antibodies against fgf2  (Servicebio Inc)

Journal: Materials Today Bio

Article Title: Multidimensional nano-ion composite hydrogel based on enzymatic blood glucose control, gas therapy and ion liquid permeation for repairing diabetic wounds

doi: 10.1016/j.mtbio.2026.103213

Figure Lengend Snippet: Skin immunofluorescence staining and immunohistochemical analysis were performed in different treatment groups. A) Immunofluorescence staining images of NF200. β 3 -Tubulin. PGP9.5. CD31. VEGF and IL-6 in skin wounds on the 14th day after treatment. Scale = 400 μm. B) Immunohistochemical images of FGF2 on day 14 in wound tissue. Scale = 400 μm. C) Images of the immunohistochemistry of AGEs. Scale bar = 400 μm. D) Fluorescence intensity of NF200. E) Fluorescence intensity of β 3 Tubulin. F) Fluorescence intensity of PGP9.5. G) CD31-labeled micro vessel density. H) Fluorescence intensity of VEGF. I) Fluorescence intensity of IL-6. J) Integrated option density (IOD) of FGF2. K) IOD of AGEs. Data are represented as mean ± SD (n = 3). Statistical analysis was performed using one-way analysis of variance (ANOVA) followed by Tukey's test ∗ p < 0.05. ∗∗ p < 0.01. ∗∗∗ p < 0.001. ∗∗∗∗ p < 0.0001.

Article Snippet: After routine deparaffinization, rehydration, and antigen retrieval, the sections were blocked and then incubated overnight at 4 °C with primary antibodies against FGF2 (1:500, GB113751 , Servicebio) and AGEs (1:200, bs-1158R, BIOSS).

Techniques: Immunofluorescence, Staining, Immunohistochemical staining, Immunohistochemistry, Fluorescence, Labeling

Journal: Journal of Agricultural and Food Chemistry

Article Title: Sodium Benzoate Inhibits Osteoblast Differentiation and Accelerates Bone Loss by Regulating the FGF2/p38/RUNX2 Pathway

doi: 10.1021/acs.jafc.5c01124

Figure Lengend Snippet: NaB inhibits FGF2 expression in vitro and in vivo . (A) MC3T3-E1 cells and BMSCs were treated with or without 10 mM NaB. The cells were then subjected to RNA sequencing analysis, and a heatmap was generated to show differentially expressed genes (DEGs). Volcano plot of DEGs analyzed by RNA-seq of MC3T3-E1 cells (B) and BMSCs (C) treated with 0 or 10 mM NaB. FGF2 mRNA (D) and protein levels (E) in MC3T3-E1 cells treated with NaB (0, 5, or 10 mM) in OIM for 4 days. GAPDH was used as a loading control. (F) Quantification of the FGF2 protein level as shown in (E). (G) IF staining for FGF2 in MC3T3-E1 cells cultured in OIM for 4 days, scale bar = 50 μm. (H) IHC staining for FGF2 in the distal femur of mice, scale bar = 100 μm. Data are presented as the mean ± SD * P < 0.05; ** P < 0.01 compared with the 0 mM group.

Article Snippet: IHC was conducted using the primary antibody against FGF2 (1:100, ABclonal, Wuhan, China) and a horseradish peroxidase (HRP)-conjugated goat antirabbit IgG (H+L) secondary antibody (1:400, ABclonal, Wuhan, China).

Techniques: Expressing, In Vitro, In Vivo, RNA Sequencing, Generated, Control, Staining, Cell Culture, Immunohistochemistry

Journal: Biomaterials Research

Article Title: Derivation of Mesenchymal Stem Cells through Sequential Presentation of Growth Factors via Gelatin Microparticles in Pluripotent Stem Cell Spheroids

doi: 10.34133/bmr.0184

Figure Lengend Snippet: Bone morphogenetic protein-4 (BMP4)- and fibroblast growth factor 2 (FGF2)-induced differentiation of induced pluripotent stem cells (iPSCs) to mesenchymal stem cells (MSCs) in 2-dimensional (2D) conditions. (A) Schematic diagram depicting iPSC-to-induced MSC (iMSC) differentiation via mesoderm induction. (B) Images of iPSCs, mesoderm-induced cells, and iMSCs. Scale bar = 200 μm. (C) Quantitative real-time gene analysis (qPCR; top panel) and western blot (WB) analysis (bottom panel) of the mesoderm markers Brachyury and SNAI1 (Snail1), along with the pluripotency marker SOX2, at 4 d postdifferentiation. (D) qPCR (top panel) and WB analysis (bottom panel) of the MSC markers CD73, CD90, CD105, and CD44 at 11 d postdifferentiation. (E) Flow cytometry (fluorescence-activated cell sorting [FACS]) analysis of the MSC markers CD73, CD90, and CD44 in cells treated with either BMP4 only or BMP4 + FGF2. The qPCR data were normalized to 18S. The WB data were normalized to β-actin. All data represent results from 3 independent experiments, each conducted in triplicate. The data are presented as mean ± SD (ns, not significant; * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001). Individual data points and significance levels are indicated in graphs. DMEM, Dulbecco’s modified Eagle medium; SR, serum replacement; hiPSCs, human iPSCs; mRNA, messenger RNA; GF, growth factor.

Article Snippet: The slow- and fast-degrading GelMPs were incubated with primary antibodies against FGF2 (Santa Cruz Biotechnology, USA) and BMP4 (PeproTech, USA) overnight and labeled with Alexa Fluor 488 (Invitrogen, Thermo Fisher Scientific, USA) and Texas Red (Invitrogen, Thermo Fisher Scientific, USA) at 1 μl/100 μl of PBS, respectively.

Techniques: Western Blot, Marker, Flow Cytometry, Fluorescence, FACS, Modification

Journal: Biomaterials Research

Article Title: Derivation of Mesenchymal Stem Cells through Sequential Presentation of Growth Factors via Gelatin Microparticles in Pluripotent Stem Cell Spheroids

doi: 10.34133/bmr.0184

Figure Lengend Snippet: Gelatin microparticle (GelMP) fabrication, characterization, GF conjugation, and the release profiles of BMP4 and FGF2. (A) Scanning electron microscopy (SEM) images of fast-degrading (4 mM glutaraldehyde) and slow-degrading (12 mM glutaraldehyde) GelMPs. Scale bar = 100 μm. Size distributions of fast- and slow-degrading GelMPs. (B) Physical properties of fast- and slow-degrading GelMPs. (C) Representative immunofluorescent images of BMP4-conjugated fast-degrading GelMPs and FGF2-conjugated slow-degrading GelMPs. Scale bar = 100 μm. (D) Degradation rate of 5 mg of microparticles in collagenase (5 μg/ml) solution. (E) Cumulative release (%) of 1 μg of BMP4 from fast-degrading GelMPs and 1 μg of FGF2 from slow-degrading GelMPs incubated for 20 d in collagenase (5 μg/ml) solution. The obtained data represent results from 3 independent experiments, each conducted in triplicate. PBS, phosphate-buffered saline.

Article Snippet: The slow- and fast-degrading GelMPs were incubated with primary antibodies against FGF2 (Santa Cruz Biotechnology, USA) and BMP4 (PeproTech, USA) overnight and labeled with Alexa Fluor 488 (Invitrogen, Thermo Fisher Scientific, USA) and Texas Red (Invitrogen, Thermo Fisher Scientific, USA) at 1 μl/100 μl of PBS, respectively.

Techniques: Conjugation Assay, Electron Microscopy, Incubation, Saline

Journal: Cancers

Article Title: Fibroblast Growth Factor 2 (FGF2) Activates Vascular Endothelial Growth Factor (VEGF) Signaling in Gastrointestinal Stromal Tumors (GIST): An Autocrine Mechanism Contributing to Imatinib Mesylate (IM) Resistance

doi: 10.3390/cancers16173103

Figure Lengend Snippet: ( A , B ) The exogenous FGF2 activates VEGFR signaling in GIST T-1 cells via up-regulation of VEGF-A. ( A ) FGF-2 stimulates, whereas anti-FGF2 neutralizing Abs abrogates VEGFR signaling GIST T-1 cells. Cells were treated with FGF2 (100 ng/mL), IM (0.02 µM) alone or in the presence of anti-FGF2 neutralizing Abs (20 µg/mL) for 72 h. Expression of VEGF-A, total and phosphorylated forms of VEGFR, KIT, MAPK, AKT, and STAT1 was assessed by immunoblot analysis. Actin stain was used as a loading control for each sample. ( B ) Concentration of VEGF-A (pg/mL, measured by ELISA) in supernatants of IM-naive (GIST T-1) cells treated with DMSO (control), FGF-2 (100 ng/mL), IM (0.02 µM) alone or in the presence of anti-FGF-2 Abs (20 µg/mL) for 72 h. Data are presented as median ± SD. Significant differences with p < 0.05 (*), p < 0.01 (**) from n ≥ 3 using unpaired Student’s t -test. ( C ) Changes in the relative expression level of mRNA VEGF-A and VEGFR1, 2, and 3 in GIST T-1 after treatment with FGF-2 (100 ng/mL), as determined by quantitative RT-PCR. The amplification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used for internal control. Data are presented as median ± SD. Significant differences with p < 0.05 (*) from n ≥ 3 using unpaired Student’s t -test. The original Western blot figures can be found in .

Article Snippet: Neutralizing antibody against bFGF (Anti-FGF2/basic FGF #05-117) and human recombinant FGF-2/basic (FGF2 #01-106) were from Merck KGaA (Darmstadt, Germany).

Techniques: Expressing, Western Blot, Staining, Control, Concentration Assay, Enzyme-linked Immunosorbent Assay, Quantitative RT-PCR, Amplification

Journal: Experimental and Therapeutic Medicine

Article Title: MicroRNA-146a attenuates isoproterenol-induced cardiac fibrosis by inhibiting FGF2

doi: 10.3892/etm.2022.11433

Figure Lengend Snippet: miR-146a-5p directly targets FGF2 and FGF2 knockdown decreases collagen I and α-SMA expression levels in CFs. (A) StarBase database showed the potential binding sites between FGF2 and miR-146a-5p. (B) Luciferase reporter assay was used to determine the binding ability between FGF2 and miR-146a-5p in 293 cells. * P<0.05 vs. NC mimics. (C) RT-qPCR and (D) western blotting were used to assess the mRNA and protein levels of FGF2 in ISO-treated CFs transfected with NC or miR-146a-5p mimics or inhibitor or inhibitor. (E) RT-qPCR and (F) western blotting showed mRNA and protein levels of FGF2 in CFs transfected with siNC or siFGF2. (G) RT-qPCR analysis showed collagen I and α-SMA mRNA levels in ISO-treated CFs transfected with siNC or siFGF2. * P<0.05 vs. siNC. miR, microRNA; FGF2, fibroblast growth factor 2; α-SMA, α-smooth muscle actin; NC, negative control; CF, cardiac fibroblast; RT-q, reverse transcription-quantitative; ISO, isoproterenol; si, small interfering; WT, wild-type; MUT, mutant.

Article Snippet: After blocking with 5% non-fat milk for 2 h at room temperature, the membrane was incubated with primary antibodies against FGF2 (1:1,000; cat. no. PB0619; Boster Biological Technology, Ltd.) and GADPH (1:1,000; cat. no. ab9485; Abcam) overnight at 4 ̊C.

Techniques: Knockdown, Expressing, Binding Assay, Luciferase, Reporter Assay, Quantitative RT-PCR, Western Blot, Transfection, Negative Control, Reverse Transcription, Mutagenesis

Journal: Experimental and Therapeutic Medicine

Article Title: MicroRNA-146a attenuates isoproterenol-induced cardiac fibrosis by inhibiting FGF2

doi: 10.3892/etm.2022.11433

Figure Lengend Snippet: miR-146a-5p suppresses ISO-treated cardiac fibrosis by targeting FGF2. (A) RT-qPCR and (B) western blotting were performed to determine the mRNA and protein levels of FGF2 in ISO-treated CFs transfected with NC or miR-146a-5p mimics or miR-146a-5p mimics + pcDNA3.1/FGF2. (C) RT-qPCR and (D) Cell Counting Kit-8 assay determined collagen I and α-SMA expression levels, as well as viability, in ISO-treated CFs transfected with NC or miR-146a-5p mimics or miR-146a-5p mimics + pcDNA3.1/FGF2. * P<0.05. miR, microRNA; ISO, isoproterenol; FGF2, fibroblast growth factor 2; RT-q, reverse transcription-quantitative; CF, cardiac fibroblast; NC, negative control; OD, optical density.

Article Snippet: After blocking with 5% non-fat milk for 2 h at room temperature, the membrane was incubated with primary antibodies against FGF2 (1:1,000; cat. no. PB0619; Boster Biological Technology, Ltd.) and GADPH (1:1,000; cat. no. ab9485; Abcam) overnight at 4 ̊C.

Techniques: Quantitative RT-PCR, Western Blot, Transfection, Cell Counting, Expressing, Reverse Transcription, Negative Control