gdh  (Cell Signaling Technology Inc)


Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc gdh
    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative <t>phosphorylation</t> <t>(OXPHOS)</t> activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of <t>GDH,</t> Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.
    Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gdh/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gdh - by Bioz Stars, 2023-10
    94/100 stars

    Images

    1) Product Images from "Exosome‐shuttled mitochondrial transcription factor A mRNA promotes the osteogenesis of dental pulp stem cells through mitochondrial oxidative phosphorylation activation"

    Article Title: Exosome‐shuttled mitochondrial transcription factor A mRNA promotes the osteogenesis of dental pulp stem cells through mitochondrial oxidative phosphorylation activation

    Journal: Cell Proliferation

    doi: 10.1111/cpr.13324

    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.
    Figure Legend Snippet: Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.

    Techniques Used: Expressing, Activity Assay, Western Blot, ECAR Assay

    gdh  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc gdh
    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative <t>phosphorylation</t> <t>(OXPHOS)</t> activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of <t>GDH,</t> Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.
    Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gdh/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gdh - by Bioz Stars, 2023-10
    94/100 stars

    Images

    1) Product Images from "Exosome‐shuttled mitochondrial transcription factor A mRNA promotes the osteogenesis of dental pulp stem cells through mitochondrial oxidative phosphorylation activation"

    Article Title: Exosome‐shuttled mitochondrial transcription factor A mRNA promotes the osteogenesis of dental pulp stem cells through mitochondrial oxidative phosphorylation activation

    Journal: Cell Proliferation

    doi: 10.1111/cpr.13324

    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.
    Figure Legend Snippet: Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.

    Techniques Used: Expressing, Activity Assay, Western Blot, ECAR Assay

    gdh 1 2 12793s  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Cell Signaling Technology Inc gdh 1 2 12793s
    Gdh 1 2 12793s, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gdh 1 2 12793s/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gdh 1 2 12793s - by Bioz Stars, 2023-10
    86/100 stars

    Images

    gdh 1 2 12793s  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Cell Signaling Technology Inc gdh 1 2 12793s
    Gdh 1 2 12793s, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gdh 1 2 12793s/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gdh 1 2 12793s - by Bioz Stars, 2023-10
    86/100 stars

    Images

    gdh  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Cell Signaling Technology Inc gdh
    Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gdh/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gdh - by Bioz Stars, 2023-10
    86/100 stars

    Images

    anti gdh  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Cell Signaling Technology Inc anti gdh
    ISKNV infection regulated expression of GLS1, <t>GDH,</t> and IDH2 <t>via</t> <t>mTOR.</t> (A) NAD+/NADH ratio in ISKNV-infected and non-infected cells. (B) mRNA expression of GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h detected by real-time PCR. (C) Protein expression of mTOR, p-mTOR, GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h determined by Western blotting. (D) The copy number of ISKNV genome in infected cells treated with LY294002, rapamycin, or MHY1485 for 36 h by determination of real-time PCR. (E) ISKNV titers in supernatant of infected cells treated with LY294002, rapamycin, or MHY1485 for 72 h by TCID 50 analysis.
    Anti Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gdh/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti gdh - by Bioz Stars, 2023-10
    86/100 stars

    Images

    1) Product Images from "The mTOR/PGC-1α/SIRT3 Pathway Drives Reductive Glutamine Metabolism to Reduce Oxidative Stress Caused by ISKNV in CPB Cells"

    Article Title: The mTOR/PGC-1α/SIRT3 Pathway Drives Reductive Glutamine Metabolism to Reduce Oxidative Stress Caused by ISKNV in CPB Cells

    Journal: Microbiology Spectrum

    doi: 10.1128/spectrum.02310-21

    ISKNV infection regulated expression of GLS1, GDH, and IDH2 via mTOR. (A) NAD+/NADH ratio in ISKNV-infected and non-infected cells. (B) mRNA expression of GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h detected by real-time PCR. (C) Protein expression of mTOR, p-mTOR, GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h determined by Western blotting. (D) The copy number of ISKNV genome in infected cells treated with LY294002, rapamycin, or MHY1485 for 36 h by determination of real-time PCR. (E) ISKNV titers in supernatant of infected cells treated with LY294002, rapamycin, or MHY1485 for 72 h by TCID 50 analysis.
    Figure Legend Snippet: ISKNV infection regulated expression of GLS1, GDH, and IDH2 via mTOR. (A) NAD+/NADH ratio in ISKNV-infected and non-infected cells. (B) mRNA expression of GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h detected by real-time PCR. (C) Protein expression of mTOR, p-mTOR, GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h determined by Western blotting. (D) The copy number of ISKNV genome in infected cells treated with LY294002, rapamycin, or MHY1485 for 36 h by determination of real-time PCR. (E) ISKNV titers in supernatant of infected cells treated with LY294002, rapamycin, or MHY1485 for 72 h by TCID 50 analysis.

    Techniques Used: Infection, Expressing, Real-time Polymerase Chain Reaction, Western Blot

    ISKNV infection enhanced reductive glutamine metabolism via the mTOR/SIRT3 pathway. (A–B) CPB cells were transfected with empty vector (V) or plasmid pCMV-SIRT3 (pS3) to construct a stable SIRT3-overexpressed cell line. CPB cells were transfected with nontargeting siRNAs (NC) or siRNAs target SIRT3 gene (siS3) to knock down the expression of SIRT3. mRNA and protein expression of SIRT3 in V cells, pS3 cells, NC cells, or siS3 cells determined by real-time PCR and Western blotting. (C) mRNA expression of SIRT3, GLS1, GDH, and IDH2 in transfected cells infected or noninfected with ISKNV. (D) Protein expression of SIRT3, GLS1, GDH, and IDH2 in pS3 or siS3 cells infected or noninfected with ISKNV detected by Western blotting. (E) IDH2 activity at 72 hpi in pS3 or siS3 cells infected with ISKNV. (F) α-KGDH at 72 hpi in pS3 or siS3 cells infected with ISKNV. (G) The copy number of ISKNV genome in pS3 or siS3 cells at 36 hpi by determination of real-time PCR. (H) ISKNV titers in supernatant of pS3 or siS3 cells at 72 hpi by TCID 50 analysis.
    Figure Legend Snippet: ISKNV infection enhanced reductive glutamine metabolism via the mTOR/SIRT3 pathway. (A–B) CPB cells were transfected with empty vector (V) or plasmid pCMV-SIRT3 (pS3) to construct a stable SIRT3-overexpressed cell line. CPB cells were transfected with nontargeting siRNAs (NC) or siRNAs target SIRT3 gene (siS3) to knock down the expression of SIRT3. mRNA and protein expression of SIRT3 in V cells, pS3 cells, NC cells, or siS3 cells determined by real-time PCR and Western blotting. (C) mRNA expression of SIRT3, GLS1, GDH, and IDH2 in transfected cells infected or noninfected with ISKNV. (D) Protein expression of SIRT3, GLS1, GDH, and IDH2 in pS3 or siS3 cells infected or noninfected with ISKNV detected by Western blotting. (E) IDH2 activity at 72 hpi in pS3 or siS3 cells infected with ISKNV. (F) α-KGDH at 72 hpi in pS3 or siS3 cells infected with ISKNV. (G) The copy number of ISKNV genome in pS3 or siS3 cells at 36 hpi by determination of real-time PCR. (H) ISKNV titers in supernatant of pS3 or siS3 cells at 72 hpi by TCID 50 analysis.

    Techniques Used: Infection, Transfection, Plasmid Preparation, Construct, Expressing, Real-time Polymerase Chain Reaction, Western Blot, Activity Assay

    PGC-1α regulated expression of SIRT3 and metabolic genes, and benefited the production of ISKNV. (A) CPB cells were transfected with non-targeting siRNAs (NC) or siRNAs target PGC-1α gene (siP) to knock down the expression of PGC-1α. mRNA and protein expressions of PGC-1α in NC and siP cells were detected by real-time PCR and Western blotting. (B) mRNA and protein expression of PGC-1α, SIRT3, GLS1, GDH, and IDH2 in NC and siP cells infected or noninfected with ISKNV, determined by real-time PCR and Western blotting. (C) mRNA and protein expression of PGC-1α in ISKNV-infected or noninfected CPB cells treated with LY294002, rapamycin, or MHY1485 for 72 h detected by real-time PCR and Western blotting. (D) The copy number of the ISKNV genome in NC or siP cells at 36 hpi by determination of real-time PCR. (E) ISKNV titers in supernatant of NC or siP cells at 72 hpi by TCID 50 analysis.
    Figure Legend Snippet: PGC-1α regulated expression of SIRT3 and metabolic genes, and benefited the production of ISKNV. (A) CPB cells were transfected with non-targeting siRNAs (NC) or siRNAs target PGC-1α gene (siP) to knock down the expression of PGC-1α. mRNA and protein expressions of PGC-1α in NC and siP cells were detected by real-time PCR and Western blotting. (B) mRNA and protein expression of PGC-1α, SIRT3, GLS1, GDH, and IDH2 in NC and siP cells infected or noninfected with ISKNV, determined by real-time PCR and Western blotting. (C) mRNA and protein expression of PGC-1α in ISKNV-infected or noninfected CPB cells treated with LY294002, rapamycin, or MHY1485 for 72 h detected by real-time PCR and Western blotting. (D) The copy number of the ISKNV genome in NC or siP cells at 36 hpi by determination of real-time PCR. (E) ISKNV titers in supernatant of NC or siP cells at 72 hpi by TCID 50 analysis.

    Techniques Used: Expressing, Transfection, Real-time Polymerase Chain Reaction, Western Blot, Infection

    Primers used in this study
    Figure Legend Snippet: Primers used in this study

    Techniques Used: Sequencing, Expressing, Clone Assay

    anti gdh  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Cell Signaling Technology Inc anti gdh
    ATF4 protein level is regulated downstream of the <t>SIRT3–GDH–TCA</t> cycle–autophagy cascade. A, Western blots show the effects of ATF4 expression to autophagy activation induced by SIRT3 shRNA in Karpas 422 cells. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. EV, empty vector. B, Western blots show the ATF4 protein level being rescued by exogenous GDH in SIRT3 knockdown Karpas 422 cells. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. C, Western blots show the ATF4 protein level being rescued by DMKG in SIRT3 knockdown Karpas 422 cells. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. D, Western blots show the ATF4 protein level being rescued by CQ (50 μmol/L) in SIRT3 knockdown Karpas 422 cells. CQ treatment was done in 16 to 18 hours, followed by immunoblot with the indicated antibodies. Densitometry values are shown <t>for</t> <t>ATF4/ACTB</t> and LC3II/LC3I ratios. Hypothetical cascade model is presented to the left. E, Western blots show the changes of ATF4 protein level control or ATG5 knockdown Karpas 422 cells with control or SIRT3 shRNAs. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. F, Summarized bar plot shows the NES ( y -axis) and FDRs (bar colors) of results from GSEA using published proteomic data . NES show the enrichment of ATF4 target genes (human and mouse) or ATF4 target genes from ChIP (mouse embryonic fibroblasts, MEF) in Atg5 knockout MEF cells in normal or starvation (5 hours) treatment condition. The experiments were done with stable isotope labeling by amino acids in cell culture (SILAC) coupled with off-gel fractionations (OG) and strong cation exchange chromatography (SCX) methods. HBSS, Hank's Balanced Salt Solution. G, Western blots show ATF4 protein levels under CHX and CQ treatment in Karpas 422 cells. Protein samples were collected at the indicated time points after treatment to monitor the kinetics of ATF4 degradation. SIRT3 and LC3 were blotted as controls. NT, not treated. H, EIF2A phosphorylation from Karpas 422 cells exposed to two different doses of CQ or DMSO, or to DMKG treatment. Proteins were blotted with the indicated antibodies, and the densitometry showed relative abundance of phospho-EIF2A over total EIF2A.
    Anti Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gdh/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti gdh - by Bioz Stars, 2023-10
    86/100 stars

    Images

    1) Product Images from "Translational Activation of ATF4 through Mitochondrial Anaplerotic Metabolic Pathways Is Required for DLBCL Growth and Survival"

    Article Title: Translational Activation of ATF4 through Mitochondrial Anaplerotic Metabolic Pathways Is Required for DLBCL Growth and Survival

    Journal: Blood Cancer Discovery

    doi: 10.1158/2643-3230.BCD-20-0183

    ATF4 protein level is regulated downstream of the SIRT3–GDH–TCA cycle–autophagy cascade. A, Western blots show the effects of ATF4 expression to autophagy activation induced by SIRT3 shRNA in Karpas 422 cells. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. EV, empty vector. B, Western blots show the ATF4 protein level being rescued by exogenous GDH in SIRT3 knockdown Karpas 422 cells. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. C, Western blots show the ATF4 protein level being rescued by DMKG in SIRT3 knockdown Karpas 422 cells. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. D, Western blots show the ATF4 protein level being rescued by CQ (50 μmol/L) in SIRT3 knockdown Karpas 422 cells. CQ treatment was done in 16 to 18 hours, followed by immunoblot with the indicated antibodies. Densitometry values are shown for ATF4/ACTB and LC3II/LC3I ratios. Hypothetical cascade model is presented to the left. E, Western blots show the changes of ATF4 protein level control or ATG5 knockdown Karpas 422 cells with control or SIRT3 shRNAs. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. F, Summarized bar plot shows the NES ( y -axis) and FDRs (bar colors) of results from GSEA using published proteomic data . NES show the enrichment of ATF4 target genes (human and mouse) or ATF4 target genes from ChIP (mouse embryonic fibroblasts, MEF) in Atg5 knockout MEF cells in normal or starvation (5 hours) treatment condition. The experiments were done with stable isotope labeling by amino acids in cell culture (SILAC) coupled with off-gel fractionations (OG) and strong cation exchange chromatography (SCX) methods. HBSS, Hank's Balanced Salt Solution. G, Western blots show ATF4 protein levels under CHX and CQ treatment in Karpas 422 cells. Protein samples were collected at the indicated time points after treatment to monitor the kinetics of ATF4 degradation. SIRT3 and LC3 were blotted as controls. NT, not treated. H, EIF2A phosphorylation from Karpas 422 cells exposed to two different doses of CQ or DMSO, or to DMKG treatment. Proteins were blotted with the indicated antibodies, and the densitometry showed relative abundance of phospho-EIF2A over total EIF2A.
    Figure Legend Snippet: ATF4 protein level is regulated downstream of the SIRT3–GDH–TCA cycle–autophagy cascade. A, Western blots show the effects of ATF4 expression to autophagy activation induced by SIRT3 shRNA in Karpas 422 cells. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. EV, empty vector. B, Western blots show the ATF4 protein level being rescued by exogenous GDH in SIRT3 knockdown Karpas 422 cells. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. C, Western blots show the ATF4 protein level being rescued by DMKG in SIRT3 knockdown Karpas 422 cells. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. D, Western blots show the ATF4 protein level being rescued by CQ (50 μmol/L) in SIRT3 knockdown Karpas 422 cells. CQ treatment was done in 16 to 18 hours, followed by immunoblot with the indicated antibodies. Densitometry values are shown for ATF4/ACTB and LC3II/LC3I ratios. Hypothetical cascade model is presented to the left. E, Western blots show the changes of ATF4 protein level control or ATG5 knockdown Karpas 422 cells with control or SIRT3 shRNAs. Protein level changes were quantified with densitometry results. Hypothetical cascade model is presented to the left. F, Summarized bar plot shows the NES ( y -axis) and FDRs (bar colors) of results from GSEA using published proteomic data . NES show the enrichment of ATF4 target genes (human and mouse) or ATF4 target genes from ChIP (mouse embryonic fibroblasts, MEF) in Atg5 knockout MEF cells in normal or starvation (5 hours) treatment condition. The experiments were done with stable isotope labeling by amino acids in cell culture (SILAC) coupled with off-gel fractionations (OG) and strong cation exchange chromatography (SCX) methods. HBSS, Hank's Balanced Salt Solution. G, Western blots show ATF4 protein levels under CHX and CQ treatment in Karpas 422 cells. Protein samples were collected at the indicated time points after treatment to monitor the kinetics of ATF4 degradation. SIRT3 and LC3 were blotted as controls. NT, not treated. H, EIF2A phosphorylation from Karpas 422 cells exposed to two different doses of CQ or DMSO, or to DMKG treatment. Proteins were blotted with the indicated antibodies, and the densitometry showed relative abundance of phospho-EIF2A over total EIF2A.

    Techniques Used: Western Blot, Expressing, Activation Assay, shRNA, Plasmid Preparation, Knock-Out, Labeling, Cell Culture, Chromatography

    gdh  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Cell Signaling Technology Inc gdh
    Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gdh/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gdh - by Bioz Stars, 2023-10
    86/100 stars

    Images

    anti gdh  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86

    Structured Review

    Cell Signaling Technology Inc anti gdh
    Mitochondrial level of GLS1 <t>isoforms:</t> <t>GAC</t> ( A ) and KGA ( B ) and glutamate dehydrogenase <t>(GDH)</t> ( C ) in controls and gerbils subjected to 5 min ischemia and 1 and 96 h of reperfusion (IR 1 h, IR 96 h). 20 µg of pure mitochondrial fractions were separated by 10% SDS-PAGE and analyzed by Western blot with anti-GAC, anti-KGA, or anti-GDH and anti-pyruvate carboxylase (PC) to assess the gel loading. The immunoblots are representative of four independent experiments. Densities of GAC, KGA and GDH bands were evaluated, and data are expressed as a percentage of PC (mean ± SD, n = 4). * p < 0.05, ** p < 0.001.
    Anti Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gdh/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti gdh - by Bioz Stars, 2023-10
    86/100 stars

    Images

    1) Product Images from "Mitochondrial Metabolism behind Region-Specific Resistance to Ischemia-Reperfusion Injury in Gerbil Hippocampus. Role of PKCβII and Phosphate-Activated Glutaminase"

    Article Title: Mitochondrial Metabolism behind Region-Specific Resistance to Ischemia-Reperfusion Injury in Gerbil Hippocampus. Role of PKCβII and Phosphate-Activated Glutaminase

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms22168504

    Mitochondrial level of GLS1 isoforms: GAC ( A ) and KGA ( B ) and glutamate dehydrogenase (GDH) ( C ) in controls and gerbils subjected to 5 min ischemia and 1 and 96 h of reperfusion (IR 1 h, IR 96 h). 20 µg of pure mitochondrial fractions were separated by 10% SDS-PAGE and analyzed by Western blot with anti-GAC, anti-KGA, or anti-GDH and anti-pyruvate carboxylase (PC) to assess the gel loading. The immunoblots are representative of four independent experiments. Densities of GAC, KGA and GDH bands were evaluated, and data are expressed as a percentage of PC (mean ± SD, n = 4). * p < 0.05, ** p < 0.001.
    Figure Legend Snippet: Mitochondrial level of GLS1 isoforms: GAC ( A ) and KGA ( B ) and glutamate dehydrogenase (GDH) ( C ) in controls and gerbils subjected to 5 min ischemia and 1 and 96 h of reperfusion (IR 1 h, IR 96 h). 20 µg of pure mitochondrial fractions were separated by 10% SDS-PAGE and analyzed by Western blot with anti-GAC, anti-KGA, or anti-GDH and anti-pyruvate carboxylase (PC) to assess the gel loading. The immunoblots are representative of four independent experiments. Densities of GAC, KGA and GDH bands were evaluated, and data are expressed as a percentage of PC (mean ± SD, n = 4). * p < 0.05, ** p < 0.001.

    Techniques Used: SDS Page, Western Blot

    anti gdh mab  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc anti gdh mab
    Anti Gdh Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gdh mab/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti gdh mab - by Bioz Stars, 2023-10
    94/100 stars

    Images

    anti gdh mab  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Cell Signaling Technology Inc anti gdh mab
    (a) Mitochondrial oxygen consumption of intact cells in regular growth medium measured by high-resolution respirometry and corrected for ROX. ETS, electron transfer system; L, leak respiration; R, routine respiration; E, ETS capacity; ROX, residual oxygen consumption. (a’) Calculation of flux control ratios. (b) Comparison of cytosolic and mitochondrial ATP content using the genetically encoded ATP sensor BTeam. Calculation of BTeam YFP/NLuc emission ratios under basal conditions revealed reduced mitochondrial ATP levels. (c) Immunoblot quantification of proteins involved in glycolysis in Ctrl and KD cells shows an increase in LDHA and <t>GDH</t> levels. HK, Hexokinase; G6PD, glucose-6-phosphate <t>dehydrogenase;</t> <t>GAPDH,</t> Glyceraldehyde 3-phosphate dehydrogenase; PKM1, pyruvate kinase M1; LDHA, lactate dehydrogenase A; PDH, pyruvate dehydrogenase; pPDK1, phospho-pyruvate dehydrogenase kinase; GDH, glutamate dehydrogenase. Actin expression served to normalize the data. (d) Diminished glutamate and glutamine levels determined by a luminescence-based assay. (e) Comparison of cytosolic ATP content using the genetically-encoded ATP sensor BTeam. BTeam YFP/NLuc emission ratios after treatment with 25 μM 2-deoxyglucose (2-DG) reveals increased non-mitochondrial ATP generation capacity in KD cells. (f) Automated high-content confocal microscopy analysis of BODIPY-stained fatty acids demonstrating less lipid droplets in KD cells identified by Höchst staining of nuclei. (g) Schematic illustration of metabolic changes observed in GDAP1 KD cells. Upregulation is shown in blue and bold lines; downregulation in magenta and dashed lines. ME, malic enzyme 1; PDC, pyruvate dehydrogenase complex; PKM1/2, pyruvate kinase M1/2; OAA, oxaloacetate. Data in a and a’ are from 12 independent experiments performed in duplicate. Data in b are from 4 independent experiments performed in triplicates. Data in d are from 4 independent experiments performed in triplicates. Data in e are from 6 independent experiments performed in triplicates. Data in f were from >10000 cells in total and were analyzed in 3 independent experiments, performed in triplicates each. Statistical variation is shown as Tukey’s boxplot, XY graph or scatter plot with the indication of the mean ± SEM. Significance was calculated using the non-parametric Kruskal-Wallis test, *p<0.05.
    Anti Gdh Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gdh mab/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti gdh mab - by Bioz Stars, 2023-10
    94/100 stars

    Images

    1) Product Images from "GDAP1 loss of function inhibits the mitochondrial pyruvate dehydrogenase complex by altering the actin cytoskeleton"

    Article Title: GDAP1 loss of function inhibits the mitochondrial pyruvate dehydrogenase complex by altering the actin cytoskeleton

    Journal: bioRxiv

    doi: 10.1101/2021.03.04.433895

    (a) Mitochondrial oxygen consumption of intact cells in regular growth medium measured by high-resolution respirometry and corrected for ROX. ETS, electron transfer system; L, leak respiration; R, routine respiration; E, ETS capacity; ROX, residual oxygen consumption. (a’) Calculation of flux control ratios. (b) Comparison of cytosolic and mitochondrial ATP content using the genetically encoded ATP sensor BTeam. Calculation of BTeam YFP/NLuc emission ratios under basal conditions revealed reduced mitochondrial ATP levels. (c) Immunoblot quantification of proteins involved in glycolysis in Ctrl and KD cells shows an increase in LDHA and GDH levels. HK, Hexokinase; G6PD, glucose-6-phosphate dehydrogenase; GAPDH, Glyceraldehyde 3-phosphate dehydrogenase; PKM1, pyruvate kinase M1; LDHA, lactate dehydrogenase A; PDH, pyruvate dehydrogenase; pPDK1, phospho-pyruvate dehydrogenase kinase; GDH, glutamate dehydrogenase. Actin expression served to normalize the data. (d) Diminished glutamate and glutamine levels determined by a luminescence-based assay. (e) Comparison of cytosolic ATP content using the genetically-encoded ATP sensor BTeam. BTeam YFP/NLuc emission ratios after treatment with 25 μM 2-deoxyglucose (2-DG) reveals increased non-mitochondrial ATP generation capacity in KD cells. (f) Automated high-content confocal microscopy analysis of BODIPY-stained fatty acids demonstrating less lipid droplets in KD cells identified by Höchst staining of nuclei. (g) Schematic illustration of metabolic changes observed in GDAP1 KD cells. Upregulation is shown in blue and bold lines; downregulation in magenta and dashed lines. ME, malic enzyme 1; PDC, pyruvate dehydrogenase complex; PKM1/2, pyruvate kinase M1/2; OAA, oxaloacetate. Data in a and a’ are from 12 independent experiments performed in duplicate. Data in b are from 4 independent experiments performed in triplicates. Data in d are from 4 independent experiments performed in triplicates. Data in e are from 6 independent experiments performed in triplicates. Data in f were from >10000 cells in total and were analyzed in 3 independent experiments, performed in triplicates each. Statistical variation is shown as Tukey’s boxplot, XY graph or scatter plot with the indication of the mean ± SEM. Significance was calculated using the non-parametric Kruskal-Wallis test, *p<0.05.
    Figure Legend Snippet: (a) Mitochondrial oxygen consumption of intact cells in regular growth medium measured by high-resolution respirometry and corrected for ROX. ETS, electron transfer system; L, leak respiration; R, routine respiration; E, ETS capacity; ROX, residual oxygen consumption. (a’) Calculation of flux control ratios. (b) Comparison of cytosolic and mitochondrial ATP content using the genetically encoded ATP sensor BTeam. Calculation of BTeam YFP/NLuc emission ratios under basal conditions revealed reduced mitochondrial ATP levels. (c) Immunoblot quantification of proteins involved in glycolysis in Ctrl and KD cells shows an increase in LDHA and GDH levels. HK, Hexokinase; G6PD, glucose-6-phosphate dehydrogenase; GAPDH, Glyceraldehyde 3-phosphate dehydrogenase; PKM1, pyruvate kinase M1; LDHA, lactate dehydrogenase A; PDH, pyruvate dehydrogenase; pPDK1, phospho-pyruvate dehydrogenase kinase; GDH, glutamate dehydrogenase. Actin expression served to normalize the data. (d) Diminished glutamate and glutamine levels determined by a luminescence-based assay. (e) Comparison of cytosolic ATP content using the genetically-encoded ATP sensor BTeam. BTeam YFP/NLuc emission ratios after treatment with 25 μM 2-deoxyglucose (2-DG) reveals increased non-mitochondrial ATP generation capacity in KD cells. (f) Automated high-content confocal microscopy analysis of BODIPY-stained fatty acids demonstrating less lipid droplets in KD cells identified by Höchst staining of nuclei. (g) Schematic illustration of metabolic changes observed in GDAP1 KD cells. Upregulation is shown in blue and bold lines; downregulation in magenta and dashed lines. ME, malic enzyme 1; PDC, pyruvate dehydrogenase complex; PKM1/2, pyruvate kinase M1/2; OAA, oxaloacetate. Data in a and a’ are from 12 independent experiments performed in duplicate. Data in b are from 4 independent experiments performed in triplicates. Data in d are from 4 independent experiments performed in triplicates. Data in e are from 6 independent experiments performed in triplicates. Data in f were from >10000 cells in total and were analyzed in 3 independent experiments, performed in triplicates each. Statistical variation is shown as Tukey’s boxplot, XY graph or scatter plot with the indication of the mean ± SEM. Significance was calculated using the non-parametric Kruskal-Wallis test, *p<0.05.

    Techniques Used: Western Blot, Expressing, Luminescence Assay, Confocal Microscopy, Staining

    (a) Immunoblot of whole cell lysates from Ctrl and GDAP1 KD cells against Hexokinase 1 (HK1), HK2, Glucose-6-phosphate dehydrogenase (G6PD), Glyceraldehyde 3-phosphate dehydrogenase (GAPDH), Pyruvate kinase M1/2 (PKM1/2), Pyruvate dehydrogenase (PDH), Lactate Dehydrogenase A (LDHA), Glutamate dehydrogenase (GDH). Sizes are indicated and actin served as loading control. n=3-7
    Figure Legend Snippet: (a) Immunoblot of whole cell lysates from Ctrl and GDAP1 KD cells against Hexokinase 1 (HK1), HK2, Glucose-6-phosphate dehydrogenase (G6PD), Glyceraldehyde 3-phosphate dehydrogenase (GAPDH), Pyruvate kinase M1/2 (PKM1/2), Pyruvate dehydrogenase (PDH), Lactate Dehydrogenase A (LDHA), Glutamate dehydrogenase (GDH). Sizes are indicated and actin served as loading control. n=3-7

    Techniques Used: Western Blot

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    Cell Signaling Technology Inc gdh
    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative <t>phosphorylation</t> <t>(OXPHOS)</t> activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of <t>GDH,</t> Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.
    Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gdh/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gdh - by Bioz Stars, 2023-10
    94/100 stars
      Buy from Supplier

    86
    Cell Signaling Technology Inc gdh 1 2 12793s
    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative <t>phosphorylation</t> <t>(OXPHOS)</t> activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of <t>GDH,</t> Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.
    Gdh 1 2 12793s, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gdh 1 2 12793s/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gdh 1 2 12793s - by Bioz Stars, 2023-10
    86/100 stars
      Buy from Supplier

    86
    Cell Signaling Technology Inc anti gdh
    ISKNV infection regulated expression of GLS1, <t>GDH,</t> and IDH2 <t>via</t> <t>mTOR.</t> (A) NAD+/NADH ratio in ISKNV-infected and non-infected cells. (B) mRNA expression of GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h detected by real-time PCR. (C) Protein expression of mTOR, p-mTOR, GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h determined by Western blotting. (D) The copy number of ISKNV genome in infected cells treated with LY294002, rapamycin, or MHY1485 for 36 h by determination of real-time PCR. (E) ISKNV titers in supernatant of infected cells treated with LY294002, rapamycin, or MHY1485 for 72 h by TCID 50 analysis.
    Anti Gdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gdh/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti gdh - by Bioz Stars, 2023-10
    86/100 stars
      Buy from Supplier

    94
    Cell Signaling Technology Inc anti gdh mab
    ISKNV infection regulated expression of GLS1, <t>GDH,</t> and IDH2 <t>via</t> <t>mTOR.</t> (A) NAD+/NADH ratio in ISKNV-infected and non-infected cells. (B) mRNA expression of GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h detected by real-time PCR. (C) Protein expression of mTOR, p-mTOR, GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h determined by Western blotting. (D) The copy number of ISKNV genome in infected cells treated with LY294002, rapamycin, or MHY1485 for 36 h by determination of real-time PCR. (E) ISKNV titers in supernatant of infected cells treated with LY294002, rapamycin, or MHY1485 for 72 h by TCID 50 analysis.
    Anti Gdh Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti gdh mab/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti gdh mab - by Bioz Stars, 2023-10
    94/100 stars
      Buy from Supplier

    Image Search Results


    Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.

    Journal: Cell Proliferation

    Article Title: Exosome‐shuttled mitochondrial transcription factor A mRNA promotes the osteogenesis of dental pulp stem cells through mitochondrial oxidative phosphorylation activation

    doi: 10.1111/cpr.13324

    Figure Lengend Snippet: Exosomes improve mitochondrial transcription factor A (TFAM) expression and oxidative phosphorylation (OXPHOS) activity in DPSCs. (A) oxygen consumption rate (OCR) from seahorse analysis in DPSCs with supplementation of exosomes. (B) Basal respiration, ATP production, proton leak, maximal respiration and spare capacity in OCR assay. N = 5 independent experiments. (C) The volume of ATP in DPSCs with supplementation of exosomes. N = 4 independent experiments. (D) The protein expression of TFAM and five OXPHOS complexes by western blot analysis. (E) NADH/NAD of DPSCs with exosomes for 24, 48 and 72 h. N = 4 independent experiments. (F) Extracellular acidification rate (ECAR) from seahorse analysis in DPSCs with supplementation of exosomes. (G) Glycolytic reserve, glycolysis and glycolytic capacity in ECAR assay. N = 5 independent experiments. (H) The expression of GDH, Glut1 and CPT1A by western blot analysis. N = 3 independent experiments. * p < 0.05; ** p < 0.01; *** p < 0.001, **** p < 0.0001. Error bars are mean ± SD.

    Article Snippet: Primary antibodies employed in this study included β‐actin (1:1000, CW0096A, CWBIO), ALP (1:500, sc‐79840, Santa Cruz Biotechnology), Runx2 (1:1000, #12556, Cell Signalling), BMP2 (1:1000, ab14933, Abcam), TFAM (1:1000, sc‐376,672, Santa Cruz Biotechnology), total OXPHOS cocktail (1:1000, ab110413, Abcam), Glut1 (1:1000, er1510‐11, Huabio), GDH (1:1000, 12793S, Cell Signalling), and CPT1A (1:1000, 12252S, Cell Signalling).

    Techniques: Expressing, Activity Assay, Western Blot, ECAR Assay

    ISKNV infection regulated expression of GLS1, GDH, and IDH2 via mTOR. (A) NAD+/NADH ratio in ISKNV-infected and non-infected cells. (B) mRNA expression of GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h detected by real-time PCR. (C) Protein expression of mTOR, p-mTOR, GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h determined by Western blotting. (D) The copy number of ISKNV genome in infected cells treated with LY294002, rapamycin, or MHY1485 for 36 h by determination of real-time PCR. (E) ISKNV titers in supernatant of infected cells treated with LY294002, rapamycin, or MHY1485 for 72 h by TCID 50 analysis.

    Journal: Microbiology Spectrum

    Article Title: The mTOR/PGC-1α/SIRT3 Pathway Drives Reductive Glutamine Metabolism to Reduce Oxidative Stress Caused by ISKNV in CPB Cells

    doi: 10.1128/spectrum.02310-21

    Figure Lengend Snippet: ISKNV infection regulated expression of GLS1, GDH, and IDH2 via mTOR. (A) NAD+/NADH ratio in ISKNV-infected and non-infected cells. (B) mRNA expression of GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h detected by real-time PCR. (C) Protein expression of mTOR, p-mTOR, GLS1, GDH, and IDH2 in ISKNV-infected and non-infected cells treated with 10 μM LY294002, 1 μM rapamycin, or 5 μM MHY1485 for 72 h determined by Western blotting. (D) The copy number of ISKNV genome in infected cells treated with LY294002, rapamycin, or MHY1485 for 36 h by determination of real-time PCR. (E) ISKNV titers in supernatant of infected cells treated with LY294002, rapamycin, or MHY1485 for 72 h by TCID 50 analysis.

    Article Snippet: Primary antibodies used in this study included anti-mTOR (7C10), anti-p-mTOR (ser2448) (Cell Signaling Technology, Danvers, MA), anti-SIRT3, anti-GLS1, anti-GDH, anti-IDH2, anti-PGC-1α, anti-α-KGDH (Proteintech, USA), and anti-β-actin (Abcam, USA).

    Techniques: Infection, Expressing, Real-time Polymerase Chain Reaction, Western Blot

    ISKNV infection enhanced reductive glutamine metabolism via the mTOR/SIRT3 pathway. (A–B) CPB cells were transfected with empty vector (V) or plasmid pCMV-SIRT3 (pS3) to construct a stable SIRT3-overexpressed cell line. CPB cells were transfected with nontargeting siRNAs (NC) or siRNAs target SIRT3 gene (siS3) to knock down the expression of SIRT3. mRNA and protein expression of SIRT3 in V cells, pS3 cells, NC cells, or siS3 cells determined by real-time PCR and Western blotting. (C) mRNA expression of SIRT3, GLS1, GDH, and IDH2 in transfected cells infected or noninfected with ISKNV. (D) Protein expression of SIRT3, GLS1, GDH, and IDH2 in pS3 or siS3 cells infected or noninfected with ISKNV detected by Western blotting. (E) IDH2 activity at 72 hpi in pS3 or siS3 cells infected with ISKNV. (F) α-KGDH at 72 hpi in pS3 or siS3 cells infected with ISKNV. (G) The copy number of ISKNV genome in pS3 or siS3 cells at 36 hpi by determination of real-time PCR. (H) ISKNV titers in supernatant of pS3 or siS3 cells at 72 hpi by TCID 50 analysis.

    Journal: Microbiology Spectrum

    Article Title: The mTOR/PGC-1α/SIRT3 Pathway Drives Reductive Glutamine Metabolism to Reduce Oxidative Stress Caused by ISKNV in CPB Cells

    doi: 10.1128/spectrum.02310-21

    Figure Lengend Snippet: ISKNV infection enhanced reductive glutamine metabolism via the mTOR/SIRT3 pathway. (A–B) CPB cells were transfected with empty vector (V) or plasmid pCMV-SIRT3 (pS3) to construct a stable SIRT3-overexpressed cell line. CPB cells were transfected with nontargeting siRNAs (NC) or siRNAs target SIRT3 gene (siS3) to knock down the expression of SIRT3. mRNA and protein expression of SIRT3 in V cells, pS3 cells, NC cells, or siS3 cells determined by real-time PCR and Western blotting. (C) mRNA expression of SIRT3, GLS1, GDH, and IDH2 in transfected cells infected or noninfected with ISKNV. (D) Protein expression of SIRT3, GLS1, GDH, and IDH2 in pS3 or siS3 cells infected or noninfected with ISKNV detected by Western blotting. (E) IDH2 activity at 72 hpi in pS3 or siS3 cells infected with ISKNV. (F) α-KGDH at 72 hpi in pS3 or siS3 cells infected with ISKNV. (G) The copy number of ISKNV genome in pS3 or siS3 cells at 36 hpi by determination of real-time PCR. (H) ISKNV titers in supernatant of pS3 or siS3 cells at 72 hpi by TCID 50 analysis.

    Article Snippet: Primary antibodies used in this study included anti-mTOR (7C10), anti-p-mTOR (ser2448) (Cell Signaling Technology, Danvers, MA), anti-SIRT3, anti-GLS1, anti-GDH, anti-IDH2, anti-PGC-1α, anti-α-KGDH (Proteintech, USA), and anti-β-actin (Abcam, USA).

    Techniques: Infection, Transfection, Plasmid Preparation, Construct, Expressing, Real-time Polymerase Chain Reaction, Western Blot, Activity Assay

    PGC-1α regulated expression of SIRT3 and metabolic genes, and benefited the production of ISKNV. (A) CPB cells were transfected with non-targeting siRNAs (NC) or siRNAs target PGC-1α gene (siP) to knock down the expression of PGC-1α. mRNA and protein expressions of PGC-1α in NC and siP cells were detected by real-time PCR and Western blotting. (B) mRNA and protein expression of PGC-1α, SIRT3, GLS1, GDH, and IDH2 in NC and siP cells infected or noninfected with ISKNV, determined by real-time PCR and Western blotting. (C) mRNA and protein expression of PGC-1α in ISKNV-infected or noninfected CPB cells treated with LY294002, rapamycin, or MHY1485 for 72 h detected by real-time PCR and Western blotting. (D) The copy number of the ISKNV genome in NC or siP cells at 36 hpi by determination of real-time PCR. (E) ISKNV titers in supernatant of NC or siP cells at 72 hpi by TCID 50 analysis.

    Journal: Microbiology Spectrum

    Article Title: The mTOR/PGC-1α/SIRT3 Pathway Drives Reductive Glutamine Metabolism to Reduce Oxidative Stress Caused by ISKNV in CPB Cells

    doi: 10.1128/spectrum.02310-21

    Figure Lengend Snippet: PGC-1α regulated expression of SIRT3 and metabolic genes, and benefited the production of ISKNV. (A) CPB cells were transfected with non-targeting siRNAs (NC) or siRNAs target PGC-1α gene (siP) to knock down the expression of PGC-1α. mRNA and protein expressions of PGC-1α in NC and siP cells were detected by real-time PCR and Western blotting. (B) mRNA and protein expression of PGC-1α, SIRT3, GLS1, GDH, and IDH2 in NC and siP cells infected or noninfected with ISKNV, determined by real-time PCR and Western blotting. (C) mRNA and protein expression of PGC-1α in ISKNV-infected or noninfected CPB cells treated with LY294002, rapamycin, or MHY1485 for 72 h detected by real-time PCR and Western blotting. (D) The copy number of the ISKNV genome in NC or siP cells at 36 hpi by determination of real-time PCR. (E) ISKNV titers in supernatant of NC or siP cells at 72 hpi by TCID 50 analysis.

    Article Snippet: Primary antibodies used in this study included anti-mTOR (7C10), anti-p-mTOR (ser2448) (Cell Signaling Technology, Danvers, MA), anti-SIRT3, anti-GLS1, anti-GDH, anti-IDH2, anti-PGC-1α, anti-α-KGDH (Proteintech, USA), and anti-β-actin (Abcam, USA).

    Techniques: Expressing, Transfection, Real-time Polymerase Chain Reaction, Western Blot, Infection

    Primers used in this study

    Journal: Microbiology Spectrum

    Article Title: The mTOR/PGC-1α/SIRT3 Pathway Drives Reductive Glutamine Metabolism to Reduce Oxidative Stress Caused by ISKNV in CPB Cells

    doi: 10.1128/spectrum.02310-21

    Figure Lengend Snippet: Primers used in this study

    Article Snippet: Primary antibodies used in this study included anti-mTOR (7C10), anti-p-mTOR (ser2448) (Cell Signaling Technology, Danvers, MA), anti-SIRT3, anti-GLS1, anti-GDH, anti-IDH2, anti-PGC-1α, anti-α-KGDH (Proteintech, USA), and anti-β-actin (Abcam, USA).

    Techniques: Sequencing, Expressing, Clone Assay