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R&D Systems goat antirage
Goat Antirage, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/goat antirage/product/R&D Systems
Average 93 stars, based on 1 article reviews

goat antirage - by Bioz Stars, 2026-04

93/100 stars

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SC79 induces the shedding of the RAGE ectodomain. HAECs were incubated with 10 µM SC79 for various times (5, 10, 30, and 60 min) ( n = 4) ( A ) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min ( n = 3) ( B ). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and an anti-actin antibody. To compare the size of RAGE in cell lysate and culture supernatant, untreated cell lysate (a) and conditioned media from cells treated with 10 µM SC79 for 30 min (b) were run on the same gel and immunoblotted with the RAGE antibody ( C ). The cell lysates of HAECs treated with different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min were immunoblotted with an antibody to the C-terminal domain of human RAGE and an anti-actin antibody (n = 4) ( D ). ( * p < 0.05 vs. control)

Journal: Scientific Reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: SC79 induces the shedding of the RAGE ectodomain. HAECs were incubated with 10 µM SC79 for various times (5, 10, 30, and 60 min) ( n = 4) ( A ) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min ( n = 3) ( B ). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and an anti-actin antibody. To compare the size of RAGE in cell lysate and culture supernatant, untreated cell lysate (a) and conditioned media from cells treated with 10 µM SC79 for 30 min (b) were run on the same gel and immunoblotted with the RAGE antibody ( C ). The cell lysates of HAECs treated with different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min were immunoblotted with an antibody to the C-terminal domain of human RAGE and an anti-actin antibody (n = 4) ( D ). ( * p < 0.05 vs. control)

Article Snippet: Antibodies for human RAGE (sc-80652; a mouse monoclonal antibody against a truncated extracellular domain of human RAGE), ADAM10 (sc-28358; a mouse monoclonal antibody for Western blotting), Rab14 (sc-271401; a mouse monoclonal antibody), ICAM-1 (sc-7891), and actin (sc-47778) were from Santa Cruz Biotechnology (Dallas, TX, USA).

Techniques: Incubation, Control

Inhibitors of AKT and ADAM10 diminish SC79-induced RAGE ectodomain shedding. HAECs were preincubated with or without MK-2206 (1 µM), GI 254023X (2 µM), or DMSO (vehicle) for 60 min. Following this, they were further incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and an anti-actin antibody. ( n = 3, * p < 0.05 vs. control, # p < 0.05 vs. SC79 treatment alone)

Journal: Scientific Reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: Inhibitors of AKT and ADAM10 diminish SC79-induced RAGE ectodomain shedding. HAECs were preincubated with or without MK-2206 (1 µM), GI 254023X (2 µM), or DMSO (vehicle) for 60 min. Following this, they were further incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and an anti-actin antibody. ( n = 3, * p < 0.05 vs. control, # p < 0.05 vs. SC79 treatment alone)

Techniques: Incubation, Control

AKT1 activation is required for SC79-induced RAGE ectodomain shedding. ( A ) HAECs express all three AKT isoforms, and AKT1-, AKT2-, and AKT3-siRNAs selectively deplete each AKT isoform. HAECs were transfected with AKT1-, AKT2-, AKT3-siRNAs, or control siRNAs, and the cell lysates were immunoblotted with antibodies to AKT1, AKT2, AKT3, or actin. ( n = 3, * p < 0.05 vs. control). ( B ) SC79 activates AKT1. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT1 (Ser473) and AKT1. ( n = 3, * p < 0.05 vs. control). ( C ) AKT1 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT1-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT1 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( D ) AKT1 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT1-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT1, and actin. ( n = 3, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with AKT1-siRNA)

Journal: Scientific Reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: AKT1 activation is required for SC79-induced RAGE ectodomain shedding. ( A ) HAECs express all three AKT isoforms, and AKT1-, AKT2-, and AKT3-siRNAs selectively deplete each AKT isoform. HAECs were transfected with AKT1-, AKT2-, AKT3-siRNAs, or control siRNAs, and the cell lysates were immunoblotted with antibodies to AKT1, AKT2, AKT3, or actin. ( n = 3, * p < 0.05 vs. control). ( B ) SC79 activates AKT1. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT1 (Ser473) and AKT1. ( n = 3, * p < 0.05 vs. control). ( C ) AKT1 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT1-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT1 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( D ) AKT1 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT1-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT1, and actin. ( n = 3, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with AKT1-siRNA)

Techniques: Activation Assay, Transfection, Control, Incubation, Knockdown

AKT2 activation is required for SC79-induced RAGE ectodomain shedding. ( A ) SC79 activates AKT2. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT2 (Ser474) and AKT2. ( n = 4, * p < 0.05 vs. control). ( B ) AKT2 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT2-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT2 and actin. ( n = 4, * p < 0.05 vs. control cells transfected with control siRNA). ( C ) AKT2 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT2-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT2, and actin. ( n = 3, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with AKT2-siRNA)

Journal: Scientific Reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: AKT2 activation is required for SC79-induced RAGE ectodomain shedding. ( A ) SC79 activates AKT2. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT2 (Ser474) and AKT2. ( n = 4, * p < 0.05 vs. control). ( B ) AKT2 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT2-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT2 and actin. ( n = 4, * p < 0.05 vs. control cells transfected with control siRNA). ( C ) AKT2 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT2-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT2, and actin. ( n = 3, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with AKT2-siRNA)

Techniques: Activation Assay, Incubation, Control, Knockdown, Transfection

AKT3 activation is required for SC79-induced RAGE ectodomain shedding. ( A ) SC79 activates AKT3. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT3 (Ser472) and AKT3. ( n = 3, * p < 0.05 vs. control). ( B ) AKT3 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT3-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT3 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( C ) AKT3 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT3-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT3, and actin. ( n = 3, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with AKT3-siRNA)

Journal: Scientific Reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: AKT3 activation is required for SC79-induced RAGE ectodomain shedding. ( A ) SC79 activates AKT3. HAECs were incubated with 10 µM SC79 for various times (1, 5, 10, and 30 min) (upper panel) or different concentrations of SC79 (0.1, 1, 5, and 10 µM) for 30 min (lower panel). The cell lysates were immunoblotted with antibodies to p-AKT3 (Ser472) and AKT3. ( n = 3, * p < 0.05 vs. control). ( B ) AKT3 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with AKT3-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to AKT3 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( C ) AKT3 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with AKT3-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, AKT3, and actin. ( n = 3, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with AKT3-siRNA)

Techniques: Activation Assay, Incubation, Control, Knockdown, Transfection

SC79 induces RAGE ectodomain shedding by promoting ADAM10 cell surface translocation. ( A ) Immunofluorescence staining to evaluate the effect of SC79 on ADAM10 localization. HAECs grown in culture dishes with a coverslip were treated with SC79 (10 µM) for 10–120 min. (a) The cells on the coverslip were fixed for 10 min with 4% paraformaldehyde without permeabilization, then immunostained with an antibody to an extracellular portion of ADAM10 and examined using confocal microscopy. DAPI was used to label the nuclei of the cells. Representative photos and the relative fluorescence intensities are shown (scale bar: 100 μm). (b) Cell lysates from cells that were not on the coverslip in the same culture plate were immunoblotted with antibodies to ADAM10 and actin. ( n = 3, * p < 0.05 vs. control). ( B ) ADAM10 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with ADAM10-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to ADAM10 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( C ) ADAM10 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with ADAM10-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, ADAM10, and actin. ( n = 3, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with ADAM10-siRNA)

Journal: Scientific Reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: SC79 induces RAGE ectodomain shedding by promoting ADAM10 cell surface translocation. ( A ) Immunofluorescence staining to evaluate the effect of SC79 on ADAM10 localization. HAECs grown in culture dishes with a coverslip were treated with SC79 (10 µM) for 10–120 min. (a) The cells on the coverslip were fixed for 10 min with 4% paraformaldehyde without permeabilization, then immunostained with an antibody to an extracellular portion of ADAM10 and examined using confocal microscopy. DAPI was used to label the nuclei of the cells. Representative photos and the relative fluorescence intensities are shown (scale bar: 100 μm). (b) Cell lysates from cells that were not on the coverslip in the same culture plate were immunoblotted with antibodies to ADAM10 and actin. ( n = 3, * p < 0.05 vs. control). ( B ) ADAM10 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with ADAM10-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to ADAM10 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( C ) ADAM10 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with ADAM10-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, ADAM10, and actin. ( n = 3, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with ADAM10-siRNA)

Techniques: Translocation Assay, Immunofluorescence, Staining, Confocal Microscopy, Fluorescence, Control, Knockdown, Transfection, Incubation

Rab14 is required for SC79-induced ADAM10 cell surface translocation. ( A ) Rab14 knockdown prevents SC79-induced ADAM10 cell surface translocation. HAECs grown in culture dishes with a coverslip were transfected with Rab14-siRNA or control siRNA and then incubated for 20 min with DMSO or SC79 (10 µM). (a) Cells grown on the coverslip were immunostained with an antibody to an extracellular portion of ADAM10. Representative photos and the relative fluorescence intensities are shown (scale bar: 100 μm). (b) Cell lysates from cells that were not on the coverslip in the same culture plate were immunoblotted with antibodies to Rab14 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( B ) Rab14 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with Rab14-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to Rab14 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( C ) Rab14 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with Rab14-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, Rab14, and actin. ( n = 4, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with Rab14-siRNA)

Journal: Scientific Reports

Article Title: AKT activation triggers Rab14-mediated ADAM10 translocation to the cell surface in human aortic endothelial cells

doi: 10.1038/s41598-025-90624-w

Figure Lengend Snippet: Rab14 is required for SC79-induced ADAM10 cell surface translocation. ( A ) Rab14 knockdown prevents SC79-induced ADAM10 cell surface translocation. HAECs grown in culture dishes with a coverslip were transfected with Rab14-siRNA or control siRNA and then incubated for 20 min with DMSO or SC79 (10 µM). (a) Cells grown on the coverslip were immunostained with an antibody to an extracellular portion of ADAM10. Representative photos and the relative fluorescence intensities are shown (scale bar: 100 μm). (b) Cell lysates from cells that were not on the coverslip in the same culture plate were immunoblotted with antibodies to Rab14 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( B ) Rab14 knockdown inhibits SC79-induced RAGE ectodomain shedding. HAECs were transfected with Rab14-siRNA or control siRNA and then incubated for 30 min with or without SC79 (10 µM). The cell lysate and culture supernatant were immunoblotted with a monoclonal antibody to the extracellular domain of human RAGE and antibodies to Rab14 and actin. ( n = 3, * p < 0.05 vs. control cells transfected with control siRNA). ( C ) Rab14 knockdown abolishes SC79’s inhibitory effect against AGE-BSA. HAECs transfected with Rab14-siRNA or control siRNA were treated for 30 min with or without SC79 (10 µM). The cells were then treated with AGE-BSA (100 µg/ml) for 24 h. The cell lysates were immunoblotted with antibodies to ICAM-1, Rab14, and actin. ( n = 4, * p < 0.05 vs. control; # p < 0.05 vs. AGE-BSA; † p < 0.05 vs. control cells transfected with Rab14-siRNA)

Techniques: Translocation Assay, Knockdown, Transfection, Control, Incubation, Fluorescence

Protective effect of MD on AGEs-induced osteoblasts. (A) Effect of MD on the survival rate of osteoblasts (n = 6); (B) ALP activity in osteoblasts (n = 6); (C) Western blotting results of OCN and RUNX2 in osteoblasts (n = 3). * P < 0.05; ** P < 0.01.

Journal: Frontiers in Pharmacology

Article Title: Screening of active components of melastoma dodecandrum lour. against diabetic osteoporosis using cell membrane chromatography-mass spectrometry

doi: 10.3389/fphar.2024.1450154

Figure Lengend Snippet: Protective effect of MD on AGEs-induced osteoblasts. (A) Effect of MD on the survival rate of osteoblasts (n = 6); (B) ALP activity in osteoblasts (n = 6); (C) Western blotting results of OCN and RUNX2 in osteoblasts (n = 3). * P < 0.05; ** P < 0.01.

Article Snippet: Proteins were separated by electrophoresis, transferred to PVDF membranes, and blocked for 2 h. The membranes were incubated overnight at 4°C with primary antibodies against OCN (#DF12303, Affinity Biosciences, 1:2000), RUNX2 (#PB0171, Bosterbio, 1:2000), RAGE (#BM4901, Bosterbio, 1:2000), and GAPDH (#BM3874, Bosterbio, 1:2000).

Techniques: Activity Assay, Western Blot

Protective effect of isovitexin on AGEs-induced osteoblasts. (A) Effect of isovitexin on the survival rate of osteoblasts (n = 6); (B) ALP activity in osteoblasts (n = 6); (C) Western blotting results of OCN and RUNX2 in osteoblasts (n = 3). ** P < 0.01.

Journal: Frontiers in Pharmacology

Article Title: Screening of active components of melastoma dodecandrum lour. against diabetic osteoporosis using cell membrane chromatography-mass spectrometry

doi: 10.3389/fphar.2024.1450154

Figure Lengend Snippet: Protective effect of isovitexin on AGEs-induced osteoblasts. (A) Effect of isovitexin on the survival rate of osteoblasts (n = 6); (B) ALP activity in osteoblasts (n = 6); (C) Western blotting results of OCN and RUNX2 in osteoblasts (n = 3). ** P < 0.01.

Techniques: Activity Assay, Western Blot

Contains a summary of the Primer Sequence List.

Journal: Frontiers in Pharmacology

Article Title: Lentivirus-mediated RNA interference targeting HMGB1 modulates AQP1 to reduce pain induced by chronic compression of the dorsal root ganglia

doi: 10.3389/fphar.2024.1469223

Figure Lengend Snippet: Contains a summary of the Primer Sequence List.

Article Snippet: The following primary antibodies were used: rabbit anti-HMGB1 antibody (20 μg, CUSABIO), rabbit anti-AQP1 antibody (20 μL, BOSTER BIOLOGICAL TECHNOLOGY), rabbit anti-RAGE antibody (10 μL, MedChemExpress), rabbit anti-GAPDH antibody (100 μL, BOSTER) and mouse anti-TLR4 antibody (20 μL, proteintech).

Techniques: Sequencing

Immunoprecipitation determinations of HMGB1 and AQP1 (A) Western blots of HMGB1 in plasmids. (B) Western blots of AQP1 in plasmids. (C) CO-IP assay results. 293T: 293T-null cells; 293T-E5061-E5077: 293T- E5061 HA empty control plasmid transfection- E5077 negative control CON238 plasmid; 293T-E5062-E5078: 293T- E5062 HA-Aqp1 overexpression plasmid transfection- E5078 Hmgb1-3flag overexpression plasmid. Flag: HMGB1; HA:AQP1.

Journal: Frontiers in Pharmacology

Article Title: Lentivirus-mediated RNA interference targeting HMGB1 modulates AQP1 to reduce pain induced by chronic compression of the dorsal root ganglia

doi: 10.3389/fphar.2024.1469223

Figure Lengend Snippet: Immunoprecipitation determinations of HMGB1 and AQP1 (A) Western blots of HMGB1 in plasmids. (B) Western blots of AQP1 in plasmids. (C) CO-IP assay results. 293T: 293T-null cells; 293T-E5061-E5077: 293T- E5061 HA empty control plasmid transfection- E5077 negative control CON238 plasmid; 293T-E5062-E5078: 293T- E5062 HA-Aqp1 overexpression plasmid transfection- E5078 Hmgb1-3flag overexpression plasmid. Flag: HMGB1; HA:AQP1.

Techniques: Immunoprecipitation, Western Blot, Co-Immunoprecipitation Assay, Control, Plasmid Preparation, Transfection, Negative Control, Over Expression

Changes in AQP1 expression after HMGB1 knockdown (A) Protein expression levels of HMGB1 and AQP1 in the spinal cords of rats in each group. (B) Protein expression levels of HMGB1 and AQP1 in the LPS inflammatory cell model in each group. (C) mRNA levels of HMGB1 and AQP1 in the spinal cords of rats in each group. (D) mRNA levels of HMGB1 and AQP1 in the LPS inflammatory cell model in each group. N = 3 per group **** p < 0.0001 *** p < 0.001 ** p < 0.01* p < 0.05.

Journal: Frontiers in Pharmacology

Article Title: Lentivirus-mediated RNA interference targeting HMGB1 modulates AQP1 to reduce pain induced by chronic compression of the dorsal root ganglia

doi: 10.3389/fphar.2024.1469223

Figure Lengend Snippet: Changes in AQP1 expression after HMGB1 knockdown (A) Protein expression levels of HMGB1 and AQP1 in the spinal cords of rats in each group. (B) Protein expression levels of HMGB1 and AQP1 in the LPS inflammatory cell model in each group. (C) mRNA levels of HMGB1 and AQP1 in the spinal cords of rats in each group. (D) mRNA levels of HMGB1 and AQP1 in the LPS inflammatory cell model in each group. N = 3 per group **** p < 0.0001 *** p < 0.001 ** p < 0.01* p < 0.05.

Techniques: Expressing, Knockdown

Changes in AQP1 expression after TAK-242 and FPS-ZM1 treatments (A) Protein expression levels of TLR4 and AQP1 in the spinal cords of rats in each group. (B) Protein expression levels of TLR4 and AQP1 in the LPS inflammatory cell model in each group. (C) Protein expression levels of RAGE and AQP1 in the spinal cords of rats in each group. (D) Protein expression levels of RAGE and AQP1 in the LPS inflammatory cell model in each group. (E) mRNA levels of TLR4 and AQP1 in each group. (F) mRNA levels of RAGE and AQP1 in each group. N = 3 per group **** p < 0.0001 *** p < 0.001 ** p < 0.01* p < 0.05.

Journal: Frontiers in Pharmacology

Article Title: Lentivirus-mediated RNA interference targeting HMGB1 modulates AQP1 to reduce pain induced by chronic compression of the dorsal root ganglia

doi: 10.3389/fphar.2024.1469223

Figure Lengend Snippet: Changes in AQP1 expression after TAK-242 and FPS-ZM1 treatments (A) Protein expression levels of TLR4 and AQP1 in the spinal cords of rats in each group. (B) Protein expression levels of TLR4 and AQP1 in the LPS inflammatory cell model in each group. (C) Protein expression levels of RAGE and AQP1 in the spinal cords of rats in each group. (D) Protein expression levels of RAGE and AQP1 in the LPS inflammatory cell model in each group. (E) mRNA levels of TLR4 and AQP1 in each group. (F) mRNA levels of RAGE and AQP1 in each group. N = 3 per group **** p < 0.0001 *** p < 0.001 ** p < 0.01* p < 0.05.

Techniques: Expressing

Changes in NF-κB expression following knockdown of HMGB1 or AQP1 (A) Protein expression levels of HMGB1 and NF-κB in the spinal cords of rats in each group. (B) mRNA levels of HMGB1 and NF-κB in the spinal cords of rats in each group. (C) Protein expression levels of AQP1 and NF-κB in the spinal cords of rats in each group. (D) mRNA levels of AQP1 and NF-κB in the spinal cords of rats in each group. (E) Protein expression levels of NF-κB and AQP1 in the LPS inflammatory cell model in each group. (F) mRNA levels of NF-κB and AQP1 in the LPS inflammatory cell model in each group. N = 3 per group **** p < 0.0001 *** p < 0.001 ** p < 0.01* p < 0.05.

Journal: Frontiers in Pharmacology

Article Title: Lentivirus-mediated RNA interference targeting HMGB1 modulates AQP1 to reduce pain induced by chronic compression of the dorsal root ganglia

doi: 10.3389/fphar.2024.1469223

Figure Lengend Snippet: Changes in NF-κB expression following knockdown of HMGB1 or AQP1 (A) Protein expression levels of HMGB1 and NF-κB in the spinal cords of rats in each group. (B) mRNA levels of HMGB1 and NF-κB in the spinal cords of rats in each group. (C) Protein expression levels of AQP1 and NF-κB in the spinal cords of rats in each group. (D) mRNA levels of AQP1 and NF-κB in the spinal cords of rats in each group. (E) Protein expression levels of NF-κB and AQP1 in the LPS inflammatory cell model in each group. (F) mRNA levels of NF-κB and AQP1 in the LPS inflammatory cell model in each group. N = 3 per group **** p < 0.0001 *** p < 0.001 ** p < 0.01* p < 0.05.

Techniques: Expressing, Knockdown

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