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93
Dojindo Labs sulfobiotics protein redox state monitoring kit plus
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Sulfobiotics Protein Redox State Monitoring Kit Plus, supplied by Dojindo Labs, 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/state/pmc07914443-126-9-20?v=Dojindo+Labs
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96
Mini-Circuits xy8
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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86
Tokyo Chemical Industry tci state
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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86
Tokyo Chemical Industry state pool
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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93
Carl Zeiss microscopy camera axiocam 702 mono
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Microscopy Camera Axiocam 702 Mono, supplied by Carl Zeiss, 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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97
AutoMate Scientific Inc grid floors
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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94
Carl Zeiss type ryb uv light source
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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type ryb uv light source - by Bioz Stars, 2026-07
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96
Carl Zeiss colibri 7
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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93
Carl Zeiss colibri 5 type rgb uv light source
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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93
Carl Zeiss colibri 7 solid state led light source
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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95
Chem Impex International buffer components
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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86
Merck & Co state name
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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Image Search Results


Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - SulfoBiotics - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).

Journal: International Journal of Molecular Sciences

Article Title: Protein Expression of Angiotensin-Converting Enzyme 2 (ACE2) is Upregulated in Brains with Alzheimer’s Disease

doi: 10.3390/ijms22041687

Figure Lengend Snippet: Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - SulfoBiotics - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).

Article Snippet: Protein thiol redox states were monitored using the - SulfoBiotics - Protein Redox State Monitoring Kit Plus (Catalog # SB12; Dojindo Molecular Technologies).

Techniques: Control, Labeling, Electrophoresis, Western Blot