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primary rabbit antibodies against got1  (Proteintech)


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    Structured Review

    Proteintech primary rabbit antibodies against got1
    Scheme showing the intersections between energy metabolism and H 2 S oxidation. Reducing equivalents generated in the cytoplasm are moved to the mitochondrion via the malate–aspartate shuttle comprising a neutral α-ketoglutarate–malate and an electrogenic aspartate–glutamate transporter ( pink ). Conversion of malate to oxaloacetate in the mitochondrion regenerates NADH, which enters the electron transport chain ( purple ) at the level of complex I (CI). The purple arrows denote proton translocation. The sulfide oxidation pathway ( blue ) converts H 2 S to thiosulfate and sulfate with electrons from the oxidation catalyzed by SQOR entering at the level of complex III (CIII) and from sulfite oxidase (SO) at the level of complex IV (CIV). At higher concentrations, H 2 S inhibits CIV. α-KG, MDH1/2, <t>GOT1/2,</t> and IMS denote α-ketoglutarate, malate dehydrogenase 1 and 2, glutamate-oxoglutarate transaminase 1 and 2, and inter mitochondrial membrane space, respectively.
    Primary Rabbit Antibodies Against Got1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/primary rabbit antibodies against got1/product/Proteintech
    Average 93 stars, based on 42 article reviews
    primary rabbit antibodies against got1 - by Bioz Stars, 2026-03
    93/100 stars

    Images

    1) Product Images from "The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis"

    Article Title: The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2021.100736

    Scheme showing the intersections between energy metabolism and H 2 S oxidation. Reducing equivalents generated in the cytoplasm are moved to the mitochondrion via the malate–aspartate shuttle comprising a neutral α-ketoglutarate–malate and an electrogenic aspartate–glutamate transporter ( pink ). Conversion of malate to oxaloacetate in the mitochondrion regenerates NADH, which enters the electron transport chain ( purple ) at the level of complex I (CI). The purple arrows denote proton translocation. The sulfide oxidation pathway ( blue ) converts H 2 S to thiosulfate and sulfate with electrons from the oxidation catalyzed by SQOR entering at the level of complex III (CIII) and from sulfite oxidase (SO) at the level of complex IV (CIV). At higher concentrations, H 2 S inhibits CIV. α-KG, MDH1/2, GOT1/2, and IMS denote α-ketoglutarate, malate dehydrogenase 1 and 2, glutamate-oxoglutarate transaminase 1 and 2, and inter mitochondrial membrane space, respectively.
    Figure Legend Snippet: Scheme showing the intersections between energy metabolism and H 2 S oxidation. Reducing equivalents generated in the cytoplasm are moved to the mitochondrion via the malate–aspartate shuttle comprising a neutral α-ketoglutarate–malate and an electrogenic aspartate–glutamate transporter ( pink ). Conversion of malate to oxaloacetate in the mitochondrion regenerates NADH, which enters the electron transport chain ( purple ) at the level of complex I (CI). The purple arrows denote proton translocation. The sulfide oxidation pathway ( blue ) converts H 2 S to thiosulfate and sulfate with electrons from the oxidation catalyzed by SQOR entering at the level of complex III (CIII) and from sulfite oxidase (SO) at the level of complex IV (CIV). At higher concentrations, H 2 S inhibits CIV. α-KG, MDH1/2, GOT1/2, and IMS denote α-ketoglutarate, malate dehydrogenase 1 and 2, glutamate-oxoglutarate transaminase 1 and 2, and inter mitochondrial membrane space, respectively.

    Techniques Used: Generated, Translocation Assay, Membrane

    Evaluation of signaling mechanisms for sulfide-stimulated aerobic glycolysis. A and B , expression level of GOT1 ( A ) and GOT2 ( B ) in GOT1 and GOT2 KD HT29 cells 96 h after treatment with 1 μg/ml doxycycline. Two shRNA sequences (#1 and 2) were used for targeting GOT1 and GOT2. Western blot analysis using anti-GOT1 antibodies ( left ) and Ponceau S staining of the same membrane showing equal loading ( right ). C and D , activation of glucose consumption ( C ) and lactate production ( D ) by the indicated concentrations of Na 2 S in HT29 scr or GOT1 or GOT2 knockdown cells. The concentration of glucose consumed and lactate produced in 20 min ± Na 2 S treatment. E , representative Western blot analysis of phosphorylated ( upper ) and total (l ower ) pyruvate dehydrogenase in HT29 scr cells after 5 and 15 min ±100 μM Na 2 S. F , Ponceau staining of membranes in ( E ) demonstrating equal protein loading and transfer. G , quantitation of Western blot data for phosphorylated PDH shown in ( E ). The error represents SD on the mean of 4 to 6 experiments, ∗ p < 0.005.
    Figure Legend Snippet: Evaluation of signaling mechanisms for sulfide-stimulated aerobic glycolysis. A and B , expression level of GOT1 ( A ) and GOT2 ( B ) in GOT1 and GOT2 KD HT29 cells 96 h after treatment with 1 μg/ml doxycycline. Two shRNA sequences (#1 and 2) were used for targeting GOT1 and GOT2. Western blot analysis using anti-GOT1 antibodies ( left ) and Ponceau S staining of the same membrane showing equal loading ( right ). C and D , activation of glucose consumption ( C ) and lactate production ( D ) by the indicated concentrations of Na 2 S in HT29 scr or GOT1 or GOT2 knockdown cells. The concentration of glucose consumed and lactate produced in 20 min ± Na 2 S treatment. E , representative Western blot analysis of phosphorylated ( upper ) and total (l ower ) pyruvate dehydrogenase in HT29 scr cells after 5 and 15 min ±100 μM Na 2 S. F , Ponceau staining of membranes in ( E ) demonstrating equal protein loading and transfer. G , quantitation of Western blot data for phosphorylated PDH shown in ( E ). The error represents SD on the mean of 4 to 6 experiments, ∗ p < 0.005.

    Techniques Used: Expressing, shRNA, Western Blot, Staining, Membrane, Activation Assay, Knockdown, Concentration Assay, Produced, Quantitation Assay



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    primary rabbit antibodies against got1  (Proteintech)
    93
    Proteintech primary rabbit antibodies against got1
    Scheme showing the intersections between energy metabolism and H 2 S oxidation. Reducing equivalents generated in the cytoplasm are moved to the mitochondrion via the malate–aspartate shuttle comprising a neutral α-ketoglutarate–malate and an electrogenic aspartate–glutamate transporter ( pink ). Conversion of malate to oxaloacetate in the mitochondrion regenerates NADH, which enters the electron transport chain ( purple ) at the level of complex I (CI). The purple arrows denote proton translocation. The sulfide oxidation pathway ( blue ) converts H 2 S to thiosulfate and sulfate with electrons from the oxidation catalyzed by SQOR entering at the level of complex III (CIII) and from sulfite oxidase (SO) at the level of complex IV (CIV). At higher concentrations, H 2 S inhibits CIV. α-KG, MDH1/2, <t>GOT1/2,</t> and IMS denote α-ketoglutarate, malate dehydrogenase 1 and 2, glutamate-oxoglutarate transaminase 1 and 2, and inter mitochondrial membrane space, respectively.
    Primary Rabbit Antibodies Against Got1, 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/result/primary rabbit antibodies against got1/product/Proteintech
    Average 93 stars, based on 1 article reviews
    primary rabbit antibodies against got1 - by Bioz Stars, 2026-03
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Scheme showing the intersections between energy metabolism and H 2 S oxidation. Reducing equivalents generated in the cytoplasm are moved to the mitochondrion via the malate–aspartate shuttle comprising a neutral α-ketoglutarate–malate and an electrogenic aspartate–glutamate transporter ( pink ). Conversion of malate to oxaloacetate in the mitochondrion regenerates NADH, which enters the electron transport chain ( purple ) at the level of complex I (CI). The purple arrows denote proton translocation. The sulfide oxidation pathway ( blue ) converts H 2 S to thiosulfate and sulfate with electrons from the oxidation catalyzed by SQOR entering at the level of complex III (CIII) and from sulfite oxidase (SO) at the level of complex IV (CIV). At higher concentrations, H 2 S inhibits CIV. α-KG, MDH1/2, GOT1/2, and IMS denote α-ketoglutarate, malate dehydrogenase 1 and 2, glutamate-oxoglutarate transaminase 1 and 2, and inter mitochondrial membrane space, respectively.

    Journal: The Journal of Biological Chemistry

    Article Title: The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis

    doi: 10.1016/j.jbc.2021.100736

    Figure Lengend Snippet: Scheme showing the intersections between energy metabolism and H 2 S oxidation. Reducing equivalents generated in the cytoplasm are moved to the mitochondrion via the malate–aspartate shuttle comprising a neutral α-ketoglutarate–malate and an electrogenic aspartate–glutamate transporter ( pink ). Conversion of malate to oxaloacetate in the mitochondrion regenerates NADH, which enters the electron transport chain ( purple ) at the level of complex I (CI). The purple arrows denote proton translocation. The sulfide oxidation pathway ( blue ) converts H 2 S to thiosulfate and sulfate with electrons from the oxidation catalyzed by SQOR entering at the level of complex III (CIII) and from sulfite oxidase (SO) at the level of complex IV (CIV). At higher concentrations, H 2 S inhibits CIV. α-KG, MDH1/2, GOT1/2, and IMS denote α-ketoglutarate, malate dehydrogenase 1 and 2, glutamate-oxoglutarate transaminase 1 and 2, and inter mitochondrial membrane space, respectively.

    Article Snippet: Primary rabbit antibodies against GOT1 (Proteintech, 14886-1-AP) and GOT 2 (Proteintech, 14800-1-AP) were used at a dilution of 1:2000.

    Techniques: Generated, Translocation Assay, Membrane

    Evaluation of signaling mechanisms for sulfide-stimulated aerobic glycolysis. A and B , expression level of GOT1 ( A ) and GOT2 ( B ) in GOT1 and GOT2 KD HT29 cells 96 h after treatment with 1 μg/ml doxycycline. Two shRNA sequences (#1 and 2) were used for targeting GOT1 and GOT2. Western blot analysis using anti-GOT1 antibodies ( left ) and Ponceau S staining of the same membrane showing equal loading ( right ). C and D , activation of glucose consumption ( C ) and lactate production ( D ) by the indicated concentrations of Na 2 S in HT29 scr or GOT1 or GOT2 knockdown cells. The concentration of glucose consumed and lactate produced in 20 min ± Na 2 S treatment. E , representative Western blot analysis of phosphorylated ( upper ) and total (l ower ) pyruvate dehydrogenase in HT29 scr cells after 5 and 15 min ±100 μM Na 2 S. F , Ponceau staining of membranes in ( E ) demonstrating equal protein loading and transfer. G , quantitation of Western blot data for phosphorylated PDH shown in ( E ). The error represents SD on the mean of 4 to 6 experiments, ∗ p < 0.005.

    Journal: The Journal of Biological Chemistry

    Article Title: The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis

    doi: 10.1016/j.jbc.2021.100736

    Figure Lengend Snippet: Evaluation of signaling mechanisms for sulfide-stimulated aerobic glycolysis. A and B , expression level of GOT1 ( A ) and GOT2 ( B ) in GOT1 and GOT2 KD HT29 cells 96 h after treatment with 1 μg/ml doxycycline. Two shRNA sequences (#1 and 2) were used for targeting GOT1 and GOT2. Western blot analysis using anti-GOT1 antibodies ( left ) and Ponceau S staining of the same membrane showing equal loading ( right ). C and D , activation of glucose consumption ( C ) and lactate production ( D ) by the indicated concentrations of Na 2 S in HT29 scr or GOT1 or GOT2 knockdown cells. The concentration of glucose consumed and lactate produced in 20 min ± Na 2 S treatment. E , representative Western blot analysis of phosphorylated ( upper ) and total (l ower ) pyruvate dehydrogenase in HT29 scr cells after 5 and 15 min ±100 μM Na 2 S. F , Ponceau staining of membranes in ( E ) demonstrating equal protein loading and transfer. G , quantitation of Western blot data for phosphorylated PDH shown in ( E ). The error represents SD on the mean of 4 to 6 experiments, ∗ p < 0.005.

    Article Snippet: Primary rabbit antibodies against GOT1 (Proteintech, 14886-1-AP) and GOT 2 (Proteintech, 14800-1-AP) were used at a dilution of 1:2000.

    Techniques: Expressing, shRNA, Western Blot, Staining, Membrane, Activation Assay, Knockdown, Concentration Assay, Produced, Quantitation Assay