pgam1 Search Results


anti pgam1  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology anti pgam1
Anti Pgam1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti pgam1  (Cell Signaling Technology Inc)
94
Cell Signaling Technology Inc anti pgam1
Anti Pgam1, 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
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supplementaryfig  (Santa Cruz Biotechnology)
92
Santa Cruz Biotechnology supplementaryfig
Supplementaryfig, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti pgam1  (Novus Biologicals)
90
Novus Biologicals anti pgam1
Anti Pgam1, supplied by Novus Biologicals, 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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pgam1  (Novus Biologicals)
93
Novus Biologicals pgam1
A OCR, an index of oxygen consumption in mitochondria indicating oxidative phosphorylation coupled with glycolytic activity, was measured in 53KOLS cells expressing scramble or Rb shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-deoxy glucose. B ECAR, an index of the rate of lactate production indicating glycolytic activity, was measured in 53KOLS cells expressing scramble or Rb shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-deoxy glucose (2-DG). C Relative 2-(N-(7-Nitrobenz-2-oxa-1,3-diazol-4-yl)Amino)-2-Deoxyglucose (2-NBDG) fluorescence intensity showing glucose uptake in 53KOLS cells expressing scramble or Rb shRNA. Paired student’s t-test was performed. * P < 0.05 and n.s., not significant. D ECAR was measured in 53KOLS cells expressing scramble or Rb shRNA following the treatment with 1 mM pyruvate. E ECAR was measured in 53KOLS. cells expressing scramble or Rb shRNA following the treatment with 4 mM glutamine. F OCR in 53KOLS cells expressing scramble or Rb shRNA was measured in the presence or absence of a glutaminase inhibitor, BPTES (5 μM). Tukey HSD test was performed. ** P < 0.01 and n.s., not significant. G Relative incorporation of [U- 14 C]-glucose into lipid. 53KOLS cells were cultured in the presence of [U- 14 C]-glucose (6.25 μCi/ml) for 24 h. 14 C activity was measured using liquid scintillation counter. Paired student’s t-test was performed. *** P < 0.001. H Relative incorporation of [U- 14 C]-glutamine into lipid. 53KOLS cells were cultured in the presence of [U- 14 C]-glutamine (62.5 μCi/ml) for 24 h. Paired student’s t-test was performed. n.s., not significant. I Relative lipid incorporation of 3 H 2 O. 53KOLS cells were cultured in the presence of 3 H 2 O (20 v/v%) for 24 h. 3 H activity was measured using liquid scintillation counter. Paired student’s t-test was performed. * P < 0.05. J IB of the indicated proteins in 53KOLS cells overexpressing Pgam2. K Relative lipid incorporation of [U- 14 C]-glucose in 53KOLS cells overexpressing Pgam2. Tukey’s HSD test was performed. * P < 0.05 and n.s., not significant. L ECAR was measured in AGS cells expressing scramble or RB1 shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-DG. M Relative 2-NBDG fluorescence intensity in AGS cells expressing scramble or RB1 shRNA. Tukey HSD test was performed. *** P < 0.001 and ** P < 0.01. N Relative 2-NBDG fluorescence intensity in SNU-638 cells expressing scramble or RB1 shRNA. Tukey HSD test was performed. ** P < 0.01 and ** P < 0.05. O Absolute glucose consumption rate within 24 h in SNU-638 cells expressing scramble or RB1 shRNA. Paired student’s t-test was performed. * P < 0.05. P Absolute lactate secretion rate within 24 h in SNU-638 cells expressing scramble or RB1 shRNA. Paired student’s t-test was performed. * P < 0.05. Q Relative incorporation of [U- 14 C]-glucose into lipid in AGS cells expressing scramble or RB1 shRNA those were cultured in the presence of [U- 14 C]-glucose (6.25 μCi/ml) for 24 h. 14 C activity was measured using liquid scintillation counter. Tukey HSD test was performed. ** P < 0.01 and * P < 0.05. R Effect of <t>PGAM1</t> overexpression on glycolytic flow in RB1-depleted AGS cells. S Effect of PGAM1 overexpression on glucose consumption for 24 h in RB1-depleted AGS cells. Glucose concentration in medium was determined using colorimetric assay. Tukey HSD test was performed. * P < 0.05. All data are shown as the mean ± SEM.
Pgam1, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pgam1  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology pgam1
A OCR, an index of oxygen consumption in mitochondria indicating oxidative phosphorylation coupled with glycolytic activity, was measured in 53KOLS cells expressing scramble or Rb shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-deoxy glucose. B ECAR, an index of the rate of lactate production indicating glycolytic activity, was measured in 53KOLS cells expressing scramble or Rb shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-deoxy glucose (2-DG). C Relative 2-(N-(7-Nitrobenz-2-oxa-1,3-diazol-4-yl)Amino)-2-Deoxyglucose (2-NBDG) fluorescence intensity showing glucose uptake in 53KOLS cells expressing scramble or Rb shRNA. Paired student’s t-test was performed. * P < 0.05 and n.s., not significant. D ECAR was measured in 53KOLS cells expressing scramble or Rb shRNA following the treatment with 1 mM pyruvate. E ECAR was measured in 53KOLS. cells expressing scramble or Rb shRNA following the treatment with 4 mM glutamine. F OCR in 53KOLS cells expressing scramble or Rb shRNA was measured in the presence or absence of a glutaminase inhibitor, BPTES (5 μM). Tukey HSD test was performed. ** P < 0.01 and n.s., not significant. G Relative incorporation of [U- 14 C]-glucose into lipid. 53KOLS cells were cultured in the presence of [U- 14 C]-glucose (6.25 μCi/ml) for 24 h. 14 C activity was measured using liquid scintillation counter. Paired student’s t-test was performed. *** P < 0.001. H Relative incorporation of [U- 14 C]-glutamine into lipid. 53KOLS cells were cultured in the presence of [U- 14 C]-glutamine (62.5 μCi/ml) for 24 h. Paired student’s t-test was performed. n.s., not significant. I Relative lipid incorporation of 3 H 2 O. 53KOLS cells were cultured in the presence of 3 H 2 O (20 v/v%) for 24 h. 3 H activity was measured using liquid scintillation counter. Paired student’s t-test was performed. * P < 0.05. J IB of the indicated proteins in 53KOLS cells overexpressing Pgam2. K Relative lipid incorporation of [U- 14 C]-glucose in 53KOLS cells overexpressing Pgam2. Tukey’s HSD test was performed. * P < 0.05 and n.s., not significant. L ECAR was measured in AGS cells expressing scramble or RB1 shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-DG. M Relative 2-NBDG fluorescence intensity in AGS cells expressing scramble or RB1 shRNA. Tukey HSD test was performed. *** P < 0.001 and ** P < 0.01. N Relative 2-NBDG fluorescence intensity in SNU-638 cells expressing scramble or RB1 shRNA. Tukey HSD test was performed. ** P < 0.01 and ** P < 0.05. O Absolute glucose consumption rate within 24 h in SNU-638 cells expressing scramble or RB1 shRNA. Paired student’s t-test was performed. * P < 0.05. P Absolute lactate secretion rate within 24 h in SNU-638 cells expressing scramble or RB1 shRNA. Paired student’s t-test was performed. * P < 0.05. Q Relative incorporation of [U- 14 C]-glucose into lipid in AGS cells expressing scramble or RB1 shRNA those were cultured in the presence of [U- 14 C]-glucose (6.25 μCi/ml) for 24 h. 14 C activity was measured using liquid scintillation counter. Tukey HSD test was performed. ** P < 0.01 and * P < 0.05. R Effect of <t>PGAM1</t> overexpression on glycolytic flow in RB1-depleted AGS cells. S Effect of PGAM1 overexpression on glucose consumption for 24 h in RB1-depleted AGS cells. Glucose concentration in medium was determined using colorimetric assay. Tukey HSD test was performed. * P < 0.05. All data are shown as the mean ± SEM.
Pgam1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pgam  (Novus Biologicals)
94
Novus Biologicals pgam
<t>PGAM</t> was localized with the use of antibody against the C-terminal peptide of the protein in the cells cultured in serum-free medium re-supplemented with IGF-1, insulin or insulin and inhibitor of PI3K (wortmannin). Bar=15 μm.
Pgam, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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phosphoglucomutase 2 pgam2 goat nb100 774 novus biologicals  (Novus Biologicals)
88
Novus Biologicals phosphoglucomutase 2 pgam2 goat nb100 774 novus biologicals
Figure 4. Co-culturing-induced changes in visibility of <t>PGAM2</t> C-terminus, immunostaining intensity of TIGAR, and ROS and lactate production. PGAM2 is presented in white, nuclei are blue. White arrow point to cardiomyocytes. Bar = 10 µm. Lactate production is presented as pmol of lactate per cell per 48 h. Error bars represent standard deviation from three measurements. RFU – relative fluorescence units.
Phosphoglucomutase 2 Pgam2 Goat Nb100 774 Novus Biologicals, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pgam1 antibody  (Novus Biologicals)
90
Novus Biologicals pgam1 antibody
Figure 4. Co-culturing-induced changes in visibility of <t>PGAM2</t> C-terminus, immunostaining intensity of TIGAR, and ROS and lactate production. PGAM2 is presented in white, nuclei are blue. White arrow point to cardiomyocytes. Bar = 10 µm. Lactate production is presented as pmol of lactate per cell per 48 h. Error bars represent standard deviation from three measurements. RFU – relative fluorescence units.
Pgam1 Antibody, supplied by Novus Biologicals, 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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alexa fluor 405  (Novus Biologicals)
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Novus Biologicals alexa fluor 405
Figure 4. Co-culturing-induced changes in visibility of <t>PGAM2</t> C-terminus, immunostaining intensity of TIGAR, and ROS and lactate production. PGAM2 is presented in white, nuclei are blue. White arrow point to cardiomyocytes. Bar = 10 µm. Lactate production is presented as pmol of lactate per cell per 48 h. Error bars represent standard deviation from three measurements. RFU – relative fluorescence units.
Alexa Fluor 405, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pgam1 antibody  (Proteintech)
94
Proteintech pgam1 antibody
Gene silencing and glycolytic regulation of si-Ce6@tLyp-1-NPs. ( A ) Effect of UTMD in vitro ( B ) CEUS mode, n = 3 ( C ) Schematic illustration of the B16F10 cells treated with si-Ce6@tLyP-1-NPs combined with US ( D ) CLSM observation of the localization of FAM-siRNA in B16-F10 cells after transfection with free siRNA, si-Ce6@NPs(+), si-Ce6@tLyP-1-NPs (+). The scale was 10 μm, and Phalloidin was the cytoskeleton. DAPI is the nucleus. ( E ) The relative mRNA expression of FTO in different groups of B16-F10 ( F , G ) The protein expression of FTO in different groups of B16-F10. ( H ) Volcano plot of DEGs. ( I ) Heat map of genes involved in the glycolytic pathway. ( J) Representative pathways enriched in the identified genes as determined by GSEA (NES= −1.4016, p-value = 0.0424). ( K , L ) The mRNA expression levels of HK2 and <t>PGAM1</t> in the control group and B16-F10 cells treated with different methods. ( M ) Representative western blot images of HK2 and PGAM1 expression in control and treated B16-F10 cell groups. ( N , O ) Quantitative analysis of HK2 and PGAM1 protein expression. ( P ) Lactate levels in cell culture medium were measured
Pgam1 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


A OCR, an index of oxygen consumption in mitochondria indicating oxidative phosphorylation coupled with glycolytic activity, was measured in 53KOLS cells expressing scramble or Rb shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-deoxy glucose. B ECAR, an index of the rate of lactate production indicating glycolytic activity, was measured in 53KOLS cells expressing scramble or Rb shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-deoxy glucose (2-DG). C Relative 2-(N-(7-Nitrobenz-2-oxa-1,3-diazol-4-yl)Amino)-2-Deoxyglucose (2-NBDG) fluorescence intensity showing glucose uptake in 53KOLS cells expressing scramble or Rb shRNA. Paired student’s t-test was performed. * P < 0.05 and n.s., not significant. D ECAR was measured in 53KOLS cells expressing scramble or Rb shRNA following the treatment with 1 mM pyruvate. E ECAR was measured in 53KOLS. cells expressing scramble or Rb shRNA following the treatment with 4 mM glutamine. F OCR in 53KOLS cells expressing scramble or Rb shRNA was measured in the presence or absence of a glutaminase inhibitor, BPTES (5 μM). Tukey HSD test was performed. ** P < 0.01 and n.s., not significant. G Relative incorporation of [U- 14 C]-glucose into lipid. 53KOLS cells were cultured in the presence of [U- 14 C]-glucose (6.25 μCi/ml) for 24 h. 14 C activity was measured using liquid scintillation counter. Paired student’s t-test was performed. *** P < 0.001. H Relative incorporation of [U- 14 C]-glutamine into lipid. 53KOLS cells were cultured in the presence of [U- 14 C]-glutamine (62.5 μCi/ml) for 24 h. Paired student’s t-test was performed. n.s., not significant. I Relative lipid incorporation of 3 H 2 O. 53KOLS cells were cultured in the presence of 3 H 2 O (20 v/v%) for 24 h. 3 H activity was measured using liquid scintillation counter. Paired student’s t-test was performed. * P < 0.05. J IB of the indicated proteins in 53KOLS cells overexpressing Pgam2. K Relative lipid incorporation of [U- 14 C]-glucose in 53KOLS cells overexpressing Pgam2. Tukey’s HSD test was performed. * P < 0.05 and n.s., not significant. L ECAR was measured in AGS cells expressing scramble or RB1 shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-DG. M Relative 2-NBDG fluorescence intensity in AGS cells expressing scramble or RB1 shRNA. Tukey HSD test was performed. *** P < 0.001 and ** P < 0.01. N Relative 2-NBDG fluorescence intensity in SNU-638 cells expressing scramble or RB1 shRNA. Tukey HSD test was performed. ** P < 0.01 and ** P < 0.05. O Absolute glucose consumption rate within 24 h in SNU-638 cells expressing scramble or RB1 shRNA. Paired student’s t-test was performed. * P < 0.05. P Absolute lactate secretion rate within 24 h in SNU-638 cells expressing scramble or RB1 shRNA. Paired student’s t-test was performed. * P < 0.05. Q Relative incorporation of [U- 14 C]-glucose into lipid in AGS cells expressing scramble or RB1 shRNA those were cultured in the presence of [U- 14 C]-glucose (6.25 μCi/ml) for 24 h. 14 C activity was measured using liquid scintillation counter. Tukey HSD test was performed. ** P < 0.01 and * P < 0.05. R Effect of PGAM1 overexpression on glycolytic flow in RB1-depleted AGS cells. S Effect of PGAM1 overexpression on glucose consumption for 24 h in RB1-depleted AGS cells. Glucose concentration in medium was determined using colorimetric assay. Tukey HSD test was performed. * P < 0.05. All data are shown as the mean ± SEM.

Journal: Cell Death & Disease

Article Title: RB1 controls differentiation through positive regulation of phosphoglycerate mutases

doi: 10.1038/s41419-025-07850-3

Figure Lengend Snippet: A OCR, an index of oxygen consumption in mitochondria indicating oxidative phosphorylation coupled with glycolytic activity, was measured in 53KOLS cells expressing scramble or Rb shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-deoxy glucose. B ECAR, an index of the rate of lactate production indicating glycolytic activity, was measured in 53KOLS cells expressing scramble or Rb shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-deoxy glucose (2-DG). C Relative 2-(N-(7-Nitrobenz-2-oxa-1,3-diazol-4-yl)Amino)-2-Deoxyglucose (2-NBDG) fluorescence intensity showing glucose uptake in 53KOLS cells expressing scramble or Rb shRNA. Paired student’s t-test was performed. * P < 0.05 and n.s., not significant. D ECAR was measured in 53KOLS cells expressing scramble or Rb shRNA following the treatment with 1 mM pyruvate. E ECAR was measured in 53KOLS. cells expressing scramble or Rb shRNA following the treatment with 4 mM glutamine. F OCR in 53KOLS cells expressing scramble or Rb shRNA was measured in the presence or absence of a glutaminase inhibitor, BPTES (5 μM). Tukey HSD test was performed. ** P < 0.01 and n.s., not significant. G Relative incorporation of [U- 14 C]-glucose into lipid. 53KOLS cells were cultured in the presence of [U- 14 C]-glucose (6.25 μCi/ml) for 24 h. 14 C activity was measured using liquid scintillation counter. Paired student’s t-test was performed. *** P < 0.001. H Relative incorporation of [U- 14 C]-glutamine into lipid. 53KOLS cells were cultured in the presence of [U- 14 C]-glutamine (62.5 μCi/ml) for 24 h. Paired student’s t-test was performed. n.s., not significant. I Relative lipid incorporation of 3 H 2 O. 53KOLS cells were cultured in the presence of 3 H 2 O (20 v/v%) for 24 h. 3 H activity was measured using liquid scintillation counter. Paired student’s t-test was performed. * P < 0.05. J IB of the indicated proteins in 53KOLS cells overexpressing Pgam2. K Relative lipid incorporation of [U- 14 C]-glucose in 53KOLS cells overexpressing Pgam2. Tukey’s HSD test was performed. * P < 0.05 and n.s., not significant. L ECAR was measured in AGS cells expressing scramble or RB1 shRNA. Cells were sequentially treated with 10.5 mM glucose and 100 mM 2-DG. M Relative 2-NBDG fluorescence intensity in AGS cells expressing scramble or RB1 shRNA. Tukey HSD test was performed. *** P < 0.001 and ** P < 0.01. N Relative 2-NBDG fluorescence intensity in SNU-638 cells expressing scramble or RB1 shRNA. Tukey HSD test was performed. ** P < 0.01 and ** P < 0.05. O Absolute glucose consumption rate within 24 h in SNU-638 cells expressing scramble or RB1 shRNA. Paired student’s t-test was performed. * P < 0.05. P Absolute lactate secretion rate within 24 h in SNU-638 cells expressing scramble or RB1 shRNA. Paired student’s t-test was performed. * P < 0.05. Q Relative incorporation of [U- 14 C]-glucose into lipid in AGS cells expressing scramble or RB1 shRNA those were cultured in the presence of [U- 14 C]-glucose (6.25 μCi/ml) for 24 h. 14 C activity was measured using liquid scintillation counter. Tukey HSD test was performed. ** P < 0.01 and * P < 0.05. R Effect of PGAM1 overexpression on glycolytic flow in RB1-depleted AGS cells. S Effect of PGAM1 overexpression on glucose consumption for 24 h in RB1-depleted AGS cells. Glucose concentration in medium was determined using colorimetric assay. Tukey HSD test was performed. * P < 0.05. All data are shown as the mean ± SEM.

Article Snippet: Primary antibodies were as follow s : Total RB (sc-50, Santa Cruz, Dallas, TX, USA), PGAM2 (PA5-24006, Thermo Fisher Scientific), PGAM1 (NBP1-49532, Novus Biologicals, Abingdon, United Kingdom), PKM1 (#7067, Cell Signaling Technology, Danvers, MA, USA), PKM2 (#4053 Cell Signaling Technology), HK1 (#2024, Cell Signaling Technology), HK2 (#2867, Cell Signaling Technology), PFKP (13389-1-AP, Proteintech, Rosemont, IL, USA), PFKM (55028-1-AP, Proteintech), PKM1 (#7607, Cell Signaling Technology), PKM2 (#4053, Cell Signaling Technology), ENO3 (55234-1-AP, Proteintech), MPC1 (#14462, Cell Signaling Technology) MPC2 (20049-1-AP, Proteintech), Phospho-PDH (AP1062, Merck Millipore), whole PDH (#3205, Cell Signaling Technology), LDHA (#2012, Cell Signaling Technology), α-Tubulin (#CP06, Merck Millipore), MEF2A (#9736, Cell Signaling Technology), MEF2D (610775, BD Biosciences, San Jose, CA), KDM5A (18825-1-AP, Proteintech), HRP-linked anti-rabbit antibody (#7074, Cell Signaling Technology) and HRP-linked anti-mouse antibody (#7076, Cell Signaling Technology).

Techniques: Phospho-proteomics, Activity Assay, Expressing, shRNA, Fluorescence, Cell Culture, Over Expression, Concentration Assay, Colorimetric Assay

A Phase-contrast image of spheres developed from Rb-depleted 53KOLS cells expressing LacZ or PGAM2. B Number of spheres developed from Rb-depleted 53KOLS cells expressing LacZ or PGAM2. C mRNA expression of the indicated gene in monolayer or spheroid. Tukey’s HSD test was performed. **** P < 0.0001. D Phase-contrast image of spheres developed from AGS cells expressing scramble or RB1 shRNA. Scale bar; 200 μm. E Number of spheres developed from RB1-depleted AGS cells under 3D culture conditions. Tukey’s HSD test was performed. ** P < 0.01 and * P < 0.05. F Phase-contrast image of spheres developed from AGS cells expressing LacZ or PGAM1, those with or without RB1-depletion. G Number of spheres developed from the indicated cells cultured under the indicated 3D conditions. H Phase-contrast image of spheres developed from AGS cells expressing scramble or PGAM1 shRNA. I Number of spheres developed from PGAM1-depleted AGS cells under 3D culture conditions. Tukey’s HSD test was performed. ** P < 0.01. All data are shown as the mean ± SEM.

Journal: Cell Death & Disease

Article Title: RB1 controls differentiation through positive regulation of phosphoglycerate mutases

doi: 10.1038/s41419-025-07850-3

Figure Lengend Snippet: A Phase-contrast image of spheres developed from Rb-depleted 53KOLS cells expressing LacZ or PGAM2. B Number of spheres developed from Rb-depleted 53KOLS cells expressing LacZ or PGAM2. C mRNA expression of the indicated gene in monolayer or spheroid. Tukey’s HSD test was performed. **** P < 0.0001. D Phase-contrast image of spheres developed from AGS cells expressing scramble or RB1 shRNA. Scale bar; 200 μm. E Number of spheres developed from RB1-depleted AGS cells under 3D culture conditions. Tukey’s HSD test was performed. ** P < 0.01 and * P < 0.05. F Phase-contrast image of spheres developed from AGS cells expressing LacZ or PGAM1, those with or without RB1-depletion. G Number of spheres developed from the indicated cells cultured under the indicated 3D conditions. H Phase-contrast image of spheres developed from AGS cells expressing scramble or PGAM1 shRNA. I Number of spheres developed from PGAM1-depleted AGS cells under 3D culture conditions. Tukey’s HSD test was performed. ** P < 0.01. All data are shown as the mean ± SEM.

Article Snippet: Primary antibodies were as follow s : Total RB (sc-50, Santa Cruz, Dallas, TX, USA), PGAM2 (PA5-24006, Thermo Fisher Scientific), PGAM1 (NBP1-49532, Novus Biologicals, Abingdon, United Kingdom), PKM1 (#7067, Cell Signaling Technology, Danvers, MA, USA), PKM2 (#4053 Cell Signaling Technology), HK1 (#2024, Cell Signaling Technology), HK2 (#2867, Cell Signaling Technology), PFKP (13389-1-AP, Proteintech, Rosemont, IL, USA), PFKM (55028-1-AP, Proteintech), PKM1 (#7607, Cell Signaling Technology), PKM2 (#4053, Cell Signaling Technology), ENO3 (55234-1-AP, Proteintech), MPC1 (#14462, Cell Signaling Technology) MPC2 (20049-1-AP, Proteintech), Phospho-PDH (AP1062, Merck Millipore), whole PDH (#3205, Cell Signaling Technology), LDHA (#2012, Cell Signaling Technology), α-Tubulin (#CP06, Merck Millipore), MEF2A (#9736, Cell Signaling Technology), MEF2D (610775, BD Biosciences, San Jose, CA), KDM5A (18825-1-AP, Proteintech), HRP-linked anti-rabbit antibody (#7074, Cell Signaling Technology) and HRP-linked anti-mouse antibody (#7076, Cell Signaling Technology).

Techniques: Expressing, shRNA, Cell Culture

A Heatmap of genes related to glycolysis in a time course microarray sampled during differentiation in C2C12 cells. B IB of the indicated proteins in differentiated and undifferentiated C2C12 cells. C mRNA expression levels of the indicated genes in C2C12 cells expressing scramble or Rb shRNA. C2C12 cells were differentiated under low serum conditions for 7 days. Tukey’s HSD test was performed. **** P < 0.0001 and * P < 0.05. D IB of the indicated proteins in C2C12 cells expressing scramble or Pgam2 shRNA those with or without exposure to stimuli to induce myogenic differentiation. E Immunocytochemistry of myosin heavy chain (MHC) in C2C12 cells expressing scramble or Pgam2 shRNA and exposed to stimuli to induce myogenic differentiation for 7 days. F mRNA expression levels of the indicated genes in C2C12 cells expressing scramble or Rb shRNA. Cells were differentiated in the presence or absence of pyruvate for 7 days. Tukey’s HSD test was performed. ** P < 0.01, * P < 0.05 and n.s.; not significant. G RNA-seq heatmap of genes related to glycolysis during adipogenic differentiation in 3T3L1 cells. H IB of the indicated proteins in differentiated and undifferentiated 3T3L1 cells. I IB of the indicated proteins in PGAM1-depleted 3T3L1 after exposure to stimuli to induce adipogenic differentiation. J Oil red staining of 3T3L1 cells transduced with the indicated gRNA and treated with vehicle or 4 mM pyruvate under the culture conditions to induce adipogenic differentiation. K IB of the indicated proteins in PGAM1-depleted 3T3L1 cells after exposure to stimuli to induce adipogenic differentiation in the presence or absence of 4 mM pyruvate. All data are shown as the mean ± SEM.

Journal: Cell Death & Disease

Article Title: RB1 controls differentiation through positive regulation of phosphoglycerate mutases

doi: 10.1038/s41419-025-07850-3

Figure Lengend Snippet: A Heatmap of genes related to glycolysis in a time course microarray sampled during differentiation in C2C12 cells. B IB of the indicated proteins in differentiated and undifferentiated C2C12 cells. C mRNA expression levels of the indicated genes in C2C12 cells expressing scramble or Rb shRNA. C2C12 cells were differentiated under low serum conditions for 7 days. Tukey’s HSD test was performed. **** P < 0.0001 and * P < 0.05. D IB of the indicated proteins in C2C12 cells expressing scramble or Pgam2 shRNA those with or without exposure to stimuli to induce myogenic differentiation. E Immunocytochemistry of myosin heavy chain (MHC) in C2C12 cells expressing scramble or Pgam2 shRNA and exposed to stimuli to induce myogenic differentiation for 7 days. F mRNA expression levels of the indicated genes in C2C12 cells expressing scramble or Rb shRNA. Cells were differentiated in the presence or absence of pyruvate for 7 days. Tukey’s HSD test was performed. ** P < 0.01, * P < 0.05 and n.s.; not significant. G RNA-seq heatmap of genes related to glycolysis during adipogenic differentiation in 3T3L1 cells. H IB of the indicated proteins in differentiated and undifferentiated 3T3L1 cells. I IB of the indicated proteins in PGAM1-depleted 3T3L1 after exposure to stimuli to induce adipogenic differentiation. J Oil red staining of 3T3L1 cells transduced with the indicated gRNA and treated with vehicle or 4 mM pyruvate under the culture conditions to induce adipogenic differentiation. K IB of the indicated proteins in PGAM1-depleted 3T3L1 cells after exposure to stimuli to induce adipogenic differentiation in the presence or absence of 4 mM pyruvate. All data are shown as the mean ± SEM.

Article Snippet: Primary antibodies were as follow s : Total RB (sc-50, Santa Cruz, Dallas, TX, USA), PGAM2 (PA5-24006, Thermo Fisher Scientific), PGAM1 (NBP1-49532, Novus Biologicals, Abingdon, United Kingdom), PKM1 (#7067, Cell Signaling Technology, Danvers, MA, USA), PKM2 (#4053 Cell Signaling Technology), HK1 (#2024, Cell Signaling Technology), HK2 (#2867, Cell Signaling Technology), PFKP (13389-1-AP, Proteintech, Rosemont, IL, USA), PFKM (55028-1-AP, Proteintech), PKM1 (#7607, Cell Signaling Technology), PKM2 (#4053, Cell Signaling Technology), ENO3 (55234-1-AP, Proteintech), MPC1 (#14462, Cell Signaling Technology) MPC2 (20049-1-AP, Proteintech), Phospho-PDH (AP1062, Merck Millipore), whole PDH (#3205, Cell Signaling Technology), LDHA (#2012, Cell Signaling Technology), α-Tubulin (#CP06, Merck Millipore), MEF2A (#9736, Cell Signaling Technology), MEF2D (610775, BD Biosciences, San Jose, CA), KDM5A (18825-1-AP, Proteintech), HRP-linked anti-rabbit antibody (#7074, Cell Signaling Technology) and HRP-linked anti-mouse antibody (#7076, Cell Signaling Technology).

Techniques: Microarray, Expressing, shRNA, Immunocytochemistry, RNA Sequencing, Staining, Transduction

A Expression levels of Pgam2 in Myod-depleted C2C12 cells exposed to stimuli to induce myogenic differentiation. Expression levels of Pgam2 from microarray were shown in log 2 Fc. B Expression levels of myogenic transcription factors in 53KOLS cells. Data from RNA-seq was shown in Log 2 RPKM. C IB of the indicated protein in Mef2a or Mef2d-depleted 53KOLS cells. D Relative mRNA levels of the indicated genes in 53KOLS cells expressing scramble, Mef2a, or Mef2d shRNA. Data are shown as the mean ± standard error (SEM). Tukey HSD test was performed. *** P < 0.001, ** P < 0.01, * P < 0.05 and n.s., not significant. E Correlation of mRNA expression level between MEF2A/D and PGAM1 genes in TCGA dataset. Spearman’s correlation test was performed. F Sequence of the promoter region of mouse Pgam2 gene. G ChIP-qPCR assessment of H3K4me2 at the Mef2 binding site in the Pgam2 promoter of 53KOLS cells, those with or without Rb depletion. Paired student’s t-test was performed. ** P < 0.01. All data are shown as the mean ± SEM.

Journal: Cell Death & Disease

Article Title: RB1 controls differentiation through positive regulation of phosphoglycerate mutases

doi: 10.1038/s41419-025-07850-3

Figure Lengend Snippet: A Expression levels of Pgam2 in Myod-depleted C2C12 cells exposed to stimuli to induce myogenic differentiation. Expression levels of Pgam2 from microarray were shown in log 2 Fc. B Expression levels of myogenic transcription factors in 53KOLS cells. Data from RNA-seq was shown in Log 2 RPKM. C IB of the indicated protein in Mef2a or Mef2d-depleted 53KOLS cells. D Relative mRNA levels of the indicated genes in 53KOLS cells expressing scramble, Mef2a, or Mef2d shRNA. Data are shown as the mean ± standard error (SEM). Tukey HSD test was performed. *** P < 0.001, ** P < 0.01, * P < 0.05 and n.s., not significant. E Correlation of mRNA expression level between MEF2A/D and PGAM1 genes in TCGA dataset. Spearman’s correlation test was performed. F Sequence of the promoter region of mouse Pgam2 gene. G ChIP-qPCR assessment of H3K4me2 at the Mef2 binding site in the Pgam2 promoter of 53KOLS cells, those with or without Rb depletion. Paired student’s t-test was performed. ** P < 0.01. All data are shown as the mean ± SEM.

Article Snippet: Primary antibodies were as follow s : Total RB (sc-50, Santa Cruz, Dallas, TX, USA), PGAM2 (PA5-24006, Thermo Fisher Scientific), PGAM1 (NBP1-49532, Novus Biologicals, Abingdon, United Kingdom), PKM1 (#7067, Cell Signaling Technology, Danvers, MA, USA), PKM2 (#4053 Cell Signaling Technology), HK1 (#2024, Cell Signaling Technology), HK2 (#2867, Cell Signaling Technology), PFKP (13389-1-AP, Proteintech, Rosemont, IL, USA), PFKM (55028-1-AP, Proteintech), PKM1 (#7607, Cell Signaling Technology), PKM2 (#4053, Cell Signaling Technology), ENO3 (55234-1-AP, Proteintech), MPC1 (#14462, Cell Signaling Technology) MPC2 (20049-1-AP, Proteintech), Phospho-PDH (AP1062, Merck Millipore), whole PDH (#3205, Cell Signaling Technology), LDHA (#2012, Cell Signaling Technology), α-Tubulin (#CP06, Merck Millipore), MEF2A (#9736, Cell Signaling Technology), MEF2D (610775, BD Biosciences, San Jose, CA), KDM5A (18825-1-AP, Proteintech), HRP-linked anti-rabbit antibody (#7074, Cell Signaling Technology) and HRP-linked anti-mouse antibody (#7076, Cell Signaling Technology).

Techniques: Expressing, Microarray, RNA Sequencing, shRNA, Sequencing, ChIP-qPCR, Binding Assay

A H3K4me2 ChIP-qPCR of PGAM1 and intergenic regions in SNU-638 cells those transduced with scramble or RB1 shRNA. Tukey’s HSD test was performed. ** P < 0.01, and n.s., not significant. B H3K9Ac ChIP-qPCR of PGAM1 and intergenic regions in SNU-638 cells those transduced with scramble or RB1 shRNA. Tukey’s HSD test was performed. n.s., not significant. C Venn diagram of number of genes that were down-regulated in RB1-depleted and upregulated in RB1-depleted SNU-638 cells upon treatment with a KDM inhibitor. D Relative mRNA levels of PGAM1 in RB1-depleted SNU-638 cells upon treatment with 1 mM JIB-4 or DMSO. Tukey’s HSD test was performed. **** P < 0.0001, *** P < 0.001 and ** P < 0.01. E IB of the indicated proteins in SNU-638 cells expressing scramble or RB1 shRNA and treated with 1 mM JIB-4 or DMSO. F IB of the indicated proteins in RB1-depleted cells expressing scramble or KDM5A shRNA. All data are shown as the mean ± SEM.

Journal: Cell Death & Disease

Article Title: RB1 controls differentiation through positive regulation of phosphoglycerate mutases

doi: 10.1038/s41419-025-07850-3

Figure Lengend Snippet: A H3K4me2 ChIP-qPCR of PGAM1 and intergenic regions in SNU-638 cells those transduced with scramble or RB1 shRNA. Tukey’s HSD test was performed. ** P < 0.01, and n.s., not significant. B H3K9Ac ChIP-qPCR of PGAM1 and intergenic regions in SNU-638 cells those transduced with scramble or RB1 shRNA. Tukey’s HSD test was performed. n.s., not significant. C Venn diagram of number of genes that were down-regulated in RB1-depleted and upregulated in RB1-depleted SNU-638 cells upon treatment with a KDM inhibitor. D Relative mRNA levels of PGAM1 in RB1-depleted SNU-638 cells upon treatment with 1 mM JIB-4 or DMSO. Tukey’s HSD test was performed. **** P < 0.0001, *** P < 0.001 and ** P < 0.01. E IB of the indicated proteins in SNU-638 cells expressing scramble or RB1 shRNA and treated with 1 mM JIB-4 or DMSO. F IB of the indicated proteins in RB1-depleted cells expressing scramble or KDM5A shRNA. All data are shown as the mean ± SEM.

Article Snippet: Primary antibodies were as follow s : Total RB (sc-50, Santa Cruz, Dallas, TX, USA), PGAM2 (PA5-24006, Thermo Fisher Scientific), PGAM1 (NBP1-49532, Novus Biologicals, Abingdon, United Kingdom), PKM1 (#7067, Cell Signaling Technology, Danvers, MA, USA), PKM2 (#4053 Cell Signaling Technology), HK1 (#2024, Cell Signaling Technology), HK2 (#2867, Cell Signaling Technology), PFKP (13389-1-AP, Proteintech, Rosemont, IL, USA), PFKM (55028-1-AP, Proteintech), PKM1 (#7607, Cell Signaling Technology), PKM2 (#4053, Cell Signaling Technology), ENO3 (55234-1-AP, Proteintech), MPC1 (#14462, Cell Signaling Technology) MPC2 (20049-1-AP, Proteintech), Phospho-PDH (AP1062, Merck Millipore), whole PDH (#3205, Cell Signaling Technology), LDHA (#2012, Cell Signaling Technology), α-Tubulin (#CP06, Merck Millipore), MEF2A (#9736, Cell Signaling Technology), MEF2D (610775, BD Biosciences, San Jose, CA), KDM5A (18825-1-AP, Proteintech), HRP-linked anti-rabbit antibody (#7074, Cell Signaling Technology) and HRP-linked anti-mouse antibody (#7076, Cell Signaling Technology).

Techniques: ChIP-qPCR, Transduction, shRNA, Expressing

PGAM was localized with the use of antibody against the C-terminal peptide of the protein in the cells cultured in serum-free medium re-supplemented with IGF-1, insulin or insulin and inhibitor of PI3K (wortmannin). Bar=15 μm.

Journal: Oncotarget

Article Title: Insulin/IGF1-PI3K-dependent nucleolar localization of a glycolytic enzyme – phosphoglycerate mutase 2, is necessary for proper structure of nucleolus and RNA synthesis

doi:

Figure Lengend Snippet: PGAM was localized with the use of antibody against the C-terminal peptide of the protein in the cells cultured in serum-free medium re-supplemented with IGF-1, insulin or insulin and inhibitor of PI3K (wortmannin). Bar=15 μm.

Article Snippet: Goat antibodies specific to C-terminal peptide of PGAM (NB100-774) were from Novus Biologicals.

Techniques: Cell Culture

Figure 4. Co-culturing-induced changes in visibility of PGAM2 C-terminus, immunostaining intensity of TIGAR, and ROS and lactate production. PGAM2 is presented in white, nuclei are blue. White arrow point to cardiomyocytes. Bar = 10 µm. Lactate production is presented as pmol of lactate per cell per 48 h. Error bars represent standard deviation from three measurements. RFU – relative fluorescence units.

Journal: Aging

Article Title: Cell-to-cell lactate shuttle operates in heart and is important in age-related heart failure.

doi: 10.18632/aging.102818

Figure Lengend Snippet: Figure 4. Co-culturing-induced changes in visibility of PGAM2 C-terminus, immunostaining intensity of TIGAR, and ROS and lactate production. PGAM2 is presented in white, nuclei are blue. White arrow point to cardiomyocytes. Bar = 10 µm. Lactate production is presented as pmol of lactate per cell per 48 h. Error bars represent standard deviation from three measurements. RFU – relative fluorescence units.

Article Snippet: Fructose 1,6-bisphosphatase (FBP) rabbit - [1] 1:800 C-terminal peptide of phosphoglucomutase 2 (PGAM2) goat NB100-774 Novus Biologicals 1:1000 Aldolase A rabbit - [2] 1:300 Hexokinase 2 rabbit AB3279 Sigma-Aldrich 1:400 Glycogen synthase kinase-3 beta (GSK3, total protein) mouse 610201 BD Biosciences 1:300 GSK3 phospho-Ser9 rabbit 04-1075 Merck 1:250 GSK3 phospho-Tyr216 mouse 612612 BD Biosciences 1:150 Hypoxia-inducible factor 1-alpha (HIF-1 alpha) rabbit bs-0737R Bioss 1:500 Proliferation marker protein Ki67 rabbit 301107 Novocastra 1:100 Phosphofructokinase muscle form (PFKM) rabbit HPA002117 Atlas Antibodies 1:200 Pyruvate kinase muscle form (PKM) goat R1108 Acris 1:400 Lactate dehydrogenase A (LDHA) rabbit NBP1-48336 Novus Biologicals 1:200 Lactate dehydrogenase B (LDHB) rabbit ab75167 Abcam 1:400 Monocarboxylate transporter 1 MCT1 (SLC16A1) mouse ab90582 Abcam 1:100 Monocarboxylate transporter 2 MCT2 (SLC16A7) rabbit bs-3995R Bioss 1:100 Monocarboxylate transporter 4 MCT4 (SLC16A3) rabbit HPA021451 Atlas Antibodies 1:50 TP53-induced glycolysis and apoptosis regulator (TIGAR) rabbit PRS4051 Sigma-Aldrich 1:400 Glucose transporter 1 (GLUT1) mouse ab40084 Abcam 1:50

Techniques: Immunostaining, Standard Deviation, Fluorescence

Gene silencing and glycolytic regulation of si-Ce6@tLyp-1-NPs. ( A ) Effect of UTMD in vitro ( B ) CEUS mode, n = 3 ( C ) Schematic illustration of the B16F10 cells treated with si-Ce6@tLyP-1-NPs combined with US ( D ) CLSM observation of the localization of FAM-siRNA in B16-F10 cells after transfection with free siRNA, si-Ce6@NPs(+), si-Ce6@tLyP-1-NPs (+). The scale was 10 μm, and Phalloidin was the cytoskeleton. DAPI is the nucleus. ( E ) The relative mRNA expression of FTO in different groups of B16-F10 ( F , G ) The protein expression of FTO in different groups of B16-F10. ( H ) Volcano plot of DEGs. ( I ) Heat map of genes involved in the glycolytic pathway. ( J) Representative pathways enriched in the identified genes as determined by GSEA (NES= −1.4016, p-value = 0.0424). ( K , L ) The mRNA expression levels of HK2 and PGAM1 in the control group and B16-F10 cells treated with different methods. ( M ) Representative western blot images of HK2 and PGAM1 expression in control and treated B16-F10 cell groups. ( N , O ) Quantitative analysis of HK2 and PGAM1 protein expression. ( P ) Lactate levels in cell culture medium were measured

Journal: Journal of Nanobiotechnology

Article Title: Peptide-modified phase-transition nanoparticles co-deliver FTO siRNA and Ce6 for sonodynamic metabolism-immunotherapy of melanoma

doi: 10.1186/s12951-025-03872-3

Figure Lengend Snippet: Gene silencing and glycolytic regulation of si-Ce6@tLyp-1-NPs. ( A ) Effect of UTMD in vitro ( B ) CEUS mode, n = 3 ( C ) Schematic illustration of the B16F10 cells treated with si-Ce6@tLyP-1-NPs combined with US ( D ) CLSM observation of the localization of FAM-siRNA in B16-F10 cells after transfection with free siRNA, si-Ce6@NPs(+), si-Ce6@tLyP-1-NPs (+). The scale was 10 μm, and Phalloidin was the cytoskeleton. DAPI is the nucleus. ( E ) The relative mRNA expression of FTO in different groups of B16-F10 ( F , G ) The protein expression of FTO in different groups of B16-F10. ( H ) Volcano plot of DEGs. ( I ) Heat map of genes involved in the glycolytic pathway. ( J) Representative pathways enriched in the identified genes as determined by GSEA (NES= −1.4016, p-value = 0.0424). ( K , L ) The mRNA expression levels of HK2 and PGAM1 in the control group and B16-F10 cells treated with different methods. ( M ) Representative western blot images of HK2 and PGAM1 expression in control and treated B16-F10 cell groups. ( N , O ) Quantitative analysis of HK2 and PGAM1 protein expression. ( P ) Lactate levels in cell culture medium were measured

Article Snippet: CRT antibody (IF:1:300, 27298-1), FTO antibody (WB:1:2000, IHC:1:300, 68111-1), PGAM1 antibody (WB:1:2000, 16126-1) were obtained from Proteintech (Wuhan, China).

Techniques: In Vitro, Transfection, Expressing, Control, Western Blot, Cell Culture