dc plus protein assay kit Search Results


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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).
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Chem Impex International glycerol chem impex
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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Bio-Rad dc assay
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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Bio-Rad rc dc lowry protein assay
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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96
Bio-Rad dctm protein assay
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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Bio-Rad rcdc assay kit
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).
Rcdc Assay Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
Norgen Biotek rna dna protein purification kit
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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90
Sangon Biotech immunoprecipitation protein a/g plus agarose kit
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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Proteigene rna/dna/protein purification plus kit
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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Click Chemistry Tools click-&-go plus 555 opp protein synthesis assay kit
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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Amersham Life Sciences Inc silver staining kit - protein plus 0ne tm
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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Bangs Laboratories biomag amine biomagplus amine protein coupling kit
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