fgfr1 antibody Search Results


92
R&D Systems mouse anti fgfr1
Mouse Anti Fgfr1, supplied by R&D Systems, 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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Novus Biologicals fgfr1 mouse monoclonal m19b2
A) Heatmap showing expression of <t>FGFR1/3</t> and FGF2/9 across a panel of cell lines derived from MCL, ABC-DLBCL, and germinal center B-cell (GCB) DLBCL; heatmap is based on log2 CPM (counts per million). The scale ranges from low (-4, blue) to high (+4, red). Each horizontal represents the values for one cell line. B) Immunoblot for <t>FGFR1</t> <t>protein</t> in a subset of selected cell lines and C) its protein quantification expressed as a ratio to SP53; data is the average with the second replicate shown in Supplementary Figure 1.
Fgfr1 Mouse Monoclonal M19b2, 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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94
Proteintech mouse anti fgfr1
A) Heatmap showing expression of <t>FGFR1/3</t> and FGF2/9 across a panel of cell lines derived from MCL, ABC-DLBCL, and germinal center B-cell (GCB) DLBCL; heatmap is based on log2 CPM (counts per million). The scale ranges from low (-4, blue) to high (+4, red). Each horizontal represents the values for one cell line. B) Immunoblot for <t>FGFR1</t> <t>protein</t> in a subset of selected cell lines and C) its protein quantification expressed as a ratio to SP53; data is the average with the second replicate shown in Supplementary Figure 1.
Mouse Anti Fgfr1, 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
https://www.bioz.com/product/fgfr1+antibody/FGFR1+Antibody/pmc10160558-75-65-68
Average 94 stars, based on 1 article reviews
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92
R&D Systems anti p fgfr2 antibody
A) Heatmap showing expression of <t>FGFR1/3</t> and FGF2/9 across a panel of cell lines derived from MCL, ABC-DLBCL, and germinal center B-cell (GCB) DLBCL; heatmap is based on log2 CPM (counts per million). The scale ranges from low (-4, blue) to high (+4, red). Each horizontal represents the values for one cell line. B) Immunoblot for <t>FGFR1</t> <t>protein</t> in a subset of selected cell lines and C) its protein quantification expressed as a ratio to SP53; data is the average with the second replicate shown in Supplementary Figure 1.
Anti P Fgfr2 Antibody, supplied by R&D Systems, 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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R&D Systems anti fgfr1 mab
FGFR, <t> Fibroblast Growth Factor Receptor </t>
Anti Fgfr1 Mab, supplied by R&D Systems, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
R&D Systems human neutralizing fgfr1 mab765
Figure 1: Proximity between apelin and <t>FGFR1</t> suppresses the TGFβ/Smad signaling pathway in HMVECs. (a) HMVECs were treated with TGFβ2 (5 ng/mL) or N-FGFR1 (1.5 μg/mL) for 48 h with or without preincubation with apelin (100 nM) for 2 h. The proximity between apelin and FGFR1 was then analyzed by the Duolink In Situ Assay. For each slide, images at a ×400 original magnification were obtained from six different areas. The scale bar is 60 μm in each panel. (b) HMVECs were treated with TGFβ2 (5 ng/mL) or with apelin (100 nM) for 48 h, and the p-Smad3, TGFβR1, TGFβR2, and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-Smad3/Smad3, TGFβR1/β-actin, TGFβR2/β-actin, and FGFR1/β-actin levels from each group (n = 5) was analyzed. (c) HMVECs were treated with or without apelin (100 nM) for 48 h, and the FGFR1 levels were analyzed by western blot. Densitometric analysis of the FGFR1/GADPH levels from each group (n = 5) was analyzed.
Human Neutralizing Fgfr1 Mab765, 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/product/fgfr1+antibody/Human+FGFR1+(IIIb)+Antibody/pm36785790-42-0-7
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94
R&D Systems monoclonal anti fgfr1 antibody
Figure 1: Proximity between apelin and <t>FGFR1</t> suppresses the TGFβ/Smad signaling pathway in HMVECs. (a) HMVECs were treated with TGFβ2 (5 ng/mL) or N-FGFR1 (1.5 μg/mL) for 48 h with or without preincubation with apelin (100 nM) for 2 h. The proximity between apelin and FGFR1 was then analyzed by the Duolink In Situ Assay. For each slide, images at a ×400 original magnification were obtained from six different areas. The scale bar is 60 μm in each panel. (b) HMVECs were treated with TGFβ2 (5 ng/mL) or with apelin (100 nM) for 48 h, and the p-Smad3, TGFβR1, TGFβR2, and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-Smad3/Smad3, TGFβR1/β-actin, TGFβR2/β-actin, and FGFR1/β-actin levels from each group (n = 5) was analyzed. (c) HMVECs were treated with or without apelin (100 nM) for 48 h, and the FGFR1 levels were analyzed by western blot. Densitometric analysis of the FGFR1/GADPH levels from each group (n = 5) was analyzed.
Monoclonal Anti Fgfr1 Antibody, supplied by R&D Systems, 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/product/fgfr1+antibody/Human+FGFR1+Antibody/pmc03308836-213-18-22
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93
Proteintech nb600
Figure 1: Proximity between apelin and <t>FGFR1</t> suppresses the TGFβ/Smad signaling pathway in HMVECs. (a) HMVECs were treated with TGFβ2 (5 ng/mL) or N-FGFR1 (1.5 μg/mL) for 48 h with or without preincubation with apelin (100 nM) for 2 h. The proximity between apelin and FGFR1 was then analyzed by the Duolink In Situ Assay. For each slide, images at a ×400 original magnification were obtained from six different areas. The scale bar is 60 μm in each panel. (b) HMVECs were treated with TGFβ2 (5 ng/mL) or with apelin (100 nM) for 48 h, and the p-Smad3, TGFβR1, TGFβR2, and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-Smad3/Smad3, TGFβR1/β-actin, TGFβR2/β-actin, and FGFR1/β-actin levels from each group (n = 5) was analyzed. (c) HMVECs were treated with or without apelin (100 nM) for 48 h, and the FGFR1 levels were analyzed by western blot. Densitometric analysis of the FGFR1/GADPH levels from each group (n = 5) was analyzed.
Nb600, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fgfr1+antibody/FGFR1OP+Antibody/pm33932338-654-82-86
Average 93 stars, based on 1 article reviews
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90
Novus Biologicals fgfr1 antibody
Figure 1: Proximity between apelin and <t>FGFR1</t> suppresses the TGFβ/Smad signaling pathway in HMVECs. (a) HMVECs were treated with TGFβ2 (5 ng/mL) or N-FGFR1 (1.5 μg/mL) for 48 h with or without preincubation with apelin (100 nM) for 2 h. The proximity between apelin and FGFR1 was then analyzed by the Duolink In Situ Assay. For each slide, images at a ×400 original magnification were obtained from six different areas. The scale bar is 60 μm in each panel. (b) HMVECs were treated with TGFβ2 (5 ng/mL) or with apelin (100 nM) for 48 h, and the p-Smad3, TGFβR1, TGFβR2, and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-Smad3/Smad3, TGFβR1/β-actin, TGFβR2/β-actin, and FGFR1/β-actin levels from each group (n = 5) was analyzed. (c) HMVECs were treated with or without apelin (100 nM) for 48 h, and the FGFR1 levels were analyzed by western blot. Densitometric analysis of the FGFR1/GADPH levels from each group (n = 5) was analyzed.
Fgfr1 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
https://www.bioz.com/product/fgfr1+antibody/FGFR1+Antibody/pm35236856-229-12-14
Average 90 stars, based on 1 article reviews
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OriGene fgfr1 antibody
Figure 1: Proximity between apelin and <t>FGFR1</t> suppresses the TGFβ/Smad signaling pathway in HMVECs. (a) HMVECs were treated with TGFβ2 (5 ng/mL) or N-FGFR1 (1.5 μg/mL) for 48 h with or without preincubation with apelin (100 nM) for 2 h. The proximity between apelin and FGFR1 was then analyzed by the Duolink In Situ Assay. For each slide, images at a ×400 original magnification were obtained from six different areas. The scale bar is 60 μm in each panel. (b) HMVECs were treated with TGFβ2 (5 ng/mL) or with apelin (100 nM) for 48 h, and the p-Smad3, TGFβR1, TGFβR2, and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-Smad3/Smad3, TGFβR1/β-actin, TGFβR2/β-actin, and FGFR1/β-actin levels from each group (n = 5) was analyzed. (c) HMVECs were treated with or without apelin (100 nM) for 48 h, and the FGFR1 levels were analyzed by western blot. Densitometric analysis of the FGFR1/GADPH levels from each group (n = 5) was analyzed.
Fgfr1 Antibody, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fgfr1+antibody/FGFR1+Rabbit+Polyclonal+Antibody/10__1158_slash_0008___5472__can___17___0109-64-32-38
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94
R&D Systems polyclonal p fgfr2
Figure 1: Proximity between apelin and <t>FGFR1</t> suppresses the TGFβ/Smad signaling pathway in HMVECs. (a) HMVECs were treated with TGFβ2 (5 ng/mL) or N-FGFR1 (1.5 μg/mL) for 48 h with or without preincubation with apelin (100 nM) for 2 h. The proximity between apelin and FGFR1 was then analyzed by the Duolink In Situ Assay. For each slide, images at a ×400 original magnification were obtained from six different areas. The scale bar is 60 μm in each panel. (b) HMVECs were treated with TGFβ2 (5 ng/mL) or with apelin (100 nM) for 48 h, and the p-Smad3, TGFβR1, TGFβR2, and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-Smad3/Smad3, TGFβR1/β-actin, TGFβR2/β-actin, and FGFR1/β-actin levels from each group (n = 5) was analyzed. (c) HMVECs were treated with or without apelin (100 nM) for 48 h, and the FGFR1 levels were analyzed by western blot. Densitometric analysis of the FGFR1/GADPH levels from each group (n = 5) was analyzed.
Polyclonal P Fgfr2, supplied by R&D Systems, 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/product/fgfr1+antibody/Human+Phospho-FGFR1-4+(Y653%2FY654)+Antibody/pmc04579967-47-40-46
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90
OriGene fgfr1
Figure 4. bFGF and <t>FGFR1</t> analysis. (A) bFGF (left) and FGFR1 (right) analysis by Western Blot. Statistical analysis was performed by one-way ANOVA test followed by Tukey test. Data are shown as mean ± SE (n = 4). *p < 0,05; **p < 0,01; ***p < 0,001 versus Control. #p < 0,05; ##p < 0,01; ###p < 0,001 versus LD. Original western blots presented are available in Supplementary Fig. S3. (B) Representative confocal images of retinal cryosections immunolabelled for bFGF (green) and FGFR1 (red). Nuclei were stained with Bisbenzimide (blue). (a–e) High magnification of a random area of the sections showing co-localization in yellow (white arrows) of bFGF and FGFR1. Both bFGF and FGFR1 increased in the rat retina after light damage over time. CTRL (Control); LD (Light damage); LD + 7rec (Light damage + 7 days of recovery); LD + 60rec (Light damage + 60 days of recovery); LD + 120rec (Light damage + 120 days of recovery); ONL (Outer nuclear layer); INL (Inner nuclear layer); GCL (Ganglion cell layer).
Fgfr1, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fgfr1+antibody/FGFR1+Rabbit+Polyclonal+Antibody/pm32286488-331-37-38
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Image Search Results


A) Heatmap showing expression of FGFR1/3 and FGF2/9 across a panel of cell lines derived from MCL, ABC-DLBCL, and germinal center B-cell (GCB) DLBCL; heatmap is based on log2 CPM (counts per million). The scale ranges from low (-4, blue) to high (+4, red). Each horizontal represents the values for one cell line. B) Immunoblot for FGFR1 protein in a subset of selected cell lines and C) its protein quantification expressed as a ratio to SP53; data is the average with the second replicate shown in Supplementary Figure 1.

Journal: bioRxiv

Article Title: Targeting Aberrant FGFR Signaling with Infigratinib Enhances the Efficacy of BTK/PI3K Inhibitors and Bendamustine in Lymphoma Cells

doi: 10.64898/2025.12.23.695986

Figure Lengend Snippet: A) Heatmap showing expression of FGFR1/3 and FGF2/9 across a panel of cell lines derived from MCL, ABC-DLBCL, and germinal center B-cell (GCB) DLBCL; heatmap is based on log2 CPM (counts per million). The scale ranges from low (-4, blue) to high (+4, red). Each horizontal represents the values for one cell line. B) Immunoblot for FGFR1 protein in a subset of selected cell lines and C) its protein quantification expressed as a ratio to SP53; data is the average with the second replicate shown in Supplementary Figure 1.

Article Snippet: The following primary antibodies were used in TBST 5% BSA buffer: FGFR1 mouse monoclonal (M19B2) (NB600-1287, Novus),Bek/FGFR2 mouse monoclonal (C-8) (sc-6930, Santa Cruz), FGFR3 mouse monoclonal (MAB766-100, ReD) and FGFR-4 mouse monoclonal (A-10) (sc-136988, Santa Cruz).

Techniques: Expressing, Derivative Assay, Western Blot

FGFR,  Fibroblast Growth Factor Receptor

Journal: Investigative Ophthalmology & Visual Science

Article Title: Goblet Cell Differentiation Potential in Human Corneal Limbal Epithelial Progenitor Cells In Vitro

doi: 10.1167/iovs.61.12.27

Figure Lengend Snippet: FGFR, Fibroblast Growth Factor Receptor

Article Snippet: The following Abs were used: mouse anti-cytokeratin-3/2p monoclonal antibody (mAb; AE-5, 1:100; Santa Cruz Biotechnology, Inc, Dallas, TX, USA), mouse anti-human cytokeratin-4 mAb (6B10, 1:300; Abcam, Cambridge, UK), rabbit monoclonal [EP1599Y] anti-human cytokeratin 4 (1:200, Abcam), mouse anti-human cytokeratin-7 mAb (RCK105, 1:10000; Millipore, Billerica, MA, USA), mouse anti-human cytokeratin-13 mAb (1:20; American Research Products, Inc., Palos Verdes, CA, USA), mouse anti-human cytokeratin-12 mAb (N-16; 1:500; Santa Cruz Biotechnology), rabbit anti-cytokeratin 12/K12 mAb (1:200, EPR17882, Abcam), rabbit anti-human MUC5AC polyclonal Ab (H-160, 1:100, Santa Cruz Biotechnology), anti-FGFR1 mAb (1:200, 133105; R&D Systems, Minneapolis, MN, USA), anti-human FGFR2 (blocking) mAb (1:200, 98725; R&D Systems), anti-FGFR3 mAb (1:200, 135334; R&D Systems), anti-FGFR4 mAb (1:200, 137114; R&D Systems), and anti-FGFR1 blocking mAb (VBS1; Chemicon, Temecula, CA, USA).

Techniques:

FGF receptor expression and effect of FGF receptor blockade in colonies derived from adherent single cells. ( A ) FGFR1 and FGFR2, but not FGFR3 and FGFR4, are detected in the adherent colonies by RT-PCR. ( B ) FGFR1 and FGFR2 expression is detected by Western blotting. ( C ) Effect of FGF receptor blockade was tested in colonies derived from adherent single cells. PAS-positive colony number in the anti-FGFR1 monoclonal antibody group significantly decreases as compared with that in the control Ig group. Treatment with an anti-FGFR2 blocking mAb does not affect the number of colony. ( D ) Colony with amorphous material and epithelium is observed with control IgG. ( E ) Anti-FGFR1 mAb suppresses the proliferation of both goblet-like cell and epithelium. Similar results were obtained with repeated three experiments. M, size markers; S, sample; P, positive control; N, negative control, N.S., not significant.

Journal: Investigative Ophthalmology & Visual Science

Article Title: Goblet Cell Differentiation Potential in Human Corneal Limbal Epithelial Progenitor Cells In Vitro

doi: 10.1167/iovs.61.12.27

Figure Lengend Snippet: FGF receptor expression and effect of FGF receptor blockade in colonies derived from adherent single cells. ( A ) FGFR1 and FGFR2, but not FGFR3 and FGFR4, are detected in the adherent colonies by RT-PCR. ( B ) FGFR1 and FGFR2 expression is detected by Western blotting. ( C ) Effect of FGF receptor blockade was tested in colonies derived from adherent single cells. PAS-positive colony number in the anti-FGFR1 monoclonal antibody group significantly decreases as compared with that in the control Ig group. Treatment with an anti-FGFR2 blocking mAb does not affect the number of colony. ( D ) Colony with amorphous material and epithelium is observed with control IgG. ( E ) Anti-FGFR1 mAb suppresses the proliferation of both goblet-like cell and epithelium. Similar results were obtained with repeated three experiments. M, size markers; S, sample; P, positive control; N, negative control, N.S., not significant.

Article Snippet: The following Abs were used: mouse anti-cytokeratin-3/2p monoclonal antibody (mAb; AE-5, 1:100; Santa Cruz Biotechnology, Inc, Dallas, TX, USA), mouse anti-human cytokeratin-4 mAb (6B10, 1:300; Abcam, Cambridge, UK), rabbit monoclonal [EP1599Y] anti-human cytokeratin 4 (1:200, Abcam), mouse anti-human cytokeratin-7 mAb (RCK105, 1:10000; Millipore, Billerica, MA, USA), mouse anti-human cytokeratin-13 mAb (1:20; American Research Products, Inc., Palos Verdes, CA, USA), mouse anti-human cytokeratin-12 mAb (N-16; 1:500; Santa Cruz Biotechnology), rabbit anti-cytokeratin 12/K12 mAb (1:200, EPR17882, Abcam), rabbit anti-human MUC5AC polyclonal Ab (H-160, 1:100, Santa Cruz Biotechnology), anti-FGFR1 mAb (1:200, 133105; R&D Systems, Minneapolis, MN, USA), anti-human FGFR2 (blocking) mAb (1:200, 98725; R&D Systems), anti-FGFR3 mAb (1:200, 135334; R&D Systems), anti-FGFR4 mAb (1:200, 137114; R&D Systems), and anti-FGFR1 blocking mAb (VBS1; Chemicon, Temecula, CA, USA).

Techniques: Expressing, Derivative Assay, Reverse Transcription Polymerase Chain Reaction, Western Blot, Control, Blocking Assay, Positive Control, Negative Control

Figure 1: Proximity between apelin and FGFR1 suppresses the TGFβ/Smad signaling pathway in HMVECs. (a) HMVECs were treated with TGFβ2 (5 ng/mL) or N-FGFR1 (1.5 μg/mL) for 48 h with or without preincubation with apelin (100 nM) for 2 h. The proximity between apelin and FGFR1 was then analyzed by the Duolink In Situ Assay. For each slide, images at a ×400 original magnification were obtained from six different areas. The scale bar is 60 μm in each panel. (b) HMVECs were treated with TGFβ2 (5 ng/mL) or with apelin (100 nM) for 48 h, and the p-Smad3, TGFβR1, TGFβR2, and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-Smad3/Smad3, TGFβR1/β-actin, TGFβR2/β-actin, and FGFR1/β-actin levels from each group (n = 5) was analyzed. (c) HMVECs were treated with or without apelin (100 nM) for 48 h, and the FGFR1 levels were analyzed by western blot. Densitometric analysis of the FGFR1/GADPH levels from each group (n = 5) was analyzed.

Journal: Oxidative medicine and cellular longevity

Article Title: The Interaction of Apelin and FGFR1 Ameliorated the Kidney Fibrosis through Suppression of TGF β -Induced Endothelial-to-Mesenchymal Transition.

doi: 10.1155/2023/5012474

Figure Lengend Snippet: Figure 1: Proximity between apelin and FGFR1 suppresses the TGFβ/Smad signaling pathway in HMVECs. (a) HMVECs were treated with TGFβ2 (5 ng/mL) or N-FGFR1 (1.5 μg/mL) for 48 h with or without preincubation with apelin (100 nM) for 2 h. The proximity between apelin and FGFR1 was then analyzed by the Duolink In Situ Assay. For each slide, images at a ×400 original magnification were obtained from six different areas. The scale bar is 60 μm in each panel. (b) HMVECs were treated with TGFβ2 (5 ng/mL) or with apelin (100 nM) for 48 h, and the p-Smad3, TGFβR1, TGFβR2, and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-Smad3/Smad3, TGFβR1/β-actin, TGFβR2/β-actin, and FGFR1/β-actin levels from each group (n = 5) was analyzed. (c) HMVECs were treated with or without apelin (100 nM) for 48 h, and the FGFR1 levels were analyzed by western blot. Densitometric analysis of the FGFR1/GADPH levels from each group (n = 5) was analyzed.

Article Snippet: Human neutralizing FGFR1 (MAB765) was obtained from R&D Systems (Minneapolis, MN, USA).

Techniques: In Situ, Western Blot

Figure 4: CEBPA knockdown promotes TGFβ-mediated EndMT. (a) HMVECs were transfected with or without CEBPA siRNA for 48 h in the presence or absence of TGFβ2, and the VE-cadherin, α-SMA, vimentin, and SM22α levels were analyzed by western blot. Densitometric analysis of the VE-cadherin/GADPH, α-SMA/GADPH, vimentin/GADPH, and SM22α/GADPH levels from each group (n = 5) was analyzed. (b) HMVECs were transfected with CEBPA siRNA for 48 h in the presence or absence of TGFβ2 and apelin, and the VE- cadherin, α-SMA, vimentin, and SM22α levels were analyzed by western blot. Densitometric analysis of the VE-cadherin/GADPH, α- SMA/GADPH, vimentin/GADPH, and SM22α/GADPH levels from each group (n = 5) was analyzed. (c) HMVECs were treated with TGFβ2 for 15 min or 48 h with or without preincubation with apelin for 2 h, and the CEBPA levels were analyzed by western blot. Densitometric analysis of the CEBPA/GADPH level from each group (n = 5) was analyzed. (d) HMVECs were treated with N-FGFR1 for 48 h or 15 min in the presence or absence of apelin, and the CEBPA levels was analyzed by western blot. Densitometric analysis of the CEBPA/GADPH level from each group (n = 5) was analyzed. Immunofluorescence analysis of CD31 (e) and α-SMA (f) coexpression in HUVECs following TGFβ2 or/and apelin or/and CEBPA siRNA treatment. For each slide, images of six different fields of view at ×200 magnification were evaluated. The scale bar is 50 μm in each panel.

Journal: Oxidative medicine and cellular longevity

Article Title: The Interaction of Apelin and FGFR1 Ameliorated the Kidney Fibrosis through Suppression of TGF β -Induced Endothelial-to-Mesenchymal Transition.

doi: 10.1155/2023/5012474

Figure Lengend Snippet: Figure 4: CEBPA knockdown promotes TGFβ-mediated EndMT. (a) HMVECs were transfected with or without CEBPA siRNA for 48 h in the presence or absence of TGFβ2, and the VE-cadherin, α-SMA, vimentin, and SM22α levels were analyzed by western blot. Densitometric analysis of the VE-cadherin/GADPH, α-SMA/GADPH, vimentin/GADPH, and SM22α/GADPH levels from each group (n = 5) was analyzed. (b) HMVECs were transfected with CEBPA siRNA for 48 h in the presence or absence of TGFβ2 and apelin, and the VE- cadherin, α-SMA, vimentin, and SM22α levels were analyzed by western blot. Densitometric analysis of the VE-cadherin/GADPH, α- SMA/GADPH, vimentin/GADPH, and SM22α/GADPH levels from each group (n = 5) was analyzed. (c) HMVECs were treated with TGFβ2 for 15 min or 48 h with or without preincubation with apelin for 2 h, and the CEBPA levels were analyzed by western blot. Densitometric analysis of the CEBPA/GADPH level from each group (n = 5) was analyzed. (d) HMVECs were treated with N-FGFR1 for 48 h or 15 min in the presence or absence of apelin, and the CEBPA levels was analyzed by western blot. Densitometric analysis of the CEBPA/GADPH level from each group (n = 5) was analyzed. Immunofluorescence analysis of CD31 (e) and α-SMA (f) coexpression in HUVECs following TGFβ2 or/and apelin or/and CEBPA siRNA treatment. For each slide, images of six different fields of view at ×200 magnification were evaluated. The scale bar is 50 μm in each panel.

Article Snippet: Human neutralizing FGFR1 (MAB765) was obtained from R&D Systems (Minneapolis, MN, USA).

Techniques: Knockdown, Transfection, Western Blot

Figure 4. bFGF and FGFR1 analysis. (A) bFGF (left) and FGFR1 (right) analysis by Western Blot. Statistical analysis was performed by one-way ANOVA test followed by Tukey test. Data are shown as mean ± SE (n = 4). *p < 0,05; **p < 0,01; ***p < 0,001 versus Control. #p < 0,05; ##p < 0,01; ###p < 0,001 versus LD. Original western blots presented are available in Supplementary Fig. S3. (B) Representative confocal images of retinal cryosections immunolabelled for bFGF (green) and FGFR1 (red). Nuclei were stained with Bisbenzimide (blue). (a–e) High magnification of a random area of the sections showing co-localization in yellow (white arrows) of bFGF and FGFR1. Both bFGF and FGFR1 increased in the rat retina after light damage over time. CTRL (Control); LD (Light damage); LD + 7rec (Light damage + 7 days of recovery); LD + 60rec (Light damage + 60 days of recovery); LD + 120rec (Light damage + 120 days of recovery); ONL (Outer nuclear layer); INL (Inner nuclear layer); GCL (Ganglion cell layer).

Journal: Scientific reports

Article Title: Up-regulation of pro-angiogenic pathways and induction of neovascularization by an acute retinal light damage.

doi: 10.1038/s41598-020-63449-y

Figure Lengend Snippet: Figure 4. bFGF and FGFR1 analysis. (A) bFGF (left) and FGFR1 (right) analysis by Western Blot. Statistical analysis was performed by one-way ANOVA test followed by Tukey test. Data are shown as mean ± SE (n = 4). *p < 0,05; **p < 0,01; ***p < 0,001 versus Control. #p < 0,05; ##p < 0,01; ###p < 0,001 versus LD. Original western blots presented are available in Supplementary Fig. S3. (B) Representative confocal images of retinal cryosections immunolabelled for bFGF (green) and FGFR1 (red). Nuclei were stained with Bisbenzimide (blue). (a–e) High magnification of a random area of the sections showing co-localization in yellow (white arrows) of bFGF and FGFR1. Both bFGF and FGFR1 increased in the rat retina after light damage over time. CTRL (Control); LD (Light damage); LD + 7rec (Light damage + 7 days of recovery); LD + 60rec (Light damage + 60 days of recovery); LD + 120rec (Light damage + 120 days of recovery); ONL (Outer nuclear layer); INL (Inner nuclear layer); GCL (Ganglion cell layer).

Article Snippet: After blocking at RT for 1 h with 5% nonfat dry milk in TBST, the membranes were washed briefly and incubated with primary antibodies directed either against VEGF (Santa Cruz sc-7269), VEGFR2 (Invitrogen, AHR5102), bFGF (Merck, 05-117), FGFR1 (OriGene, TA324059) and Tubulin (Thermo Scientific, 62204) diluted in 5% non fat dry milk in TBST.

Techniques: Western Blot, Control, Staining