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primary antibody against got1 (ABclonal Biotechnology)

Name: primary antibody against got1
Brand: ABclonal Biotechnology
Rating: 90 (1 reviews)

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ABclonal Biotechnology primary antibody against got1

a Schematic of AOAA treatment in BMDMs differentiated from <t>Got1</t> f/f and Got1 ΔLysM mice. b , c Supernatant IL-6, TNFα protein levels of BMDMs derived from Got1 f/f and Got1 ΔLysM mice. BMDMs were pre-treated with 10 mM AOAA and then stimulated with 10 mM AOAA and LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments, Got1 ΔLysM mice, n = 3 biologically independent experiments. d NO production level in BMDMs derived from Got1 f/f and Got1 ΔLysM mice. Seahorse analysis of OCR in M0 macrophages ( e ) and M1 macrophages ( f ), ECAR in M0 macrophages ( g ) and M1 macrophages ( h ). ns, p > 0.05, not significant, ** p < 0.01, *** p < 0.001, **** p < 0.0001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Primary Antibody Against Got1, supplied by ABclonal 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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primary antibody against got1 - by Bioz Stars, 2026-03

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1) Product Images from "Glutamate oxaloacetate transaminase 1 is dispensable in macrophage differentiation and anti-pathogen response"

Article Title: Glutamate oxaloacetate transaminase 1 is dispensable in macrophage differentiation and anti-pathogen response

Journal: Communications Biology

doi: 10.1038/s42003-024-06479-w

a Schematic of AOAA treatment in BMDMs differentiated from Got1 f/f and Got1 ΔLysM mice. b , c Supernatant IL-6, TNFα protein levels of BMDMs derived from Got1 f/f and Got1 ΔLysM mice. BMDMs were pre-treated with 10 mM AOAA and then stimulated with 10 mM AOAA and LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments, Got1 ΔLysM mice, n = 3 biologically independent experiments. d NO production level in BMDMs derived from Got1 f/f and Got1 ΔLysM mice. Seahorse analysis of OCR in M0 macrophages ( e ) and M1 macrophages ( f ), ECAR in M0 macrophages ( g ) and M1 macrophages ( h ). ns, p > 0.05, not significant, ** p < 0.01, *** p < 0.001, **** p < 0.0001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Figure Legend Snippet: a Schematic of AOAA treatment in BMDMs differentiated from Got1 f/f and Got1 ΔLysM mice. b , c Supernatant IL-6, TNFα protein levels of BMDMs derived from Got1 f/f and Got1 ΔLysM mice. BMDMs were pre-treated with 10 mM AOAA and then stimulated with 10 mM AOAA and LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments, Got1 ΔLysM mice, n = 3 biologically independent experiments. d NO production level in BMDMs derived from Got1 f/f and Got1 ΔLysM mice. Seahorse analysis of OCR in M0 macrophages ( e ) and M1 macrophages ( f ), ECAR in M0 macrophages ( g ) and M1 macrophages ( h ). ns, p > 0.05, not significant, ** p < 0.01, *** p < 0.001, **** p < 0.0001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Techniques Used: Derivative Assay, Two Tailed Test

a Schematic of pro-inflammatory macrophages differentiation. b – d Il6 , Tnfa and Il1b mRNA levels in BMDMs stimulated with LPS (100 ng/mL) for 4 h or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. e , f IL-6, TNFα protein levels in the supernatant determined by ELISA. g NO production level in BMDMs stimulated with LPS (100 ng/mL) or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. h Lactate production levels in BMDMs stimulated with LPS (100 ng/mL) or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. ns, p > 0.05, not significant, unpaired, two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Figure Legend Snippet: a Schematic of pro-inflammatory macrophages differentiation. b – d Il6 , Tnfa and Il1b mRNA levels in BMDMs stimulated with LPS (100 ng/mL) for 4 h or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. e , f IL-6, TNFα protein levels in the supernatant determined by ELISA. g NO production level in BMDMs stimulated with LPS (100 ng/mL) or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. h Lactate production levels in BMDMs stimulated with LPS (100 ng/mL) or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. ns, p > 0.05, not significant, unpaired, two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Techniques Used: Enzyme-linked Immunosorbent Assay, Two Tailed Test

a Model of GOT1 in malate-aspartate shuttle. b Schematic of Aspartate treatment in wildtype BMDMs stimulated with LPS (100 ng/mL) or LPS (20 ng/mL) + IFNγ (100 ng/mL). c Il1b mRNA levels in BMDMs stimulated with LPS (100 ng/mL) for 4 h or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. n = 3 biologically independent experiments. d – f Il6 , Tnfa and Il1b mRNA levels in BMDMs stimulated with LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 stop/+ mice, n = 3 biologically independent experiments; Got1 stop/+ ; Lyz2-Cre mice, n = 3 biologically independent experiments. g – i Il6 , Tnfa and Il1b mRNA levels in BMDMs stimulated with LPS (100 ng/mL) or HKCA (HKCA: BMDM = 1:1) for 4 h. Got1 stop/+ mice, n = 3 biologically independent experiments; Got1 stop/+ ; Lyz2-Cre mice, n = 3 biologically independent experiments. j , k IL-6, TNFα protein levels in the supernatant determined by ELISA. BMDMs were stimulated with 100 ng/mL LPS, LPS (20 ng/mL) + IFNγ (100 ng/mL) or HKCA (HKCA: BMDM = 1:1) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, unpaired, two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Figure Legend Snippet: a Model of GOT1 in malate-aspartate shuttle. b Schematic of Aspartate treatment in wildtype BMDMs stimulated with LPS (100 ng/mL) or LPS (20 ng/mL) + IFNγ (100 ng/mL). c Il1b mRNA levels in BMDMs stimulated with LPS (100 ng/mL) for 4 h or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. n = 3 biologically independent experiments. d – f Il6 , Tnfa and Il1b mRNA levels in BMDMs stimulated with LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 stop/+ mice, n = 3 biologically independent experiments; Got1 stop/+ ; Lyz2-Cre mice, n = 3 biologically independent experiments. g – i Il6 , Tnfa and Il1b mRNA levels in BMDMs stimulated with LPS (100 ng/mL) or HKCA (HKCA: BMDM = 1:1) for 4 h. Got1 stop/+ mice, n = 3 biologically independent experiments; Got1 stop/+ ; Lyz2-Cre mice, n = 3 biologically independent experiments. j , k IL-6, TNFα protein levels in the supernatant determined by ELISA. BMDMs were stimulated with 100 ng/mL LPS, LPS (20 ng/mL) + IFNγ (100 ng/mL) or HKCA (HKCA: BMDM = 1:1) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, unpaired, two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Techniques Used: Enzyme-linked Immunosorbent Assay, Two Tailed Test

a Schematic of ROS detection in macrophages. b ROS production in BMDMs. Prior to ROS detection, BMDMs were pre-treated with AOAA for 24 h, then treated with HKCA (HKCA: BMDM = 1:1) for 1 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. c Phagocytosis of BMDMs. FITC labeled-HKCA was utilized for phagocytosis assay with BMDMs. d CFU Count of S. aureus and E. coli in BMDMs-In-Vitro-Killing Assay. e Schematic of infection design. f , g Percentage of mice survival. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, unpaired, p values were determined by two-tailed Student’s t test in b – d and log-rank test was used for survival comparison in f and g . Data are representative of three independent experiments (mean ± SD).

Figure Legend Snippet: a Schematic of ROS detection in macrophages. b ROS production in BMDMs. Prior to ROS detection, BMDMs were pre-treated with AOAA for 24 h, then treated with HKCA (HKCA: BMDM = 1:1) for 1 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. c Phagocytosis of BMDMs. FITC labeled-HKCA was utilized for phagocytosis assay with BMDMs. d CFU Count of S. aureus and E. coli in BMDMs-In-Vitro-Killing Assay. e Schematic of infection design. f , g Percentage of mice survival. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, unpaired, p values were determined by two-tailed Student’s t test in b – d and log-rank test was used for survival comparison in f and g . Data are representative of three independent experiments (mean ± SD).

Techniques Used: Labeling, Phagocytosis Assay, In Vitro, Infection, Two Tailed Test, Comparison

a Schematic of the differentiation of M2 macrophages. b – d Chil3 , Arg1 , and Retnla mRNA levels in BMDMs, derived from Got1 f/f and Got1 ΔLysM mice, pretreated with 10 mM AOAA for 24 h, then treated with IL-4 (20 ng/mL) for 24 h. n = 3 biologically independent experiments. e – g Chil3 , Arg1 , and Retnla mRNA levels in PMs, derived from Got1 f/f and Got1 ΔLysM mice, pretreated with 10 mM AOAA for 24 h, then treated with IL-4 (20 ng/mL) for 24 h. n = 3 biologically independent experiments. h – j Chil3 , Arg1 , and Retnla mRNA levels in BMDMs, derived from Got1 stop/+ and Got1 stop/+ ; Lyz2-Cre mice, treated with IL-4 (20 ng/mL) for 24 h. n = 3 biologically independent experiments. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, *** p < 0.001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Figure Legend Snippet: a Schematic of the differentiation of M2 macrophages. b – d Chil3 , Arg1 , and Retnla mRNA levels in BMDMs, derived from Got1 f/f and Got1 ΔLysM mice, pretreated with 10 mM AOAA for 24 h, then treated with IL-4 (20 ng/mL) for 24 h. n = 3 biologically independent experiments. e – g Chil3 , Arg1 , and Retnla mRNA levels in PMs, derived from Got1 f/f and Got1 ΔLysM mice, pretreated with 10 mM AOAA for 24 h, then treated with IL-4 (20 ng/mL) for 24 h. n = 3 biologically independent experiments. h – j Chil3 , Arg1 , and Retnla mRNA levels in BMDMs, derived from Got1 stop/+ and Got1 stop/+ ; Lyz2-Cre mice, treated with IL-4 (20 ng/mL) for 24 h. n = 3 biologically independent experiments. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, *** p < 0.001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Techniques Used: Derivative Assay, Two Tailed Test

a Schematic of immune tolerance induced with LPS. b , c IL-6, TNFα protein levels in the supernatant of Got1 f/f and Got1 ΔLysM mice derived BMDMs were determined by ELISA. Before LPS retreatment, BMDMs were pretreated with 10 mM AOAA for 24 h, n = 3 biologically independent experiments. d Lactate production level in BMDMs stimulated with LPS (100 ng/mL) retreatment for 24 h. e NO production level in BMDMs stimulated with LPS (100 ng/mL) retreatment for 24 h. f , g IL-6, TNFα protein levels in the supernatant of Got1 stop/+ and Got1 stop/+ ; Lyz2-Cre mice derived BMDMs were determined by ELISA in. n = 3 biologically independent experiments. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, *** p < 0.001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Figure Legend Snippet: a Schematic of immune tolerance induced with LPS. b , c IL-6, TNFα protein levels in the supernatant of Got1 f/f and Got1 ΔLysM mice derived BMDMs were determined by ELISA. Before LPS retreatment, BMDMs were pretreated with 10 mM AOAA for 24 h, n = 3 biologically independent experiments. d Lactate production level in BMDMs stimulated with LPS (100 ng/mL) retreatment for 24 h. e NO production level in BMDMs stimulated with LPS (100 ng/mL) retreatment for 24 h. f , g IL-6, TNFα protein levels in the supernatant of Got1 stop/+ and Got1 stop/+ ; Lyz2-Cre mice derived BMDMs were determined by ELISA in. n = 3 biologically independent experiments. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, *** p < 0.001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Techniques Used: Derivative Assay, Enzyme-linked Immunosorbent Assay, Two Tailed Test

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Journal: Communications Biology

Article Title: Glutamate oxaloacetate transaminase 1 is dispensable in macrophage differentiation and anti-pathogen response

doi: 10.1038/s42003-024-06479-w

Figure Lengend Snippet: a Schematic of AOAA treatment in BMDMs differentiated from Got1 f/f and Got1 ΔLysM mice. b , c Supernatant IL-6, TNFα protein levels of BMDMs derived from Got1 f/f and Got1 ΔLysM mice. BMDMs were pre-treated with 10 mM AOAA and then stimulated with 10 mM AOAA and LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments, Got1 ΔLysM mice, n = 3 biologically independent experiments. d NO production level in BMDMs derived from Got1 f/f and Got1 ΔLysM mice. Seahorse analysis of OCR in M0 macrophages ( e ) and M1 macrophages ( f ), ECAR in M0 macrophages ( g ) and M1 macrophages ( h ). ns, p > 0.05, not significant, ** p < 0.01, *** p < 0.001, **** p < 0.0001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Article Snippet: Following blocking, the PVDF membrane was incubated overnight at 4°C with the primary antibody against GOT1 (1:1000 dilution, Abclonal A11363), GOT2 (1:1000 dilution, Abclonal A19245) and β-Actin (1:1000 dilution, Abcam ab8226).

Techniques: Derivative Assay, Two Tailed Test

Journal: Communications Biology

Article Title: Glutamate oxaloacetate transaminase 1 is dispensable in macrophage differentiation and anti-pathogen response

doi: 10.1038/s42003-024-06479-w

Figure Lengend Snippet: a Schematic of pro-inflammatory macrophages differentiation. b – d Il6 , Tnfa and Il1b mRNA levels in BMDMs stimulated with LPS (100 ng/mL) for 4 h or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. e , f IL-6, TNFα protein levels in the supernatant determined by ELISA. g NO production level in BMDMs stimulated with LPS (100 ng/mL) or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. h Lactate production levels in BMDMs stimulated with LPS (100 ng/mL) or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. ns, p > 0.05, not significant, unpaired, two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Techniques: Enzyme-linked Immunosorbent Assay, Two Tailed Test

Journal: Communications Biology

Article Title: Glutamate oxaloacetate transaminase 1 is dispensable in macrophage differentiation and anti-pathogen response

doi: 10.1038/s42003-024-06479-w

Figure Lengend Snippet: a Model of GOT1 in malate-aspartate shuttle. b Schematic of Aspartate treatment in wildtype BMDMs stimulated with LPS (100 ng/mL) or LPS (20 ng/mL) + IFNγ (100 ng/mL). c Il1b mRNA levels in BMDMs stimulated with LPS (100 ng/mL) for 4 h or LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. n = 3 biologically independent experiments. d – f Il6 , Tnfa and Il1b mRNA levels in BMDMs stimulated with LPS (20 ng/mL) + IFNγ (100 ng/mL) for 24 h. Got1 stop/+ mice, n = 3 biologically independent experiments; Got1 stop/+ ; Lyz2-Cre mice, n = 3 biologically independent experiments. g – i Il6 , Tnfa and Il1b mRNA levels in BMDMs stimulated with LPS (100 ng/mL) or HKCA (HKCA: BMDM = 1:1) for 4 h. Got1 stop/+ mice, n = 3 biologically independent experiments; Got1 stop/+ ; Lyz2-Cre mice, n = 3 biologically independent experiments. j , k IL-6, TNFα protein levels in the supernatant determined by ELISA. BMDMs were stimulated with 100 ng/mL LPS, LPS (20 ng/mL) + IFNγ (100 ng/mL) or HKCA (HKCA: BMDM = 1:1) for 24 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, unpaired, two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Techniques: Enzyme-linked Immunosorbent Assay, Two Tailed Test

Journal: Communications Biology

Article Title: Glutamate oxaloacetate transaminase 1 is dispensable in macrophage differentiation and anti-pathogen response

doi: 10.1038/s42003-024-06479-w

Figure Lengend Snippet: a Schematic of ROS detection in macrophages. b ROS production in BMDMs. Prior to ROS detection, BMDMs were pre-treated with AOAA for 24 h, then treated with HKCA (HKCA: BMDM = 1:1) for 1 h. Got1 f/f mice, n = 3 biologically independent experiments; Got1 ΔLysM mice, n = 3 biologically independent experiments. c Phagocytosis of BMDMs. FITC labeled-HKCA was utilized for phagocytosis assay with BMDMs. d CFU Count of S. aureus and E. coli in BMDMs-In-Vitro-Killing Assay. e Schematic of infection design. f , g Percentage of mice survival. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, unpaired, p values were determined by two-tailed Student’s t test in b – d and log-rank test was used for survival comparison in f and g . Data are representative of three independent experiments (mean ± SD).

Techniques: Labeling, Phagocytosis Assay, In Vitro, Infection, Two Tailed Test, Comparison

Journal: Communications Biology

Article Title: Glutamate oxaloacetate transaminase 1 is dispensable in macrophage differentiation and anti-pathogen response

doi: 10.1038/s42003-024-06479-w

Figure Lengend Snippet: a Schematic of the differentiation of M2 macrophages. b – d Chil3 , Arg1 , and Retnla mRNA levels in BMDMs, derived from Got1 f/f and Got1 ΔLysM mice, pretreated with 10 mM AOAA for 24 h, then treated with IL-4 (20 ng/mL) for 24 h. n = 3 biologically independent experiments. e – g Chil3 , Arg1 , and Retnla mRNA levels in PMs, derived from Got1 f/f and Got1 ΔLysM mice, pretreated with 10 mM AOAA for 24 h, then treated with IL-4 (20 ng/mL) for 24 h. n = 3 biologically independent experiments. h – j Chil3 , Arg1 , and Retnla mRNA levels in BMDMs, derived from Got1 stop/+ and Got1 stop/+ ; Lyz2-Cre mice, treated with IL-4 (20 ng/mL) for 24 h. n = 3 biologically independent experiments. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, *** p < 0.001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Techniques: Derivative Assay, Two Tailed Test

Journal: Communications Biology

Article Title: Glutamate oxaloacetate transaminase 1 is dispensable in macrophage differentiation and anti-pathogen response

doi: 10.1038/s42003-024-06479-w

Figure Lengend Snippet: a Schematic of immune tolerance induced with LPS. b , c IL-6, TNFα protein levels in the supernatant of Got1 f/f and Got1 ΔLysM mice derived BMDMs were determined by ELISA. Before LPS retreatment, BMDMs were pretreated with 10 mM AOAA for 24 h, n = 3 biologically independent experiments. d Lactate production level in BMDMs stimulated with LPS (100 ng/mL) retreatment for 24 h. e NO production level in BMDMs stimulated with LPS (100 ng/mL) retreatment for 24 h. f , g IL-6, TNFα protein levels in the supernatant of Got1 stop/+ and Got1 stop/+ ; Lyz2-Cre mice derived BMDMs were determined by ELISA in. n = 3 biologically independent experiments. ns, p > 0.05, not significant, * p < 0.05, ** p < 0.01, *** p < 0.001, unpaired, p values were determined by two-tailed Student’s t test. Data are representative of three independent experiments (mean ± SD).

Techniques: Derivative Assay, Enzyme-linked Immunosorbent Assay, Two Tailed Test

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

Continuous low-dose cisplatin pressure changed the expression patterns of hsa_circRNA_103809, miR-377-3p and GOT1 in NSCLC cells. The parental CS-NSCLC cells (A549, H1299 and Calu-3) were subjected to continuous low-dose cisplatin treatment to generate CR-NSCLC cells (A549/DDP, H1299/DDP and Calu-3/DDP). a-c Cell proliferation abilities in CS-NSCLC and CR-NSCLC cells were determined by using the CCK-8 assay (Note: “Control: without cisplatin stimulation”). d-f Trypan blue staining assay was conducted to evaluate NSCLC cell viability. g Cell apoptosis ratio was measured by using the Annexin V-FITC/PI double staining method. Real-Time qPCR was used to examine the expression levels of ( h ) hsa_circRNA_103809, i miR-377-3p and j GOT1 mRNA in NSCLC cells. k Western Blot analysis was employed to determine the protein levels of GOT1 in NSCLC cells, full-length blots/gels are presented in Supplementary Figure S . Each experiment was repeated at least 3 times. * P < 0.05

Journal: BMC Cancer

Article Title: A novel circular RNA hsa_circRNA_103809/miR-377-3p/GOT1 pathway regulates cisplatin-resistance in non-small cell lung cancer (NSCLC)

doi: 10.1186/s12885-020-07680-w

Figure Lengend Snippet: Continuous low-dose cisplatin pressure changed the expression patterns of hsa_circRNA_103809, miR-377-3p and GOT1 in NSCLC cells. The parental CS-NSCLC cells (A549, H1299 and Calu-3) were subjected to continuous low-dose cisplatin treatment to generate CR-NSCLC cells (A549/DDP, H1299/DDP and Calu-3/DDP). a-c Cell proliferation abilities in CS-NSCLC and CR-NSCLC cells were determined by using the CCK-8 assay (Note: “Control: without cisplatin stimulation”). d-f Trypan blue staining assay was conducted to evaluate NSCLC cell viability. g Cell apoptosis ratio was measured by using the Annexin V-FITC/PI double staining method. Real-Time qPCR was used to examine the expression levels of ( h ) hsa_circRNA_103809, i miR-377-3p and j GOT1 mRNA in NSCLC cells. k Western Blot analysis was employed to determine the protein levels of GOT1 in NSCLC cells, full-length blots/gels are presented in Supplementary Figure S . Each experiment was repeated at least 3 times. * P < 0.05

Article Snippet: Next, the membranes were incubated with 5% skim milk for 70 min at room temperature for blocking, and the membranes were probed with the primary antibodies against GOT1 (1:1500, MW: 50 kDa, #PA5–24634, Thermo, USA), β-actin (1:2000, MW: 42 kDa, #ab6276, Abcam, UK), cyclin D1 (1:1500, MW: 35 kDa, #ab40754, Abcam, UK), CDK2 (1:2000, MW: 33 kDa, #ab32147, Abcam, UK), cleaved caspase-3 (1:1500, MW: 17 kDa, #ab32042, Abcam, UK) and Bax (1:1500, MW: 21 kDa, #ab32503, Abcam, UK) overnight at 4 °C.

Techniques: Expressing, CCK-8 Assay, Control, Staining, Double Staining, Western Blot

The regulatory link between hsa_circRNA_103809, miR-377-3p and GOT1. The online miRDB software ( http://mirdb.org/ ) indicated that miR-377-3p potentially bound to ( a ) hsa_circRNA_103809 and (F) 3′ untranslated region (3’UTR) of GOT1 mRNA. Dual-luciferase reporter gene system assay was performed to validate the binding sites of miR-377-3p with ( b-d ) hsa_circRNA_103809 and (G-I) 3′ UTR region of GOT1 mRNA in NSCLC cells. RNA pull-down assay suggested that miR-377-3p tended to be enriched by the biotin-labelled probes for ( e ) hsa_circRNA_103809 and ( j ) GOT1 mRNA. ( k, l ) GOT1 was positively regulated by hsa_circRNA_103809 in NSCLC cells, full-length blots/gels are presented in Supplementary Figure S A. ( m, n ) MiR-377-3p inhibited GOT1 expressions in NSCLC cells, full-length blots/gels are presented in Supplementary Figure S B. ( o, p ) Hsa_circRNA_103809 sponged miR-377-3p to upregulate GOT1 in NSCLC cells, full-length blots/gels are presented in Supplementary Figure S C. (Note: “Control: without vectors transfection”). Each experiment was repeated at least 3 times. * P < 0.05

Journal: BMC Cancer

Article Title: A novel circular RNA hsa_circRNA_103809/miR-377-3p/GOT1 pathway regulates cisplatin-resistance in non-small cell lung cancer (NSCLC)

doi: 10.1186/s12885-020-07680-w

Figure Lengend Snippet: The regulatory link between hsa_circRNA_103809, miR-377-3p and GOT1. The online miRDB software ( http://mirdb.org/ ) indicated that miR-377-3p potentially bound to ( a ) hsa_circRNA_103809 and (F) 3′ untranslated region (3’UTR) of GOT1 mRNA. Dual-luciferase reporter gene system assay was performed to validate the binding sites of miR-377-3p with ( b-d ) hsa_circRNA_103809 and (G-I) 3′ UTR region of GOT1 mRNA in NSCLC cells. RNA pull-down assay suggested that miR-377-3p tended to be enriched by the biotin-labelled probes for ( e ) hsa_circRNA_103809 and ( j ) GOT1 mRNA. ( k, l ) GOT1 was positively regulated by hsa_circRNA_103809 in NSCLC cells, full-length blots/gels are presented in Supplementary Figure S A. ( m, n ) MiR-377-3p inhibited GOT1 expressions in NSCLC cells, full-length blots/gels are presented in Supplementary Figure S B. ( o, p ) Hsa_circRNA_103809 sponged miR-377-3p to upregulate GOT1 in NSCLC cells, full-length blots/gels are presented in Supplementary Figure S C. (Note: “Control: without vectors transfection”). Each experiment was repeated at least 3 times. * P < 0.05

Techniques: Software, Luciferase, Binding Assay, Pull Down Assay, Control, Transfection

Knock-down of hsa_circRNA_103809 increased cisplatin-sensitivity in CR-NSCLC cells by targeting miR-377-3p and GOT1. a-c CCK-8 assay was performed to determine cell proliferation abilities. d-f Trypan blue staining assay was used to examine cell viability. g Annexin V-FITC/PI double staining assay was performed to measure cell apoptosis ratio in CR-NSCLC cells. (Note: “Control: without vectors transfection and cisplatin treatment”). Each experiment was repeated at least 3 times. * P < 0.05

Journal: BMC Cancer

Article Title: A novel circular RNA hsa_circRNA_103809/miR-377-3p/GOT1 pathway regulates cisplatin-resistance in non-small cell lung cancer (NSCLC)

doi: 10.1186/s12885-020-07680-w

Figure Lengend Snippet: Knock-down of hsa_circRNA_103809 increased cisplatin-sensitivity in CR-NSCLC cells by targeting miR-377-3p and GOT1. a-c CCK-8 assay was performed to determine cell proliferation abilities. d-f Trypan blue staining assay was used to examine cell viability. g Annexin V-FITC/PI double staining assay was performed to measure cell apoptosis ratio in CR-NSCLC cells. (Note: “Control: without vectors transfection and cisplatin treatment”). Each experiment was repeated at least 3 times. * P < 0.05

Techniques: Knockdown, CCK-8 Assay, Staining, Double Staining, Control, Transfection

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