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anti transforming growth factor tgf β2  (R&D Systems)


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    R&D Systems anti transforming growth factor tgf β2
    Anti Transforming Growth Factor Tgf β2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+transforming+growth+factor+tgf+%CE%B22/TGF-beta+2+Antibody/pmc12186380-140-102-109
    Average 93 stars, based on 21 article reviews
    anti transforming growth factor tgf β2 - by Bioz Stars, 2026-10
    93/100 stars

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    Article Title: Delivery of LOXL1-AS1 -siRNAs using targeting peptide-engineered extracellular vesicles with focused ultrasound to suppress medulloblastoma metastasis
    Article Snippet: First antibodies, including anti-β-actin (cat. no. GTX109639, GeneTex, Irvine, CA, USA), anti-Bmi1 (D20B7, cat. no. #6964, Cell Signaling Technology, Danvers, MA, USA), anti-bovine serum albumin (BSA; cat. no. 2A3E6, Santa Cruz Biotechnology), anti-calnexin (cat. no. #2433, Cell Signaling Technology), anti-cluster of differentiation 63 (CD63; cat. no. 10628D, ThermoFisher Scientific), anti-CD81 (cat. no. sc-7637, Santa Cruz Biotechnology), anti-CD9 (cat. no. sc-59140, Santa Cruz Biotechnology), anti-CD90 (cat. no. 13801, Cell Signaling Technology), anti-lamin A/C (cat. no. 10298-1-AP, ProteinTech, Rosemont, IL, USA), anti-Lamp2 (cat. no. GTX103214, GeneTex), anti-Nanog (D73G4, cat. no. 4903, Cell Signaling Technology), anti-Oct4 (cat. no. GTX101507, GeneTex), anti-Sox2 (cat. no. GTX101507, GeneTex), anti-transforming growth factor (TGF)-β2 (cat. no. MAB612, R&D Systems, Minneapolis, MN, USA), anti-TSG101 (cat. no. 72312, Cell Signaling Technology), and anti-V5 (cat. no. A01724, GenScript, Piscataway, NJ, USA) were probed at a 1:1000 dilution overnight at 4°C.

    Article Title: Delivery of LOXL1-AS1-siRNAs using targeting peptide-engineered extracellular vesicles with focused ultrasound to suppress medulloblastoma metastasis.
    Article Snippet: First antibodies, including anti-β-actin (cat. no. GTX109639, GeneTex, Irvine, CA, USA), anti-Bmi1 (D20B7, cat. no. #6964, Cell Signaling Technology, Danvers, MA, USA), anti-bovine serum albumin (BSA; cat. no. 2A3E6, Santa Cruz Biotechnology), anti-calnexin (cat. no. #2433, Cell Signaling Technology), anti-cluster of differentiation 63 (CD63; cat. no. 10628D, ThermoFisher Scientific), anti-CD81 (cat. no. sc-7637, Santa Cruz Biotechnology), anti-CD9 (cat. no. sc-59140, Santa Cruz Biotechnology), anti-CD90 (cat. no. 13801, Cell Signaling Technology), anti-lamin A/C (cat. no. 10298-1-AP, ProteinTech, Rosemont, IL, USA), anti-Lamp2 (cat. no. GTX103214, GeneTex), anti-Nanog (D73G4, cat. no. 4903, Cell Signaling Technology), anti-Oct4 (cat. no. GTX101507, GeneTex), anti-Sox2 (cat. no. GTX101507, GeneTex), anti-transforming growth factor (TGF)-β2 (cat. no. MAB612, R&D Systems, Minneapolis, MN, USA), anti-TSG101 (cat. no. 72312, Cell Signaling Technology), and anti-V5 (cat. no. A01724, GenScript, Piscataway, NJ, USA) were probed at a 1:1000 dilution overnight at 4°C.



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    uMSC-EVs inhibited <t>TGF-β2</t> and TGF-βR2 expression in lung tissues of BLM-induced mice. a , b Expression levels of TGF-β2 and TGF-βR2 were detected using IF staining and qRT-PCR. Scale bar = 200 μm. Mean ± SEM; * p < 0.05, ** p < 0.01, *** p < 0.001; n = 5. TGF-β2, transforming growth factor-β2; TGF-βR2, transforming growth factor-β receptor type II
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    Expression levels of transforming growth factor <t>(TGF)-β2</t> in human macrophages. The macrophages were transfected with mR-142-5p inhibitor or mimic, and incubated with ox-LDL for 24 h. (A) Western blot analysis of TGF-β2 protein expression levels. (B) Quantification of protein expression levels, normalized to that of GAPDH. (C) Quantitative polymerase chain reaction analysis of relative TGF-β2 mRNA expression levels, normalized to that of β-actin. The data are expressed as the means ± standard error of the mean from three independent experiments. * P<0.05 vs control, # P<0.05 vs control+ox-LDL. NC, negative control; KD, kilodaltons.
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    Image Search Results


    Fig. 6 Supernatant of osteoclast after Fer-1 treatment promotes osteogenesis and angiogenesis. (A-D) Concentration of TGF-β, SDF-1, S1P and PDGF- BB in the supernatant of osteoclast of each group. (E) ALP staining of BMSCs of each group after co-culture with supernatant of osteoclast for 14 days. Scale bar = 200 μm. (F) Positive area of ALP staining. (G) Alizarin Red staining of BMSCs of each group after co-culture with supernatant of osteoclast for 14 days. Scale bar = 200 μm. (H) Positive area of Alizarin Red staining. (I) Tube formation assay of ECs of each group after co-culture with supernatant of osteoclast for 6 h. (J) Numbers of Meshes of Tube formation assay. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, ns = not statistically significant

    Journal: Journal of orthopaedic surgery and research

    Article Title: Ferrostatin-1 inhibits osteoclast differentiation and prevents osteoporosis by suppressing lipid peroxidation.

    doi: 10.1186/s13018-025-05544-2

    Figure Lengend Snippet: Fig. 6 Supernatant of osteoclast after Fer-1 treatment promotes osteogenesis and angiogenesis. (A-D) Concentration of TGF-β, SDF-1, S1P and PDGF- BB in the supernatant of osteoclast of each group. (E) ALP staining of BMSCs of each group after co-culture with supernatant of osteoclast for 14 days. Scale bar = 200 μm. (F) Positive area of ALP staining. (G) Alizarin Red staining of BMSCs of each group after co-culture with supernatant of osteoclast for 14 days. Scale bar = 200 μm. (H) Positive area of Alizarin Red staining. (I) Tube formation assay of ECs of each group after co-culture with supernatant of osteoclast for 6 h. (J) Numbers of Meshes of Tube formation assay. Data are presented as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, ns = not statistically significant

    Article Snippet: The cell supernatant or serum was collected and centrifuged for 20 min at 1000×g at 2–8°C and then added to a 96-well plate covered by ELISA antibodies against TGF-β (Elabscience, USA, E-EL-M1191), SDF-1 (Elabscience, USA, E-EL-M3046), S1P (Meimian, China, MM44778M2), PDGF-BB (Elabscience, USA, E-EL-M0632), Trap-5b (Elabscience, USA, E-EL-M1116), RANKL (Elabscience, USA, E-EL-M0644), CTX-1 (Elabscience, USA, E-EL-M3023) and PINP (Elabscience, USA, E-ELM0233).

    Techniques: Concentration Assay, Staining, Co-Culture Assay, Tube Formation Assay

    uMSC-EVs inhibited TGF-β2 and TGF-βR2 expression in lung tissues of BLM-induced mice. a , b Expression levels of TGF-β2 and TGF-βR2 were detected using IF staining and qRT-PCR. Scale bar = 200 μm. Mean ± SEM; * p < 0.05, ** p < 0.01, *** p < 0.001; n = 5. TGF-β2, transforming growth factor-β2; TGF-βR2, transforming growth factor-β receptor type II

    Journal: Stem Cell Research & Therapy

    Article Title: Extracellular vesicles derived from umbilical cord mesenchymal stromal cells alleviate pulmonary fibrosis by means of transforming growth factor-β signaling inhibition

    doi: 10.1186/s13287-021-02296-8

    Figure Lengend Snippet: uMSC-EVs inhibited TGF-β2 and TGF-βR2 expression in lung tissues of BLM-induced mice. a , b Expression levels of TGF-β2 and TGF-βR2 were detected using IF staining and qRT-PCR. Scale bar = 200 μm. Mean ± SEM; * p < 0.05, ** p < 0.01, *** p < 0.001; n = 5. TGF-β2, transforming growth factor-β2; TGF-βR2, transforming growth factor-β receptor type II

    Article Snippet: The primary antibodies used in the study were anti-Ki67 (bs-23105R, Bioss, China), anti-α-SMA (bsm-33188M, Bioss, China), anti-fibronectin (anti-Fn; bs-0666R, Bioss, China), anti-transforming growth factor-β1 (anti-TGF-β1; bsm33345M, Bioss, China), anti-transforming growth factor-β2 (anti-TGF-β2; bs-20412R, Bioss, China), anti-transforming growth factor-β3 (anti-TGF-β3; AF8142, Beyotime, China), anti-transforming growth factor-β receptor type I (anti-TGF-βR1; bs0638R, Bioss, China), and anti-transforming growth factor-β receptor type II (anti-TGF-βR2; AF8151, Beyotime, China).

    Techniques: Expressing, Staining, Quantitative RT-PCR

    uMSC-EVs inhibited TGF-β1-induced myofibroblast differentiation in vitro. WML2 fibroblast cells were cultured for 48 h with TGF-β1 to induce myofibroblast differentiation, some of the cells were also treated with uMSC-EVs as indicated, then expression levels of α-SMA ( a , b ), TGF-β2 ( c , d ), and TGF-βR2 ( c , e ) were detected in different treatments using qRT-PCR and IF. Scale bar = 200 μm. Mean ± SEM; * p < 0.05, ** p < 0.01, *** p < 0.001; n = 3. TGF-β1, transforming growth factor-β1

    Journal: Stem Cell Research & Therapy

    Article Title: Extracellular vesicles derived from umbilical cord mesenchymal stromal cells alleviate pulmonary fibrosis by means of transforming growth factor-β signaling inhibition

    doi: 10.1186/s13287-021-02296-8

    Figure Lengend Snippet: uMSC-EVs inhibited TGF-β1-induced myofibroblast differentiation in vitro. WML2 fibroblast cells were cultured for 48 h with TGF-β1 to induce myofibroblast differentiation, some of the cells were also treated with uMSC-EVs as indicated, then expression levels of α-SMA ( a , b ), TGF-β2 ( c , d ), and TGF-βR2 ( c , e ) were detected in different treatments using qRT-PCR and IF. Scale bar = 200 μm. Mean ± SEM; * p < 0.05, ** p < 0.01, *** p < 0.001; n = 3. TGF-β1, transforming growth factor-β1

    Article Snippet: The primary antibodies used in the study were anti-Ki67 (bs-23105R, Bioss, China), anti-α-SMA (bsm-33188M, Bioss, China), anti-fibronectin (anti-Fn; bs-0666R, Bioss, China), anti-transforming growth factor-β1 (anti-TGF-β1; bsm33345M, Bioss, China), anti-transforming growth factor-β2 (anti-TGF-β2; bs-20412R, Bioss, China), anti-transforming growth factor-β3 (anti-TGF-β3; AF8142, Beyotime, China), anti-transforming growth factor-β receptor type I (anti-TGF-βR1; bs0638R, Bioss, China), and anti-transforming growth factor-β receptor type II (anti-TGF-βR2; AF8151, Beyotime, China).

    Techniques: In Vitro, Cell Culture, Expressing, Quantitative RT-PCR

    uMSC-EV-specific miRNAs target TGF-β2 and TGF-βR2 to inhibit myofibroblast differentiation. a Main miRNAs in uMSC-EVs using qRT-PCR. b A list of predicted binding sites of uMSC-EV-specific miRNAs and their targets. c – e Effect of uMSC-EV-specific miRNAs (mimics) on the expression levels of α-SMA, TGF-β2, and TGF-βR2 in TGF-β1-induced WML2 fibroblast cells (5 ng/mL) using IF and qRT-PCR. Scale bar = 200 μm. Mean ± SEM; * p < 0.05, ** p < 0.01, *** p < 0.001; n = 3

    Journal: Stem Cell Research & Therapy

    Article Title: Extracellular vesicles derived from umbilical cord mesenchymal stromal cells alleviate pulmonary fibrosis by means of transforming growth factor-β signaling inhibition

    doi: 10.1186/s13287-021-02296-8

    Figure Lengend Snippet: uMSC-EV-specific miRNAs target TGF-β2 and TGF-βR2 to inhibit myofibroblast differentiation. a Main miRNAs in uMSC-EVs using qRT-PCR. b A list of predicted binding sites of uMSC-EV-specific miRNAs and their targets. c – e Effect of uMSC-EV-specific miRNAs (mimics) on the expression levels of α-SMA, TGF-β2, and TGF-βR2 in TGF-β1-induced WML2 fibroblast cells (5 ng/mL) using IF and qRT-PCR. Scale bar = 200 μm. Mean ± SEM; * p < 0.05, ** p < 0.01, *** p < 0.001; n = 3

    Article Snippet: The primary antibodies used in the study were anti-Ki67 (bs-23105R, Bioss, China), anti-α-SMA (bsm-33188M, Bioss, China), anti-fibronectin (anti-Fn; bs-0666R, Bioss, China), anti-transforming growth factor-β1 (anti-TGF-β1; bsm33345M, Bioss, China), anti-transforming growth factor-β2 (anti-TGF-β2; bs-20412R, Bioss, China), anti-transforming growth factor-β3 (anti-TGF-β3; AF8142, Beyotime, China), anti-transforming growth factor-β receptor type I (anti-TGF-βR1; bs0638R, Bioss, China), and anti-transforming growth factor-β receptor type II (anti-TGF-βR2; AF8151, Beyotime, China).

    Techniques: Quantitative RT-PCR, Binding Assay, Expressing

    Expression levels of transforming growth factor (TGF)-β2 in human macrophages. The macrophages were transfected with mR-142-5p inhibitor or mimic, and incubated with ox-LDL for 24 h. (A) Western blot analysis of TGF-β2 protein expression levels. (B) Quantification of protein expression levels, normalized to that of GAPDH. (C) Quantitative polymerase chain reaction analysis of relative TGF-β2 mRNA expression levels, normalized to that of β-actin. The data are expressed as the means ± standard error of the mean from three independent experiments. * P<0.05 vs control, # P<0.05 vs control+ox-LDL. NC, negative control; KD, kilodaltons.

    Journal: Molecular Medicine Reports

    Article Title: Upregulation of miR-142-5p in atherosclerotic plaques and regulation of oxidized low-density lipoprotein-induced apoptosis in macrophages

    doi: 10.3892/mmr.2015.3191

    Figure Lengend Snippet: Expression levels of transforming growth factor (TGF)-β2 in human macrophages. The macrophages were transfected with mR-142-5p inhibitor or mimic, and incubated with ox-LDL for 24 h. (A) Western blot analysis of TGF-β2 protein expression levels. (B) Quantification of protein expression levels, normalized to that of GAPDH. (C) Quantitative polymerase chain reaction analysis of relative TGF-β2 mRNA expression levels, normalized to that of β-actin. The data are expressed as the means ± standard error of the mean from three independent experiments. * P<0.05 vs control, # P<0.05 vs control+ox-LDL. NC, negative control; KD, kilodaltons.

    Article Snippet: The following reagents, kits, primers and cells were used and sourced from the following companies: Anti-rabbit transforming growth factor-β2 (TGF-β2) monoclonal antibody (ProteinTech Group, Inc., Chicago, IL, USA); anti-mouse GAPDH monoclonal antibody (SunShineBio, Nanjing, China); miR-142-5p primers (Exiqon Co., Copenhagen, Denmark); TGF-β2 primers (ShangDe Biomedical Engineering, Shanghai, China); total RNA extraction kit (TRIzol ® ; Invitrogen Life Technologies, Carlsbad, CA, USA); THP-1 human monocytes, smooth muscle and endothelial cells (American Type Culture Collection, Manassas, VA, USA).

    Techniques: Expressing, Transfection, Incubation, Western Blot, Real-time Polymerase Chain Reaction, Control, Negative Control