), goat anti-BMP7 (1:500, Santa Cruz Biotechnology; RRID:AB_2227926), goat anti-BMP4 (1:500, Santa Cruz Biotechnology; RRID:AB_2243391), rabbit anti-Gremlin (1:200, Santa Cruz Biotechnology; RRID:AB_2279266), rabbit anti-TGF- β1 (1:200, Promega), rabbit anti- TGF- β2 (1:200; Santa Cruz Biotechnology), rabbit anti-α-Tubulin (1:2500, Rockland; RRID:AB_2612816), rabbit anti-pSmad2 (1:200, Cell Signaling Technology; RRID:AB_390732), rabbit anti-pSmad3 (1:200, Cell Signaling Technology; RRID:AB_2193207), rabbit anti-GAPDH-HRP (1:5,000, Cell Signaling Technology; RRID:AB_1642205), rabbit anti-LaminB1 (1:1,000; Cell signaling Technology; Cat# 13435, RRID:AB_2737428), chicken anti-goat (HRP, 1:2000, Santa Cruz Biotechnology), chicken anti-goat (AP, 1:2000, Santa Cruz Biotechnology), chicken anti-rabbit (HRP, 1:2000 Cell Signaling Technology) and chicken anti-rabbit (AP, 1:2000, Santa Cruz Biotechnology). α -Tubulin, GAPDH and total protein staining with Coomassie were used as loading control to normalize the signal intensity of the Western blots.

Techniques: In Vitro, In Vivo, Quantitative RT-PCR, Expressing, Western Blot, MANN-WHITNEY, Immunohistochemical staining, Staining

CCN2/CTGF induced TGF-β signaling activation is mediated via the Erk- and RhoA/ROCK signaling pathway. (A) Real-time RT-PCR analysis of Tgf-b1 , Tgf-b2 and Ccn2/Ctgf in HTM-N cells after the inhibition of the Erk-pathway. After treatment with CCN2/CTGF expression of Tgf-b1 , Tgf-b2 , and Ccn2/Ctgf was significantly higher than in DMSO treated control cells. Combined treatment with the Mek1/2 inhibitor and CCN2/CTGF did not lead to changes in expression compared to DMSO treated control cells, but the upregulation was significantly inhibited compared to cells treated with CCN2/CTGF only. Tgf-b2 and Ccn2/Ctgf mRNA expression was significantly reduced after the treatment with the Mek1/2 inhibitor only, compared to DMSO treated control cells (n ≥ 4; # p ≤ .05, ## p < 0.01 to DMSO control; * p ≤ 0.05, ** p < 0.01 to CCN2/CTGF treatment only). (B) Western blot analysis of TGF-β1 in HTMN-cells after the inhibition of the Erk-pathway. After the treatment with CCN2/CTGF protein synthesis of TGF-β1 is significantly increased compared to DMSO treated control cells. Combined treatment with the Mek1/2 inhibitor and CCN2/CTGF did not lead to changes in protein synthesis compared to DMSO treated control cells, but the upregulation was significantly blocked compared to cells treated with CCN2/CTGF only (n ≥ 4, # p ≤ 0.05 to DMSO control; * p ≤ 0.05 to CCN2/CTGF treatment only). Right panel shows a representative Western blot. Mean value of untreated control cells was set at 1. α -Tubulin was used to normalize protein synthesis. (C) Western blot analysis of TGF-β2 in HTMN-cells after the inhibition of the Erk-pathway. After the treatment with CCN2/CTGF protein synthesis of TGF-β2 is significantly increased compared to DMSO treated control cells. Combined treatment with the Mek1/2 inhibitor and CCN2/CTGF did not lead to changes in protein synthesis compared to DMSO treated control cells, but the upregulation was significantly blocked compared to cells treated with CCN2/CTGF only (n = 4, # p ≤ 0.05 to DMSO control; * p ≤ 0.05 to CCN2/CTGF treatment only). Total protein stained with Coomassie was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. (D) Real-time RT-PCR analyses of Tgf-b1 , Tgf-b2 , and Ccn2/Ctgf in HTM-N cells after the inhibition of the RhoA/ROCK signaling pathway. After treatment with CCN2/CTGF expression of Tgf-b1 , Tgf-b2 , and Ccn2/Ctgf was significantly higher than in DMSO treated control cells. Combined treatment with Fasudil and CCN2/CTGF did not lead to changes in expression compared to DMSO treated control cells, but the upregulation was significantly inhibited compared to cells treated with CCN2/CTGF only. Tgf-b2 and Ccn2/Ctgf mRNA expression was significantly reduced after the treatment with the Fasudil only, compared to DMSO treated control cells (n ≥ 5; # p ≤ 0.05, ## p < 0.01 to DMSO control; * p ≤ 0.05, ** p < 0.01 to CCN2/CTGF treatment only). (E) Western blot analysis of TGF-β1 in HTMN-cells after the inhibition of the RhoA/ROCK signaling pathway. After the treatment with CCN2/CTGF protein synthesis of TGF-β1 is significantly increased compared to DMSO treated control cells. Combined treatment with Fasudil and CCN2/CTGF did not lead to changes in protein synthesis compared to DMSO treated control cells, but the upregulation was significantly blocked compared to cells treated with CCN2/CTGF only (n = 3, # p ≤ 0.05 to DMSO control; ** p < 0.01 to CCN2/CTGF treatment only). Right panel shows a representative Western blot. Mean value of untreated control cells was set to1. α -Tubulin was used to normalize protein synthesis. (F) Western blot analysis of TGF-β2 in HTMN-cells after the inhibition of the RhoA/ROCK signaling pathway. After the treatment with CCN2/CTGF protein synthesis of TGF-β2 was significantly increased compared to DMSO treated control cells. Combined treatment with Fasudil and CCN2/CTGF did not lead to changes in protein synthesis compared to DMSO treated control cells, but the upregulation was significantly blocked compared to cells treated with CCN2/CTGF only (n = 7, ## p < 0.01 to DMSO control; * p ≤ 0.05, ** p < 0.01 to CCN2/CTGF treatment only). Total protein stained with Coomassie was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. Dotted line indicates the control group treated with the solvent of the inhibitor for the appropriate experiment. For statistical analysis a one-way ANOVA was performed.

Journal: Frontiers in Molecular Biosciences

Article Title: CCN2/CTGF tip the balance of growth factors towards TGF-β2 in primary open-angle glaucoma

doi: 10.3389/fmolb.2023.1045411

Figure Lengend Snippet: CCN2/CTGF induced TGF-β signaling activation is mediated via the Erk- and RhoA/ROCK signaling pathway. (A) Real-time RT-PCR analysis of Tgf-b1 , Tgf-b2 and Ccn2/Ctgf in HTM-N cells after the inhibition of the Erk-pathway. After treatment with CCN2/CTGF expression of Tgf-b1 , Tgf-b2 , and Ccn2/Ctgf was significantly higher than in DMSO treated control cells. Combined treatment with the Mek1/2 inhibitor and CCN2/CTGF did not lead to changes in expression compared to DMSO treated control cells, but the upregulation was significantly inhibited compared to cells treated with CCN2/CTGF only. Tgf-b2 and Ccn2/Ctgf mRNA expression was significantly reduced after the treatment with the Mek1/2 inhibitor only, compared to DMSO treated control cells (n ≥ 4; # p ≤ .05, ## p < 0.01 to DMSO control; * p ≤ 0.05, ** p < 0.01 to CCN2/CTGF treatment only). (B) Western blot analysis of TGF-β1 in HTMN-cells after the inhibition of the Erk-pathway. After the treatment with CCN2/CTGF protein synthesis of TGF-β1 is significantly increased compared to DMSO treated control cells. Combined treatment with the Mek1/2 inhibitor and CCN2/CTGF did not lead to changes in protein synthesis compared to DMSO treated control cells, but the upregulation was significantly blocked compared to cells treated with CCN2/CTGF only (n ≥ 4, # p ≤ 0.05 to DMSO control; * p ≤ 0.05 to CCN2/CTGF treatment only). Right panel shows a representative Western blot. Mean value of untreated control cells was set at 1. α -Tubulin was used to normalize protein synthesis. (C) Western blot analysis of TGF-β2 in HTMN-cells after the inhibition of the Erk-pathway. After the treatment with CCN2/CTGF protein synthesis of TGF-β2 is significantly increased compared to DMSO treated control cells. Combined treatment with the Mek1/2 inhibitor and CCN2/CTGF did not lead to changes in protein synthesis compared to DMSO treated control cells, but the upregulation was significantly blocked compared to cells treated with CCN2/CTGF only (n = 4, # p ≤ 0.05 to DMSO control; * p ≤ 0.05 to CCN2/CTGF treatment only). Total protein stained with Coomassie was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. (D) Real-time RT-PCR analyses of Tgf-b1 , Tgf-b2 , and Ccn2/Ctgf in HTM-N cells after the inhibition of the RhoA/ROCK signaling pathway. After treatment with CCN2/CTGF expression of Tgf-b1 , Tgf-b2 , and Ccn2/Ctgf was significantly higher than in DMSO treated control cells. Combined treatment with Fasudil and CCN2/CTGF did not lead to changes in expression compared to DMSO treated control cells, but the upregulation was significantly inhibited compared to cells treated with CCN2/CTGF only. Tgf-b2 and Ccn2/Ctgf mRNA expression was significantly reduced after the treatment with the Fasudil only, compared to DMSO treated control cells (n ≥ 5; # p ≤ 0.05, ## p < 0.01 to DMSO control; * p ≤ 0.05, ** p < 0.01 to CCN2/CTGF treatment only). (E) Western blot analysis of TGF-β1 in HTMN-cells after the inhibition of the RhoA/ROCK signaling pathway. After the treatment with CCN2/CTGF protein synthesis of TGF-β1 is significantly increased compared to DMSO treated control cells. Combined treatment with Fasudil and CCN2/CTGF did not lead to changes in protein synthesis compared to DMSO treated control cells, but the upregulation was significantly blocked compared to cells treated with CCN2/CTGF only (n = 3, # p ≤ 0.05 to DMSO control; ** p < 0.01 to CCN2/CTGF treatment only). Right panel shows a representative Western blot. Mean value of untreated control cells was set to1. α -Tubulin was used to normalize protein synthesis. (F) Western blot analysis of TGF-β2 in HTMN-cells after the inhibition of the RhoA/ROCK signaling pathway. After the treatment with CCN2/CTGF protein synthesis of TGF-β2 was significantly increased compared to DMSO treated control cells. Combined treatment with Fasudil and CCN2/CTGF did not lead to changes in protein synthesis compared to DMSO treated control cells, but the upregulation was significantly blocked compared to cells treated with CCN2/CTGF only (n = 7, ## p < 0.01 to DMSO control; * p ≤ 0.05, ** p < 0.01 to CCN2/CTGF treatment only). Total protein stained with Coomassie was used to normalize protein synthesis. Data represented as mean ± SD. Right panel shows a representative Western blot. Dotted line indicates the control group treated with the solvent of the inhibitor for the appropriate experiment. For statistical analysis a one-way ANOVA was performed.

Article Snippet: Specific antibodies were used as follows: rabbit anti-pSmad1/5/8 (1:1,000, Cell Signaling Technology, Danvers, MA, United States; RRID:AB_331671), goat anti-BMP7 (1:500, Santa Cruz Biotechnology; RRID:AB_2227926), goat anti-BMP4 (1:500, Santa Cruz Biotechnology; RRID:AB_2243391), rabbit anti-Gremlin (1:200, Santa Cruz Biotechnology; RRID:AB_2279266), rabbit anti-TGF- β1 (1:200, Promega), rabbit anti- TGF- β2 (1:200; Santa Cruz Biotechnology), rabbit anti-α-Tubulin (1:2500, Rockland; RRID:AB_2612816), rabbit anti-pSmad2 (1:200, Cell Signaling Technology; RRID:AB_390732), rabbit anti-pSmad3 (1:200, Cell Signaling Technology; RRID:AB_2193207), rabbit anti-GAPDH-HRP (1:5,000, Cell Signaling Technology; RRID:AB_1642205), rabbit anti-LaminB1 (1:1,000; Cell signaling Technology; Cat# 13435, RRID:AB_2737428), chicken anti-goat (HRP, 1:2000, Santa Cruz Biotechnology), chicken anti-goat (AP, 1:2000, Santa Cruz Biotechnology), chicken anti-rabbit (HRP, 1:2000 Cell Signaling Technology) and chicken anti-rabbit (AP, 1:2000, Santa Cruz Biotechnology). α -Tubulin, GAPDH and total protein staining with Coomassie were used as loading control to normalize the signal intensity of the Western blots.

Techniques: Activation Assay, Quantitative RT-PCR, Inhibition, Expressing, Western Blot, Staining

Soleus muscle morphometric analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed HDAC4. (A) Representative immunofluorescence photomicrographs of soleus muscle, laminin (green) and DAPI (blue, used for nuclei identification) (scale bar 100 μm) and hematoxylin–eosin staining (scale bar 50 μm). The asterisk corresponds to the same fiber in both HE and immunofluorescence technique. (B) Soleus muscle mass, (C) whole muscle CSA, (D) fiber CSA and (E) fiber distribution from EV, pCMVHDAC4, Imm/pCMVHDAC4 and Imm + Leu/pCMVHDAC4 groups. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001 ( n = 5 per group).

Journal: Muscle & Nerve

Article Title: Leucine Supplementation Counteracts the Atrophic Effects of HDAC4 in Rat Skeletal Muscle Submitted to Hindlimb Immobilization

doi: 10.1002/mus.28411

Figure Lengend Snippet: Soleus muscle morphometric analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed HDAC4. (A) Representative immunofluorescence photomicrographs of soleus muscle, laminin (green) and DAPI (blue, used for nuclei identification) (scale bar 100 μm) and hematoxylin–eosin staining (scale bar 50 μm). The asterisk corresponds to the same fiber in both HE and immunofluorescence technique. (B) Soleus muscle mass, (C) whole muscle CSA, (D) fiber CSA and (E) fiber distribution from EV, pCMVHDAC4, Imm/pCMVHDAC4 and Imm + Leu/pCMVHDAC4 groups. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001 ( n = 5 per group).

Article Snippet: After 30 min, muscles were injected with 50 μL of the HDAC4 expression vector (1.0 μg/μL, pCMVHDAC4, Origene CAT#: RR217458, Rockville, MD, USA) or the empty vector (EV) and an electric pulse generator delivered a burst of pulses (6 pulses of 20 ms with 980 ms pause, 25 V).

Techniques: Immunofluorescence, Staining

HDAC4 protein expression analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed HDAC4. (A) HDAC4 and GAPDH western blot showing representative bands. (B) Densitometry analysis by using GAPDH protein level as loading control. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . ** p < 0.01 ( n = 5 per group).

Journal: Muscle & Nerve

Article Title: Leucine Supplementation Counteracts the Atrophic Effects of HDAC4 in Rat Skeletal Muscle Submitted to Hindlimb Immobilization

doi: 10.1002/mus.28411

Figure Lengend Snippet: HDAC4 protein expression analysis after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed HDAC4. (A) HDAC4 and GAPDH western blot showing representative bands. (B) Densitometry analysis by using GAPDH protein level as loading control. Data are expressed as mean ± SEM. Statistical analysis included the two‐way ANOVA test followed by Tukey's post hoc . ** p < 0.01 ( n = 5 per group).

Article Snippet: After 30 min, muscles were injected with 50 μL of the HDAC4 expression vector (1.0 μg/μL, pCMVHDAC4, Origene CAT#: RR217458, Rockville, MD, USA) or the empty vector (EV) and an electric pulse generator delivered a burst of pulses (6 pulses of 20 ms with 980 ms pause, 25 V).

Techniques: Expressing, Western Blot, Control

Effect of leucine on HDAC4 canonical pathway in animals that overexpressed HDAC4. (A) HDAC4 and (B) Atrogin‐1 mRNA levels were determined by qPCR. (C) Schematic illustrating HDAC4 action in the skeletal muscle fiber nucleus. Cyclophilin A expression was used as housekeeping. Data were expressed as mean ± SEM. Statistical analysis included one‐way ANOVA followed by Tukey's post hoc test. * p < 0.05; ** p < 0.01 ( n = 5 per group).

Journal: Muscle & Nerve

Article Title: Leucine Supplementation Counteracts the Atrophic Effects of HDAC4 in Rat Skeletal Muscle Submitted to Hindlimb Immobilization

doi: 10.1002/mus.28411

Figure Lengend Snippet: Effect of leucine on HDAC4 canonical pathway in animals that overexpressed HDAC4. (A) HDAC4 and (B) Atrogin‐1 mRNA levels were determined by qPCR. (C) Schematic illustrating HDAC4 action in the skeletal muscle fiber nucleus. Cyclophilin A expression was used as housekeeping. Data were expressed as mean ± SEM. Statistical analysis included one‐way ANOVA followed by Tukey's post hoc test. * p < 0.05; ** p < 0.01 ( n = 5 per group).

Article Snippet: After 30 min, muscles were injected with 50 μL of the HDAC4 expression vector (1.0 μg/μL, pCMVHDAC4, Origene CAT#: RR217458, Rockville, MD, USA) or the empty vector (EV) and an electric pulse generator delivered a burst of pulses (6 pulses of 20 ms with 980 ms pause, 25 V).

Techniques: Expressing

HDAC4 nuclei localization after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed HDAC4. (A) Representative immunofluorescence photomicrographs of HDAC4 in soleus muscle, HDAC4 (red), DAPI (blue, used for nuclei identification) (scale bar 100 μm). (B) Number of positive HDAC4 nuclei per total nuclei (%). Data were expressed as mean ± SEM. Statistical analysis included two‐way ANOVA followed by Tukey's post hoc test. * p < 0.05; ** p < 0.01 ( n = 5 per group).

Journal: Muscle & Nerve

Article Title: Leucine Supplementation Counteracts the Atrophic Effects of HDAC4 in Rat Skeletal Muscle Submitted to Hindlimb Immobilization

doi: 10.1002/mus.28411

Figure Lengend Snippet: HDAC4 nuclei localization after 7 days of hind limb immobilization and leucine supplementation in animals that overexpressed HDAC4. (A) Representative immunofluorescence photomicrographs of HDAC4 in soleus muscle, HDAC4 (red), DAPI (blue, used for nuclei identification) (scale bar 100 μm). (B) Number of positive HDAC4 nuclei per total nuclei (%). Data were expressed as mean ± SEM. Statistical analysis included two‐way ANOVA followed by Tukey's post hoc test. * p < 0.05; ** p < 0.01 ( n = 5 per group).

Article Snippet: After 30 min, muscles were injected with 50 μL of the HDAC4 expression vector (1.0 μg/μL, pCMVHDAC4, Origene CAT#: RR217458, Rockville, MD, USA) or the empty vector (EV) and an electric pulse generator delivered a burst of pulses (6 pulses of 20 ms with 980 ms pause, 25 V).

Techniques: Immunofluorescence