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mouse monoclonal antibody against macnos  (Bio-Rad)


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    Bio-Rad mouse monoclonal antibody against macnos
    FIG. 1. SDS-PAGE, native PAGE, and Western blot analysis of mtNOS. Panel A, SDS-PAGE was performed using a 10% polyacryl- amide precast gel (Novex, San Diego, CA) under reducing conditions. The proteins were stained with Coomassie Blue. The mitochondrial fractions were, from left to right: I, 8,000 3 g pellet; II, 150,000 3 g supernatant; III, NADPH eluate from the 29,59-ADP Sepharose 4B column. Mac-Lysate, a lysate of the mouse macrophage RAW 264.7 cell line. The molecular mass of protein markers is indicated in kDa. Panel B, native PAGE was performed using 4–15% gradient polyacrylamide gel stained with Coomassie Blue using PhastSystem from Amersham Pharmacia Biotech. In the same gel, catalase (232 kDa) was run under identical conditions. Panel C, for Western blot analysis, proteins were separated with SDS-PAGE gel under the conditions described under “Materials and Methods.” The proteins were transferred to nitrocellu- lose membranes, and later were incubated with mouse <t>monoclonal</t> antibodies against <t>macNOS.</t> The immunocomplexes were developed using enhanced horseradish peroxidase/luminol chemiluminescence re- action, detected with photographic film.
    Mouse Monoclonal Antibody Against Macnos, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 15901 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse monoclonal antibody against macnos/product/Bio-Rad
    Average 98 stars, based on 15901 article reviews
    mouse monoclonal antibody against macnos - by Bioz Stars, 2026-05
    98/100 stars

    Images

    1) Product Images from "Purification and characterization of a nitric-oxide synthase from rat liver mitochondria."

    Article Title: Purification and characterization of a nitric-oxide synthase from rat liver mitochondria.

    Journal: The Journal of biological chemistry

    doi: 10.1074/jbc.273.18.11044

    FIG. 1. SDS-PAGE, native PAGE, and Western blot analysis of mtNOS. Panel A, SDS-PAGE was performed using a 10% polyacryl- amide precast gel (Novex, San Diego, CA) under reducing conditions. The proteins were stained with Coomassie Blue. The mitochondrial fractions were, from left to right: I, 8,000 3 g pellet; II, 150,000 3 g supernatant; III, NADPH eluate from the 29,59-ADP Sepharose 4B column. Mac-Lysate, a lysate of the mouse macrophage RAW 264.7 cell line. The molecular mass of protein markers is indicated in kDa. Panel B, native PAGE was performed using 4–15% gradient polyacrylamide gel stained with Coomassie Blue using PhastSystem from Amersham Pharmacia Biotech. In the same gel, catalase (232 kDa) was run under identical conditions. Panel C, for Western blot analysis, proteins were separated with SDS-PAGE gel under the conditions described under “Materials and Methods.” The proteins were transferred to nitrocellu- lose membranes, and later were incubated with mouse monoclonal antibodies against macNOS. The immunocomplexes were developed using enhanced horseradish peroxidase/luminol chemiluminescence re- action, detected with photographic film.
    Figure Legend Snippet: FIG. 1. SDS-PAGE, native PAGE, and Western blot analysis of mtNOS. Panel A, SDS-PAGE was performed using a 10% polyacryl- amide precast gel (Novex, San Diego, CA) under reducing conditions. The proteins were stained with Coomassie Blue. The mitochondrial fractions were, from left to right: I, 8,000 3 g pellet; II, 150,000 3 g supernatant; III, NADPH eluate from the 29,59-ADP Sepharose 4B column. Mac-Lysate, a lysate of the mouse macrophage RAW 264.7 cell line. The molecular mass of protein markers is indicated in kDa. Panel B, native PAGE was performed using 4–15% gradient polyacrylamide gel stained with Coomassie Blue using PhastSystem from Amersham Pharmacia Biotech. In the same gel, catalase (232 kDa) was run under identical conditions. Panel C, for Western blot analysis, proteins were separated with SDS-PAGE gel under the conditions described under “Materials and Methods.” The proteins were transferred to nitrocellu- lose membranes, and later were incubated with mouse monoclonal antibodies against macNOS. The immunocomplexes were developed using enhanced horseradish peroxidase/luminol chemiluminescence re- action, detected with photographic film.

    Techniques Used: SDS Page, Clear Native PAGE, Western Blot, Staining, Incubation, Bioprocessing



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    mouse monoclonal antibody against macnos  (Bio-Rad)
    98
    Bio-Rad mouse monoclonal antibody against macnos
    FIG. 1. SDS-PAGE, native PAGE, and Western blot analysis of mtNOS. Panel A, SDS-PAGE was performed using a 10% polyacryl- amide precast gel (Novex, San Diego, CA) under reducing conditions. The proteins were stained with Coomassie Blue. The mitochondrial fractions were, from left to right: I, 8,000 3 g pellet; II, 150,000 3 g supernatant; III, NADPH eluate from the 29,59-ADP Sepharose 4B column. Mac-Lysate, a lysate of the mouse macrophage RAW 264.7 cell line. The molecular mass of protein markers is indicated in kDa. Panel B, native PAGE was performed using 4–15% gradient polyacrylamide gel stained with Coomassie Blue using PhastSystem from Amersham Pharmacia Biotech. In the same gel, catalase (232 kDa) was run under identical conditions. Panel C, for Western blot analysis, proteins were separated with SDS-PAGE gel under the conditions described under “Materials and Methods.” The proteins were transferred to nitrocellu- lose membranes, and later were incubated with mouse <t>monoclonal</t> antibodies against <t>macNOS.</t> The immunocomplexes were developed using enhanced horseradish peroxidase/luminol chemiluminescence re- action, detected with photographic film.
    Mouse Monoclonal Antibody Against Macnos, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse monoclonal antibody against macnos/product/Bio-Rad
    Average 98 stars, based on 1 article reviews
    mouse monoclonal antibody against macnos - by Bioz Stars, 2026-05
    98/100 stars
    		  Buy from Supplier

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    FIG. 1. SDS-PAGE, native PAGE, and Western blot analysis of mtNOS. Panel A, SDS-PAGE was performed using a 10% polyacryl- amide precast gel (Novex, San Diego, CA) under reducing conditions. The proteins were stained with Coomassie Blue. The mitochondrial fractions were, from left to right: I, 8,000 3 g pellet; II, 150,000 3 g supernatant; III, NADPH eluate from the 29,59-ADP Sepharose 4B column. Mac-Lysate, a lysate of the mouse macrophage RAW 264.7 cell line. The molecular mass of protein markers is indicated in kDa. Panel B, native PAGE was performed using 4–15% gradient polyacrylamide gel stained with Coomassie Blue using PhastSystem from Amersham Pharmacia Biotech. In the same gel, catalase (232 kDa) was run under identical conditions. Panel C, for Western blot analysis, proteins were separated with SDS-PAGE gel under the conditions described under “Materials and Methods.” The proteins were transferred to nitrocellu- lose membranes, and later were incubated with mouse monoclonal antibodies against macNOS. The immunocomplexes were developed using enhanced horseradish peroxidase/luminol chemiluminescence re- action, detected with photographic film.

    Journal: The Journal of biological chemistry

    Article Title: Purification and characterization of a nitric-oxide synthase from rat liver mitochondria.

    doi: 10.1074/jbc.273.18.11044

    Figure Lengend Snippet: FIG. 1. SDS-PAGE, native PAGE, and Western blot analysis of mtNOS. Panel A, SDS-PAGE was performed using a 10% polyacryl- amide precast gel (Novex, San Diego, CA) under reducing conditions. The proteins were stained with Coomassie Blue. The mitochondrial fractions were, from left to right: I, 8,000 3 g pellet; II, 150,000 3 g supernatant; III, NADPH eluate from the 29,59-ADP Sepharose 4B column. Mac-Lysate, a lysate of the mouse macrophage RAW 264.7 cell line. The molecular mass of protein markers is indicated in kDa. Panel B, native PAGE was performed using 4–15% gradient polyacrylamide gel stained with Coomassie Blue using PhastSystem from Amersham Pharmacia Biotech. In the same gel, catalase (232 kDa) was run under identical conditions. Panel C, for Western blot analysis, proteins were separated with SDS-PAGE gel under the conditions described under “Materials and Methods.” The proteins were transferred to nitrocellu- lose membranes, and later were incubated with mouse monoclonal antibodies against macNOS. The immunocomplexes were developed using enhanced horseradish peroxidase/luminol chemiluminescence re- action, detected with photographic film.

    Article Snippet: The membranes were thoroughly washed with 0.05% Tween 20 in TBS, and incubated with mouse monoclonal antibody against macNOS (1/2, 500 in 0.05% Tween 20 in TBS) for 2 h. The membranes were extensively washed with 0.05% Tween 20 in TBS, and subsequently incubated with goat antibodies against mouse IgG conjugated with horseradish peroxidase (1/30,000; Bio-Rad) for 1 h. After washing the membranes with 0.05% Tween 20 in TBS, the immunocomplexes were developed using enhanced horseradish peroxidase/luminol chemiluminescence reaction, detected with photographic film (Hyperfilm ECL; Amersham Pharmacia Biotech) recorded after 30 s to 7 min of exposure.

    Techniques: SDS Page, Clear Native PAGE, Western Blot, Staining, Incubation, Bioprocessing