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human neutralizing fgfr1 mab765 (R&D Systems)

Name: human neutralizing fgfr1 mab765
Brand: R&D Systems
Rating: 93 (10 reviews)

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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 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "The Interaction of Apelin and FGFR1 Ameliorated the Kidney Fibrosis through Suppression of TGF β -Induced Endothelial-to-Mesenchymal Transition."

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

Journal: Oxidative medicine and cellular longevity

doi: 10.1155/2023/5012474

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.

Figure Legend 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.

Techniques Used: 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.

Figure Legend 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.

Techniques Used: Knockdown, Transfection, Western Blot

Image Search Results

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

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

ADAM9 is required for the entry phase of EMCV infection. (A) EMCV or CV-B3 were pretreated with the indicated concentrations of soluble ADAM9 protein or 100 μg/ml soluble FGFR1α/FGFR1β proteins for 1 h at 37°C and used to infect HAP1 cells. Capsid proteins (EMCV) or 3A protein (CV-B3) and nuclei (blue) were stained at 7 h postinfection. (B) HAP1 cells were pretreated with the indicated concentrations of antibody targeting ADAM9 and infected with virus for 7 h, followed by staining as described above for panel A. Representative confocal micrographs are shown in panels A, B, and C. Values (percentages) on the micrographs are mean ± SEM values for 3 or 4 (A) or 4 (B) technical replicates, normalized to the value for mock treatment. (C) WT, ADAM9 KO , or ADAM9 KO HAP1 cells overexpressing mouse ADAM9 mutant E348A (mADAM9) were incubated with EMCV or CV-B3 on ice, followed by qPCR analysis of bound virus. The values are means plus standard deviations (SD) (error bars) for three biological replicates. Experiments were conducted twice with similar results.

Journal: mBio

Article Title: Identification of the Cell-Surface Protease ADAM9 as an Entry Factor for Encephalomyocarditis Virus

doi: 10.1128/mBio.01780-19

Figure Lengend Snippet: ADAM9 is required for the entry phase of EMCV infection. (A) EMCV or CV-B3 were pretreated with the indicated concentrations of soluble ADAM9 protein or 100 μg/ml soluble FGFR1α/FGFR1β proteins for 1 h at 37°C and used to infect HAP1 cells. Capsid proteins (EMCV) or 3A protein (CV-B3) and nuclei (blue) were stained at 7 h postinfection. (B) HAP1 cells were pretreated with the indicated concentrations of antibody targeting ADAM9 and infected with virus for 7 h, followed by staining as described above for panel A. Representative confocal micrographs are shown in panels A, B, and C. Values (percentages) on the micrographs are mean ± SEM values for 3 or 4 (A) or 4 (B) technical replicates, normalized to the value for mock treatment. (C) WT, ADAM9 KO , or ADAM9 KO HAP1 cells overexpressing mouse ADAM9 mutant E348A (mADAM9) were incubated with EMCV or CV-B3 on ice, followed by qPCR analysis of bound virus. The values are means plus standard deviations (SD) (error bars) for three biological replicates. Experiments were conducted twice with similar results.

Article Snippet: The following chemicals and reagents were used in this study: recombinant human FGFR1α IIIb (catalog no. 655-FR; R&D Systems), recombinant human FGFR1β IIIc (catalog no. 661-FR; R&D Systems), recombinant human ADAM9 (catalog no. 939-AD-020; R&D Systems), goat polyclonal anti-ADAM9 (catalog no. AF939; R&D Systems), and batimastat (catalog no. 2961; Tocris).

Techniques: Infection, Staining, Virus, Mutagenesis, Incubation

Proximity between AcSDKP and FGFR1 inhibits the TGF β /smad signaling pathway in HMVECs. ( a ) HMVECs were treated with N-FGFR1 (1.5 μ g/ml) for 48 h with or without preincubation with AcSDKP (100 nM) for 2 h, and the proximity between AcSDKP and FGFR1 was analyzed by the Duolink In Situ Assay. For each slide, images at a × 400 original magnification were obtained from six different areas. ( b and c ) HMVECs were treated with TGF β 2 (5 ng/ml) for 15 min or 48 h with or without preincubation with AcSDKP for 2 h, and the p-smad3, TGF β R1, TGF β R2 and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-smad3/smad3, TGF β R1/ β -actin, TGF β R2/ β -actin and FGFR1/ β -actin levels from each group ( n =6) were analyzed. ( d and e ) HMVECs were incubated with TGF β 2 for 15 min or 48 h with or without preincubation with AcSDKP or its mutants (Ac DSPK , AcSDK A , Ac A DKP) (100 nM) for 2 h. The p-smad3/smad3, TGF β R1/ β -actin, TGF β R2/ β -actin and FGFR1/ β -actin protein levels were analyzed by western blot

Journal: Cell Death & Disease

Article Title: FGFR1 is critical for the anti-endothelial mesenchymal transition effect of N -acetyl-seryl-aspartyl-lysyl-proline via induction of the MAP4K4 pathway

doi: 10.1038/cddis.2017.353

Figure Lengend Snippet: Proximity between AcSDKP and FGFR1 inhibits the TGF β /smad signaling pathway in HMVECs. ( a ) HMVECs were treated with N-FGFR1 (1.5 μ g/ml) for 48 h with or without preincubation with AcSDKP (100 nM) for 2 h, and the proximity between AcSDKP and FGFR1 was analyzed by the Duolink In Situ Assay. For each slide, images at a × 400 original magnification were obtained from six different areas. ( b and c ) HMVECs were treated with TGF β 2 (5 ng/ml) for 15 min or 48 h with or without preincubation with AcSDKP for 2 h, and the p-smad3, TGF β R1, TGF β R2 and FGFR1 levels were analyzed by western blot. Densitometric analysis of the p-smad3/smad3, TGF β R1/ β -actin, TGF β R2/ β -actin and FGFR1/ β -actin levels from each group ( n =6) were analyzed. ( d and e ) HMVECs were incubated with TGF β 2 for 15 min or 48 h with or without preincubation with AcSDKP or its mutants (Ac DSPK , AcSDK A , Ac A DKP) (100 nM) for 2 h. The p-smad3/smad3, TGF β R1/ β -actin, TGF β R2/ β -actin and FGFR1/ β -actin protein levels were analyzed by western blot

Article Snippet: The mouse monoclonal anti-human CD31 (1 : 1000, AF3628), human neutralizing FGFR1 (1 : 500, MAB765) and neutralizing TGF β (1-2-3) (1 : 500, MAB1835) antibodies were purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: In Situ, Western Blot, Incubation

AcSDKP suppresses TGF β /smad signaling and EndMT through the FGFR1/FRS2 pathway. ( a ) HMVECs were treated with N-FGFR1 for 48 h, and the FGFR1, TGF β R1 and TGF β R2 protein levels were analyzed by western blot. ( b ) HMVECs were treated with TGF β 2 in the presence or absence of N-FGFR1 for 15 min with or without AcSDKP preincubation. The p-smad3 and TGF β R1 protein levels were analyzed by western blot. Densitometric analysis of the p-smad3/smad3 and TGF β R1/ β -actin levels ( n =3) in each group was performed. ( c ) HMVECs were incubated with either N-FGFR1 in the presence or absence of TGF β 2 for 48 h with or without preincubation with AcSDKP for 2 h or with N-FGFR1 in the presence or absence of TGF β 2 for 48 h with or without 24 h of incubation with FGF2 (50 ng/ml). The CD31, SM22 α , FSP1 and α -SMA protein levels were analyzed by western blot. ( d ) HMVECs were transfected with FRS2 siRNA (100 nM) for 48 h with or without AcSDKP preincubation. The VE-cadherin, FSP1, vimentin, SM22 α and p-smad3 levels were analyzed by western blot. ( e ) HMVECs were treated with N-FGFR1 for 48 h or 15 min in the presence or absence of N-TGF β (1, 2, 3) (1.0 μ g/ml). The CD31, VE-cadherin, SM22 α , FSP1, TGF β R1, TGF β R2 and p-smad3 levels were analyzed by western blot

Journal: Cell Death & Disease

Article Title: FGFR1 is critical for the anti-endothelial mesenchymal transition effect of N -acetyl-seryl-aspartyl-lysyl-proline via induction of the MAP4K4 pathway

doi: 10.1038/cddis.2017.353

Figure Lengend Snippet: AcSDKP suppresses TGF β /smad signaling and EndMT through the FGFR1/FRS2 pathway. ( a ) HMVECs were treated with N-FGFR1 for 48 h, and the FGFR1, TGF β R1 and TGF β R2 protein levels were analyzed by western blot. ( b ) HMVECs were treated with TGF β 2 in the presence or absence of N-FGFR1 for 15 min with or without AcSDKP preincubation. The p-smad3 and TGF β R1 protein levels were analyzed by western blot. Densitometric analysis of the p-smad3/smad3 and TGF β R1/ β -actin levels ( n =3) in each group was performed. ( c ) HMVECs were incubated with either N-FGFR1 in the presence or absence of TGF β 2 for 48 h with or without preincubation with AcSDKP for 2 h or with N-FGFR1 in the presence or absence of TGF β 2 for 48 h with or without 24 h of incubation with FGF2 (50 ng/ml). The CD31, SM22 α , FSP1 and α -SMA protein levels were analyzed by western blot. ( d ) HMVECs were transfected with FRS2 siRNA (100 nM) for 48 h with or without AcSDKP preincubation. The VE-cadherin, FSP1, vimentin, SM22 α and p-smad3 levels were analyzed by western blot. ( e ) HMVECs were treated with N-FGFR1 for 48 h or 15 min in the presence or absence of N-TGF β (1, 2, 3) (1.0 μ g/ml). The CD31, VE-cadherin, SM22 α , FSP1, TGF β R1, TGF β R2 and p-smad3 levels were analyzed by western blot

Techniques: Western Blot, Incubation, Transfection

FGF2/FGFR1 mediates MAP4K4 signaling in endothelial cells. ( a ) Immunofluorescence microscopy analysis of P-MAP4K4 expression following FRS2 siRNA or TGF β 2 treatment. For each slide, images of six different fields of view at × 400 magnification were evaluated. The scale bar is 60 μ m in each panel. ( b and c ) HMVECs were treated with N-FGFR1 for 48 h or FGF2 for 24 h. The P-MAP4K4 levels were analyzed by western blot

Journal: Cell Death & Disease

Article Title: FGFR1 is critical for the anti-endothelial mesenchymal transition effect of N -acetyl-seryl-aspartyl-lysyl-proline via induction of the MAP4K4 pathway

doi: 10.1038/cddis.2017.353

Figure Lengend Snippet: FGF2/FGFR1 mediates MAP4K4 signaling in endothelial cells. ( a ) Immunofluorescence microscopy analysis of P-MAP4K4 expression following FRS2 siRNA or TGF β 2 treatment. For each slide, images of six different fields of view at × 400 magnification were evaluated. The scale bar is 60 μ m in each panel. ( b and c ) HMVECs were treated with N-FGFR1 for 48 h or FGF2 for 24 h. The P-MAP4K4 levels were analyzed by western blot

Techniques: Immunofluorescence, Microscopy, Expressing, Western Blot

The proximity between FGFR1 and P-MAP4K4 decreases in FGFR1-deficient cells. ( a ) HMVECs were treated with N-FGFR1 or TGF β 2 for 48 h. The proximity between FGFR1 and P-MAP4K4 was analyzed using the Duolink In Situ Assay. For each slide, images at × 400 original magnification were obtained from six different areas. ( b ) immunoprecipitation analysis with either a P-MAP4K4 or a FGFR1 antibody was performed and analyzed by western blot. Then, the FGFR1 and P-MAP4K4 levels with N-FGFR1 or TGF β 2 treatment were analyzed by western blot in endothelial cells

Journal: Cell Death & Disease

Article Title: FGFR1 is critical for the anti-endothelial mesenchymal transition effect of N -acetyl-seryl-aspartyl-lysyl-proline via induction of the MAP4K4 pathway

doi: 10.1038/cddis.2017.353

Figure Lengend Snippet: The proximity between FGFR1 and P-MAP4K4 decreases in FGFR1-deficient cells. ( a ) HMVECs were treated with N-FGFR1 or TGF β 2 for 48 h. The proximity between FGFR1 and P-MAP4K4 was analyzed using the Duolink In Situ Assay. For each slide, images at × 400 original magnification were obtained from six different areas. ( b ) immunoprecipitation analysis with either a P-MAP4K4 or a FGFR1 antibody was performed and analyzed by western blot. Then, the FGFR1 and P-MAP4K4 levels with N-FGFR1 or TGF β 2 treatment were analyzed by western blot in endothelial cells

Techniques: In Situ, Immunoprecipitation, Western Blot

MAP4K4 signaling is mediated by AcSDKP in a FGFR1/FRS2-dependent manner. ( a and b ) HMVECs were treated with N-FGFR1 for 48 h in the presence or absence of FGF2 or AcSDKP. P-MAP4K4 levels were analyzed by western blot. Densitometric analysis of P-MAP4K4 levels normalized to MAP4K4. For each group, n =3 were analyzed. ( c and d ) HMVECs were transfected with FRS2 siRNA for 48 h with or without FGF2 or AcSDKP treatment. P-MAP4K4 levels were analyzed by western blot. Densitometric analysis of P-MAP4K4 levels, normalized to MAP4K4. A total of n =3 from each group were analyzed

Journal: Cell Death & Disease

Article Title: FGFR1 is critical for the anti-endothelial mesenchymal transition effect of N -acetyl-seryl-aspartyl-lysyl-proline via induction of the MAP4K4 pathway

doi: 10.1038/cddis.2017.353

Figure Lengend Snippet: MAP4K4 signaling is mediated by AcSDKP in a FGFR1/FRS2-dependent manner. ( a and b ) HMVECs were treated with N-FGFR1 for 48 h in the presence or absence of FGF2 or AcSDKP. P-MAP4K4 levels were analyzed by western blot. Densitometric analysis of P-MAP4K4 levels normalized to MAP4K4. For each group, n =3 were analyzed. ( c and d ) HMVECs were transfected with FRS2 siRNA for 48 h with or without FGF2 or AcSDKP treatment. P-MAP4K4 levels were analyzed by western blot. Densitometric analysis of P-MAP4K4 levels, normalized to MAP4K4. A total of n =3 from each group were analyzed

Techniques: Western Blot, Transfection

AcSDKP inhibits TGF β /smad signaling and EndMT and restores the FGFR1 and P-MAP4K4 levels in diabetic hearts. ( a ) Immunofluorescence microscopy analysis of CD31/FGFR1 and CD31/P-MAP4K4 in the heart tissues from each group of mice. The scale bar is 60 μ m in each panel. The CD31 and FGFR1 double-labeled cells and the CD31 and P-MAP4K4 double-labeled cells in each visual field were assessed by fluorescence microscopy and quantified. For each section, images from six different fields of view at × 400 magnification were evaluated. ( b and c ) Immunofluorescence microscopy analysis of CD31/ α -SMA, VE-cadherin /SM22 α and CD31/p-smad3 expression levels in the heart tissues from each group of mice. The scale bar is 60 μ m in each panel. The CD31 and α -SMA double-labeled cells, the VE-cadherin and SM22 α double-labeled cells and the CD31 and p-smad3 double-labeled cells in each visual field were analyzed by fluorescence microscopy and quantified. For each section, images from six different fields of view at × 400 magnification were evaluated. Four mice from each group were analyzed. ( d ) Western blot analysis of the FGFR1, P-MAP4K4, TGF β 1, TGF β 2 and TGF β 3 levels in cardiac tissues. A representative blot from four independent experiments was shown. The densitometric analysis of western blot data was presented ( n =4). The diabetic mice are abbreviated as DM in the figure

Journal: Cell Death & Disease

Article Title: FGFR1 is critical for the anti-endothelial mesenchymal transition effect of N -acetyl-seryl-aspartyl-lysyl-proline via induction of the MAP4K4 pathway

doi: 10.1038/cddis.2017.353

Figure Lengend Snippet: AcSDKP inhibits TGF β /smad signaling and EndMT and restores the FGFR1 and P-MAP4K4 levels in diabetic hearts. ( a ) Immunofluorescence microscopy analysis of CD31/FGFR1 and CD31/P-MAP4K4 in the heart tissues from each group of mice. The scale bar is 60 μ m in each panel. The CD31 and FGFR1 double-labeled cells and the CD31 and P-MAP4K4 double-labeled cells in each visual field were assessed by fluorescence microscopy and quantified. For each section, images from six different fields of view at × 400 magnification were evaluated. ( b and c ) Immunofluorescence microscopy analysis of CD31/ α -SMA, VE-cadherin /SM22 α and CD31/p-smad3 expression levels in the heart tissues from each group of mice. The scale bar is 60 μ m in each panel. The CD31 and α -SMA double-labeled cells, the VE-cadherin and SM22 α double-labeled cells and the CD31 and p-smad3 double-labeled cells in each visual field were analyzed by fluorescence microscopy and quantified. For each section, images from six different fields of view at × 400 magnification were evaluated. Four mice from each group were analyzed. ( d ) Western blot analysis of the FGFR1, P-MAP4K4, TGF β 1, TGF β 2 and TGF β 3 levels in cardiac tissues. A representative blot from four independent experiments was shown. The densitometric analysis of western blot data was presented ( n =4). The diabetic mice are abbreviated as DM in the figure

Techniques: Immunofluorescence, Microscopy, Labeling, Fluorescence, Expressing, Western Blot

Schematic of the AcSDKP/FGFR1/MAP4K4 pathway suppression of TGF β /smad signaling and EndMT. In endothelial cells, the close proximity between AcSDKP and FGFR1 increased FGFR1 and induced its phosphorylation levels. Interacting with co-factor FRS2, FGFR1 recruited MAP4K4 and induced its phosphorylation. Subsequently, p-MAP4K4 suppressed integrin β 1 (integrin β 1 should be localized on the cell surface interacted with some of α integrins). Integrin β 1 was a potent activator of TGF- β signaling and also EndMT. Therefore, AcSDKP could inhibit EndMT through FGFR1-MAP4K4-dependent manner

Journal: Cell Death & Disease

Article Title: FGFR1 is critical for the anti-endothelial mesenchymal transition effect of N -acetyl-seryl-aspartyl-lysyl-proline via induction of the MAP4K4 pathway

doi: 10.1038/cddis.2017.353

Figure Lengend Snippet: Schematic of the AcSDKP/FGFR1/MAP4K4 pathway suppression of TGF β /smad signaling and EndMT. In endothelial cells, the close proximity between AcSDKP and FGFR1 increased FGFR1 and induced its phosphorylation levels. Interacting with co-factor FRS2, FGFR1 recruited MAP4K4 and induced its phosphorylation. Subsequently, p-MAP4K4 suppressed integrin β 1 (integrin β 1 should be localized on the cell surface interacted with some of α integrins). Integrin β 1 was a potent activator of TGF- β signaling and also EndMT. Therefore, AcSDKP could inhibit EndMT through FGFR1-MAP4K4-dependent manner

Techniques: Phospho-proteomics

Expression of FGFR1 in cells from breast and bone tissue. a , FGFR mRNA transcript levels in normal and cancer cells. b , Fold change in FGFR mRNA based on expression in cancers cells relative to normal cells. c , FGFR protein levels in normal versus cancer cells. Results are from triplicate experiments and the Western blot is representative of the triplicates. (* p < 0.05)

Journal: Molecular Cancer

Article Title: Targeting the heparin-binding domain of fibroblast growth factor receptor 1 as a potential cancer therapy

doi: 10.1186/s12943-015-0391-4

Figure Lengend Snippet: Expression of FGFR1 in cells from breast and bone tissue. a , FGFR mRNA transcript levels in normal and cancer cells. b , Fold change in FGFR mRNA based on expression in cancers cells relative to normal cells. c , FGFR protein levels in normal versus cancer cells. Results are from triplicate experiments and the Western blot is representative of the triplicates. (* p < 0.05)

Article Snippet: FGFR1 antibody (#MAB765) was from R&D Systems.

Techniques: Expressing, Western Blot

Specificity of IMB-R1 for FGFR1. a , Binding of IMB-R1 and MAB765 to FGFR1 isoforms (representative blot from triplicate experiments). b , Affinity of IMB-R1 for FGFR isoforms (results are from triplicate experiments). c , Binding of FGFR to heparin in the presence or absence of IMB-R1 (results are from triplicate experiments). d , Binding of FGF2 to FGFR in the presence or absence of IMB-R1 (results are from triplicate experiments). e , FGFR phosphorylation stimulated by FGF2 in the presence or absence of IMB-R1 including the fold change of FGFR phosphorylation as determined by a comparison of means

Journal: Molecular Cancer

Article Title: Targeting the heparin-binding domain of fibroblast growth factor receptor 1 as a potential cancer therapy

doi: 10.1186/s12943-015-0391-4

Figure Lengend Snippet: Specificity of IMB-R1 for FGFR1. a , Binding of IMB-R1 and MAB765 to FGFR1 isoforms (representative blot from triplicate experiments). b , Affinity of IMB-R1 for FGFR isoforms (results are from triplicate experiments). c , Binding of FGFR to heparin in the presence or absence of IMB-R1 (results are from triplicate experiments). d , Binding of FGF2 to FGFR in the presence or absence of IMB-R1 (results are from triplicate experiments). e , FGFR phosphorylation stimulated by FGF2 in the presence or absence of IMB-R1 including the fold change of FGFR phosphorylation as determined by a comparison of means

Article Snippet: FGFR1 antibody (#MAB765) was from R&D Systems.

Techniques: Binding Assay, Phospho-proteomics, Comparison

Effects of FGFR1 inhibitors on cell growth. a , Fold change in cell number 48 h after treatment with IMB-R1. b , Temporal change in MG63 cell number following treatment with IMB-R1 (1:250). c , Cell number following FGF2 treatment (20 ng/ml for MG63, 5 ng/ml for MDAMB468 and T47D) for 48 h. Cells were pre-treatment with IMB-R1 for 1 h before FGF2 treatment. d , Cell number (MG63) following 48 h treatment with IMB-R1 or antigen-purified IMB-R1. e , Cell numbers following 48 h treatment with varying doses of FGFR inhibitors. f , Cell numbers following 48 h treatment with the FGFR1 antibody (MAB765) at varying doses. Unless otherwise stated, IMB-R1 was applied at a dilution of 1:250. All experiments were performed in triplicate

Journal: Molecular Cancer

Article Title: Targeting the heparin-binding domain of fibroblast growth factor receptor 1 as a potential cancer therapy

doi: 10.1186/s12943-015-0391-4

Figure Lengend Snippet: Effects of FGFR1 inhibitors on cell growth. a , Fold change in cell number 48 h after treatment with IMB-R1. b , Temporal change in MG63 cell number following treatment with IMB-R1 (1:250). c , Cell number following FGF2 treatment (20 ng/ml for MG63, 5 ng/ml for MDAMB468 and T47D) for 48 h. Cells were pre-treatment with IMB-R1 for 1 h before FGF2 treatment. d , Cell number (MG63) following 48 h treatment with IMB-R1 or antigen-purified IMB-R1. e , Cell numbers following 48 h treatment with varying doses of FGFR inhibitors. f , Cell numbers following 48 h treatment with the FGFR1 antibody (MAB765) at varying doses. Unless otherwise stated, IMB-R1 was applied at a dilution of 1:250. All experiments were performed in triplicate

Article Snippet: FGFR1 antibody (#MAB765) was from R&D Systems.

Techniques: Purification

The effect of IMB-R1 on gene expression. Cells were treated with IMB-R1 (1:250 dilution) for 48 h and RNA extracted for microarray analysis. a , The heatmaps: Red, up-regulation; Green, down-regulation. b , Top 10 affected cellular functions by IMB-R1 as determined by Ingenuity Pathway Analysis. c , The number of common genes affected across the different cells. d , The antioxidant genes significantly regulated by IMB-R1. e , The proposed signaling mechanisms disrupted by IMB-R1 during FGF2/FGFR1 dependent cell growth and survival in cancer cells

Journal: Molecular Cancer

Article Title: Targeting the heparin-binding domain of fibroblast growth factor receptor 1 as a potential cancer therapy

doi: 10.1186/s12943-015-0391-4

Figure Lengend Snippet: The effect of IMB-R1 on gene expression. Cells were treated with IMB-R1 (1:250 dilution) for 48 h and RNA extracted for microarray analysis. a , The heatmaps: Red, up-regulation; Green, down-regulation. b , Top 10 affected cellular functions by IMB-R1 as determined by Ingenuity Pathway Analysis. c , The number of common genes affected across the different cells. d , The antioxidant genes significantly regulated by IMB-R1. e , The proposed signaling mechanisms disrupted by IMB-R1 during FGF2/FGFR1 dependent cell growth and survival in cancer cells

Article Snippet: FGFR1 antibody (#MAB765) was from R&D Systems.

Techniques: Gene Expression, Microarray

IMB-R1 targets FGFR1 in multiple human cancers. a , IMB-R1 histochemical staining from a human cancer tissue array. Right panel , enlarged image of boxed area highlighting increased FGFR1 expression (detected by IMB-R1) in breast cancer tissues from twenty separate donors compared with adjacent healthy breast tissue. b , The intensity of FGFR1 expression (detected by IMB-R1) was scored and the average scores for the various cancer tissues compared with those from adjacent healthy tissues

Journal: Molecular Cancer

Article Title: Targeting the heparin-binding domain of fibroblast growth factor receptor 1 as a potential cancer therapy

doi: 10.1186/s12943-015-0391-4

Figure Lengend Snippet: IMB-R1 targets FGFR1 in multiple human cancers. a , IMB-R1 histochemical staining from a human cancer tissue array. Right panel , enlarged image of boxed area highlighting increased FGFR1 expression (detected by IMB-R1) in breast cancer tissues from twenty separate donors compared with adjacent healthy breast tissue. b , The intensity of FGFR1 expression (detected by IMB-R1) was scored and the average scores for the various cancer tissues compared with those from adjacent healthy tissues

Article Snippet: FGFR1 antibody (#MAB765) was from R&D Systems.

Techniques: Staining, Expressing

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1) Product Images from "The Interaction of Apelin and FGFR1 Ameliorated the Kidney Fibrosis through Suppression of TGF β -Induced Endothelial-to-Mesenchymal Transition."

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