xii Search Results


93
Santa Cruz Biotechnology calpain inhibitor xii
A) Representative Western blot of CAPN1, CAPN2, CAPNS1, CAPN10, CAST, and αII-spectrin in liver samples from male Wistar rats treated with 20% sucrose (S), 50 ppm of sodium arsenite (A) or both (A + S) through drinking water for 8 weeks. Coomassie brilliant blue (CBB) staining was used as a loading control. B) Quantification of the protein abundance of the members of the <t>calpain</t> system. C) Quantification of the intact αII-spectrin (240 kDa), the fragment generated by calpain activity (140 kDa) and the ratio of the abundance of the fragment/ intact αII-spectrin. The optical density of the bands was normalized to the optical density of the entire CBB lane. Data are presented as fold change relative to the mean value of the control animals. The bars denote the mean ± SD of at least 5 animals per condition. Each animal is represented by dots. Analysis by two-way ANOVA with Tukey’s post-hoc test. * denotes statistically significant differences in the post-hoc test with p < 0.05.
Calpain Inhibitor Xii, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
Novus Biologicals ca12
A) Representative Western blot of CAPN1, CAPN2, CAPNS1, CAPN10, CAST, and αII-spectrin in liver samples from male Wistar rats treated with 20% sucrose (S), 50 ppm of sodium arsenite (A) or both (A + S) through drinking water for 8 weeks. Coomassie brilliant blue (CBB) staining was used as a loading control. B) Quantification of the protein abundance of the members of the <t>calpain</t> system. C) Quantification of the intact αII-spectrin (240 kDa), the fragment generated by calpain activity (140 kDa) and the ratio of the abundance of the fragment/ intact αII-spectrin. The optical density of the bands was normalized to the optical density of the entire CBB lane. Data are presented as fold change relative to the mean value of the control animals. The bars denote the mean ± SD of at least 5 animals per condition. Each animal is represented by dots. Analysis by two-way ANOVA with Tukey’s post-hoc test. * denotes statistically significant differences in the post-hoc test with p < 0.05.
Ca12, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Addgene inc pcfb2909
A) Representative Western blot of CAPN1, CAPN2, CAPNS1, CAPN10, CAST, and αII-spectrin in liver samples from male Wistar rats treated with 20% sucrose (S), 50 ppm of sodium arsenite (A) or both (A + S) through drinking water for 8 weeks. Coomassie brilliant blue (CBB) staining was used as a loading control. B) Quantification of the protein abundance of the members of the <t>calpain</t> system. C) Quantification of the intact αII-spectrin (240 kDa), the fragment generated by calpain activity (140 kDa) and the ratio of the abundance of the fragment/ intact αII-spectrin. The optical density of the bands was normalized to the optical density of the entire CBB lane. Data are presented as fold change relative to the mean value of the control animals. The bars denote the mean ± SD of at least 5 animals per condition. Each animal is represented by dots. Analysis by two-way ANOVA with Tukey’s post-hoc test. * denotes statistically significant differences in the post-hoc test with p < 0.05.
Pcfb2909, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Santa Cruz Biotechnology light chain
A) Representative Western blot of CAPN1, CAPN2, CAPNS1, CAPN10, CAST, and αII-spectrin in liver samples from male Wistar rats treated with 20% sucrose (S), 50 ppm of sodium arsenite (A) or both (A + S) through drinking water for 8 weeks. Coomassie brilliant blue (CBB) staining was used as a loading control. B) Quantification of the protein abundance of the members of the <t>calpain</t> system. C) Quantification of the intact αII-spectrin (240 kDa), the fragment generated by calpain activity (140 kDa) and the ratio of the abundance of the fragment/ intact αII-spectrin. The optical density of the bands was normalized to the optical density of the entire CBB lane. Data are presented as fold change relative to the mean value of the control animals. The bars denote the mean ± SD of at least 5 animals per condition. Each animal is represented by dots. Analysis by two-way ANOVA with Tukey’s post-hoc test. * denotes statistically significant differences in the post-hoc test with p < 0.05.
Light Chain, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Novus Biologicals rabbit polyclonal anti collagen type iii alpha 1 antibody
Figure 1. α-SMA, Col I and <t>Col</t> <t>III</t> expression. (A) α-SMA, Col I, and Col III protein expression of myofibroblasts at 48 h of CRET or sham treatment. Fluorescence intensity measurement per MHC channel. Data normalized over the corresponding sham-exposed controls (dashed line represents the
Rabbit Polyclonal Anti Collagen Type Iii Alpha 1 Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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91
Santa Cruz Biotechnology myosin heavy chain
Figure 1. α-SMA, Col I and <t>Col</t> <t>III</t> expression. (A) α-SMA, Col I, and Col III protein expression of myofibroblasts at 48 h of CRET or sham treatment. Fluorescence intensity measurement per MHC channel. Data normalized over the corresponding sham-exposed controls (dashed line represents the
Myosin Heavy Chain, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Novus Biologicals human type xii collagen
Figure 1. α-SMA, Col I and <t>Col</t> <t>III</t> expression. (A) α-SMA, Col I, and Col III protein expression of myofibroblasts at 48 h of CRET or sham treatment. Fluorescence intensity measurement per MHC channel. Data normalized over the corresponding sham-exposed controls (dashed line represents the
Human Type Xii Collagen, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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86
R&D Systems Hematology goat anti mcar12
Figure 1. α-SMA, Col I and <t>Col</t> <t>III</t> expression. (A) α-SMA, Col I, and Col III protein expression of myofibroblasts at 48 h of CRET or sham treatment. Fluorescence intensity measurement per MHC channel. Data normalized over the corresponding sham-exposed controls (dashed line represents the
Goat Anti Mcar12, supplied by R&D Systems Hematology, 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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R&D Systems Hematology caix
Figure 1. α-SMA, Col I and <t>Col</t> <t>III</t> expression. (A) α-SMA, Col I, and Col III protein expression of myofibroblasts at 48 h of CRET or sham treatment. Fluorescence intensity measurement per MHC channel. Data normalized over the corresponding sham-exposed controls (dashed line represents the
Caix, supplied by R&D Systems Hematology, 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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92
Santa Cruz Biotechnology antibody against fxii
Figure 1. α-SMA, Col I and <t>Col</t> <t>III</t> expression. (A) α-SMA, Col I, and Col III protein expression of myofibroblasts at 48 h of CRET or sham treatment. Fluorescence intensity measurement per MHC channel. Data normalized over the corresponding sham-exposed controls (dashed line represents the
Antibody Against Fxii, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Santa Cruz Biotechnology ca xii sirna
Effects of A6 and A15 on the viability of MCF-7 and SK-BR-3 cells transfected with <t>siRNA</t> targeting CA IX, II, or <t>XII.</t> MCF-7 and SK-BR-3 cells were transfected with control siRNA or siRNA targeting ( A ) CA IX, ( B ) CA II, and ( C ) CA XII. Western blotting analyses were performed as described in the Materials and Methods to confirm the efficiency of the respective knockdown. Representative blots are shown. Transfected cells were exposed to A6 or A15 at 50 µM for 48 h. Control cells were treated with the media containing 0.1% DMSO instead. Cell viability was determined by MTT assay as described in the Materials and Methods and expressed as a percentage of the control measured in the vehicle (DMSO)-treated cells transfected with control siRNA. Data are displayed as mean ± SEM from at least three independent experiments. * p < 0.05 vs. the vehicle-treated control cells transfected with control siRNA. ns, not significant.
Ca Xii Sirna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Novus Biologicals novus biologicals nbp2
Effects of A6 and A15 on the viability of MCF-7 and SK-BR-3 cells transfected with <t>siRNA</t> targeting CA IX, II, or <t>XII.</t> MCF-7 and SK-BR-3 cells were transfected with control siRNA or siRNA targeting ( A ) CA IX, ( B ) CA II, and ( C ) CA XII. Western blotting analyses were performed as described in the Materials and Methods to confirm the efficiency of the respective knockdown. Representative blots are shown. Transfected cells were exposed to A6 or A15 at 50 µM for 48 h. Control cells were treated with the media containing 0.1% DMSO instead. Cell viability was determined by MTT assay as described in the Materials and Methods and expressed as a percentage of the control measured in the vehicle (DMSO)-treated cells transfected with control siRNA. Data are displayed as mean ± SEM from at least three independent experiments. * p < 0.05 vs. the vehicle-treated control cells transfected with control siRNA. ns, not significant.
Novus Biologicals Nbp2, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


A) Representative Western blot of CAPN1, CAPN2, CAPNS1, CAPN10, CAST, and αII-spectrin in liver samples from male Wistar rats treated with 20% sucrose (S), 50 ppm of sodium arsenite (A) or both (A + S) through drinking water for 8 weeks. Coomassie brilliant blue (CBB) staining was used as a loading control. B) Quantification of the protein abundance of the members of the calpain system. C) Quantification of the intact αII-spectrin (240 kDa), the fragment generated by calpain activity (140 kDa) and the ratio of the abundance of the fragment/ intact αII-spectrin. The optical density of the bands was normalized to the optical density of the entire CBB lane. Data are presented as fold change relative to the mean value of the control animals. The bars denote the mean ± SD of at least 5 animals per condition. Each animal is represented by dots. Analysis by two-way ANOVA with Tukey’s post-hoc test. * denotes statistically significant differences in the post-hoc test with p < 0.05.

Journal: PLOS One

Article Title: Sucrose but not arsenic induce hepatic steatosis which correlates with calpain-1 inhibition

doi: 10.1371/journal.pone.0339586

Figure Lengend Snippet: A) Representative Western blot of CAPN1, CAPN2, CAPNS1, CAPN10, CAST, and αII-spectrin in liver samples from male Wistar rats treated with 20% sucrose (S), 50 ppm of sodium arsenite (A) or both (A + S) through drinking water for 8 weeks. Coomassie brilliant blue (CBB) staining was used as a loading control. B) Quantification of the protein abundance of the members of the calpain system. C) Quantification of the intact αII-spectrin (240 kDa), the fragment generated by calpain activity (140 kDa) and the ratio of the abundance of the fragment/ intact αII-spectrin. The optical density of the bands was normalized to the optical density of the entire CBB lane. Data are presented as fold change relative to the mean value of the control animals. The bars denote the mean ± SD of at least 5 animals per condition. Each animal is represented by dots. Analysis by two-way ANOVA with Tukey’s post-hoc test. * denotes statistically significant differences in the post-hoc test with p < 0.05.

Article Snippet: The cells were treated 24 h after seeding with 10, 50 and 100 μM of calpain inhibitor XII (Santa Cruz Biotechnology), equimolar concentrations of glucose and fructose (15 and 25 mM) or 1 μM sodium arsenite for 72 h. Control cells were treated with vehicle (dimethyl sulfoxide).

Techniques: Western Blot, Staining, Control, Quantitative Proteomics, Generated, Activity Assay

A) Cell viability of HepG2 cells treated with calpain inhibitor XII for 72 h. Puro: positive control of cells treated with puromycin. B) Lipid accumulation in HepG2 cells treated with calpain inhibitor XII for 72 h. Data are expressed as the absorbance of ORO staining at 515 nm and normalized to protein content in the well. C) Representative Western blot and quantification of the abundance of PPARγ in HepG2 cells treated with calpain inhibitor XII. In A and B the bars denote the mean ± SD of 3 independent experiments with technical triplicates. In C the bars denote the mean ± SD of 5 independent experiments. Each point represents each well evaluated. Analysis by one-way ANOVA with Tukey’s post-hoc test. * denotes statistically significant differences in the post-hoc test with p < 0.05.

Journal: PLOS One

Article Title: Sucrose but not arsenic induce hepatic steatosis which correlates with calpain-1 inhibition

doi: 10.1371/journal.pone.0339586

Figure Lengend Snippet: A) Cell viability of HepG2 cells treated with calpain inhibitor XII for 72 h. Puro: positive control of cells treated with puromycin. B) Lipid accumulation in HepG2 cells treated with calpain inhibitor XII for 72 h. Data are expressed as the absorbance of ORO staining at 515 nm and normalized to protein content in the well. C) Representative Western blot and quantification of the abundance of PPARγ in HepG2 cells treated with calpain inhibitor XII. In A and B the bars denote the mean ± SD of 3 independent experiments with technical triplicates. In C the bars denote the mean ± SD of 5 independent experiments. Each point represents each well evaluated. Analysis by one-way ANOVA with Tukey’s post-hoc test. * denotes statistically significant differences in the post-hoc test with p < 0.05.

Article Snippet: The cells were treated 24 h after seeding with 10, 50 and 100 μM of calpain inhibitor XII (Santa Cruz Biotechnology), equimolar concentrations of glucose and fructose (15 and 25 mM) or 1 μM sodium arsenite for 72 h. Control cells were treated with vehicle (dimethyl sulfoxide).

Techniques: Positive Control, Staining, Western Blot

Figure 1. α-SMA, Col I and Col III expression. (A) α-SMA, Col I, and Col III protein expression of myofibroblasts at 48 h of CRET or sham treatment. Fluorescence intensity measurement per MHC channel. Data normalized over the corresponding sham-exposed controls (dashed line represents the

Journal: International journal of molecular sciences

Article Title: Anti-Fibrotic Effects of RF Electric Currents.

doi: 10.3390/ijms241310986

Figure Lengend Snippet: Figure 1. α-SMA, Col I and Col III expression. (A) α-SMA, Col I, and Col III protein expression of myofibroblasts at 48 h of CRET or sham treatment. Fluorescence intensity measurement per MHC channel. Data normalized over the corresponding sham-exposed controls (dashed line represents the

Article Snippet: At the end of 48 h RF- or sham-exposure, the samples were fixed with 4% paraformaldehyde (Merck, Darmstadt, Germany) and incubated overnight at 4 ◦C with mouse monoclonal anti- α-smooth muscle actin antibody α-SMA (1:400; cat. no. A 2547; Sigma Aldrich, St. Louis, MO, USA), rabbit polyclonal anti-collagen type I antibody (1:400; cat. no. NB600408-0.1 mg; Novus; Centennial, CO, USA) and rabbit polyclonal anti-collagen type III alpha 1 antibody (1:400, cat. no. NB600-594SS; Novus; CO, USA).

Techniques: Expressing, Fluorescence

Effects of A6 and A15 on the viability of MCF-7 and SK-BR-3 cells transfected with siRNA targeting CA IX, II, or XII. MCF-7 and SK-BR-3 cells were transfected with control siRNA or siRNA targeting ( A ) CA IX, ( B ) CA II, and ( C ) CA XII. Western blotting analyses were performed as described in the Materials and Methods to confirm the efficiency of the respective knockdown. Representative blots are shown. Transfected cells were exposed to A6 or A15 at 50 µM for 48 h. Control cells were treated with the media containing 0.1% DMSO instead. Cell viability was determined by MTT assay as described in the Materials and Methods and expressed as a percentage of the control measured in the vehicle (DMSO)-treated cells transfected with control siRNA. Data are displayed as mean ± SEM from at least three independent experiments. * p < 0.05 vs. the vehicle-treated control cells transfected with control siRNA. ns, not significant.

Journal: International Journal of Molecular Sciences

Article Title: Suppression of Tumor Growth and Cell Migration by Indole-Based Benzenesulfonamides and Their Synergistic Effects in Combination with Doxorubicin

doi: 10.3390/ijms23179903

Figure Lengend Snippet: Effects of A6 and A15 on the viability of MCF-7 and SK-BR-3 cells transfected with siRNA targeting CA IX, II, or XII. MCF-7 and SK-BR-3 cells were transfected with control siRNA or siRNA targeting ( A ) CA IX, ( B ) CA II, and ( C ) CA XII. Western blotting analyses were performed as described in the Materials and Methods to confirm the efficiency of the respective knockdown. Representative blots are shown. Transfected cells were exposed to A6 or A15 at 50 µM for 48 h. Control cells were treated with the media containing 0.1% DMSO instead. Cell viability was determined by MTT assay as described in the Materials and Methods and expressed as a percentage of the control measured in the vehicle (DMSO)-treated cells transfected with control siRNA. Data are displayed as mean ± SEM from at least three independent experiments. * p < 0.05 vs. the vehicle-treated control cells transfected with control siRNA. ns, not significant.

Article Snippet: CA II, CA IX, and CA XII siRNA and control siRNA were provided by Santa Cruz Biotechnology, Inc. (Dallas, TX, USA).

Techniques: Transfection, Control, Western Blot, Knockdown, MTT Assay