Journal: bioRxiv

Article Title: Tacrolimus rescues endothelial ALK1 loss-of-function signaling and improves HHT vascular pathology

doi: 10.1101/137737

Figure Lengend Snippet: ( A and B ) AVM number (A) and AVM diameter (B) in the retinal vasculature of P6 pups treated via the transmammary route with BMP9 and BMP10 blocking antibodies [see Methods and Ref. ], and treated with tacrolimus (FK-506, 0.5 mg/kg/d) or vehicle (DMSO). Data represent mean ± s.e.m. per retina ( n = 10-20 pups per group); * P < 0.05; Student’s t -test (A) and Mann Whitney U test (B). ( C-H ) Representative images of retinas stained with fluorescent isolectin B4 from pups treated or not (DMSO) with tacrolimus (FK-506, 0.5 mg/kg/d), and treated via the transmammary route with control IgG2a/b (C and F) or BMP9/10 blocking antibodies (D, E, G, and H). Higher magnifications in (F-H) show retinal vasculature fields (plexus area) between an artery (a) and a vein (v). Arrows in (D) and (G) denote AVMs. ( I ) Scatter plot showing the density of the retinal vascular plexus in pups treated as in (F-H). Data represent mean ± s.e.m. ( n = 6-8); ** P < 0.01, **** P < 0.0001; one-way ANOVA, Tukey’s multiple comparisons test. ( J-O ) Histochemistry analysis of the vascular front of P6 retinas treated as in (C-H) and stained with fluorescent isolectin B4 (J-L, green) and anti-Dll4 antibody (J-O, red). ( P ) Retinal ECs isolated with anti-CD31 microbeads from pups treated as in (A) were analyzed for Id1 mRNA levels by RT-qPCR. The results are expressed as relative levels of the control condition ( n = 3 determinations). ( Q ) Quantification of Dll4 levels in 3 experiments as in (N and O). Data in (P) and (Q) represent mean ± ( n = 3-5); * P < 0.05; Student’s t -test (P) and Mann Whitney U test (Q). Scale bars, 500 μm (C-E), 100 μm (F-H), 30 μm (J-O).

Article Snippet: Briefly, lactating dams were injected i.p. once on P3 with mouse monoclonal isotype control antibodies (15 mg/kg, IgG2b, MAB004; 15 mg/kg, IgG2a, MAB003; R&D Systems) or mouse monoclonal anti-BMP9 and anti-BMP10 antibodies (15 mg/kg, IgG2b, MAB3209; 15 mg/kg, IgG2a, MAB2926; R&D Systems, respectively).

Techniques: Blocking Assay, MANN-WHITNEY, Staining, Control, Isolation, Quantitative RT-PCR

Journal: bioRxiv

Article Title: An angiopoietin-2 vaccine improves arteriovenous malformation pathology in hereditary hemorrhagic telangiectasia mice

doi: 10.1101/2025.10.13.682178

Figure Lengend Snippet: ( A ) Schematic diagram of the vaccination schedule and generation of the BMP9/10ib model. ( B ) Protein sequence alignment of the C-terminal end of human ANG2 (hANG2), mouse ANG2 (mANG2), human ANG1 (hANG1), and mouse ANG1 (mANG1), along with the peptide sequences of ANG2-P3 and ANG1-P3. ( C and D ) Serum antibody titers against ANG2-P3 (C) and ANG1-P3 (D) in ANG2-P3:CRM197-vaccinated females (Vac-1 to Vac-5) and controls [injected with saline (Sal-1 and Sal-2) or CRM197-only (CRM-1 to CRM-5)]. The vaccinated females with the highest anti-ANG2-P3 titers were identified as “best responders” (marked with a red box). OD, optical density.

Article Snippet: After three additional washes with PBST, serial dilutions of individual mouse serum samples were prepared, along with a reference mouse anti-BMP9 antibody (MAB3209, R&D Systems) and a reference mouse anti-BMP10 antibody (MAB2926, R&D Systems), both diluted in 1% BSA PBS.

Techniques: Sequencing, Injection, Saline

Journal: bioRxiv

Article Title: An angiopoietin-2 vaccine improves arteriovenous malformation pathology in hereditary hemorrhagic telangiectasia mice

doi: 10.1101/2025.10.13.682178

Figure Lengend Snippet: ( A ) Serum antibody titers against ANG2-P3 in pups and their corresponding dams vaccinated with ANG2-P3:CRM197 (Vac-1 to Vac-3) or injected with saline (Saline). ( B ) Representative immunofluorescence staining with isolectin B4 (IB4, green) and of α-smooth muscle actin (SMA, red) in P6 retinas of pups treated with PBS or BMP9/10ib, from a dam vaccinated with ANG2-P3:CRM197 or injected with saline. a, artery; v, vein. Scale bar, 1.5 mm. ( C and D) AVM count per retina (C) and retinal AVM surface area (D) in BMP9/10ib pups from dams vaccinated with ANG2-P3:CRM197 or injected with saline (Saline). ( E ) Spearman’s rank correlation matrix of the indicated variables. ( F-H ) retinal artery diameter (F), retinal vein diameter (G), and SMA coverage area (H) in BMP9/10ib pups from dams vaccinated with ANG2-P3:CRM197 or injected with saline (Saline). Data are shown as meanLJ±LJs.e.m.; unpaired t-test with Welch’s correction (C), Mann-Whitney test (D), and one-way ANOVA with Tukey’s multiple comparisons test (F-H). ns, not significant; * P < 0.05; *** P ≤ 0.001; **** P < 0.0001.

Article Snippet: After three additional washes with PBST, serial dilutions of individual mouse serum samples were prepared, along with a reference mouse anti-BMP9 antibody (MAB3209, R&D Systems) and a reference mouse anti-BMP10 antibody (MAB2926, R&D Systems), both diluted in 1% BSA PBS.

Techniques: Injection, Saline, Immunofluorescence, Staining, MANN-WHITNEY

Journal: EMBO Reports

Article Title: Novel role of bone morphogenetic protein 9 in innate host responses to HCMV infection

doi: 10.1038/s44319-024-00072-2

Figure Lengend Snippet: ( A ) Relative transcript levels of type I (ALK1, ALK2, ALK3, ALK6) and type II (BMPR2, ACVR2A, ACVR2B) BMP receptors in primary human foreskin fibroblasts (HFF-1) were determined by RT-qPCR. ( B ) Schematic representation of the workflow. After 2 h of serum starvation, HFF-1 were stimulated with IFNβ (5 ng/ml), BMP4 (18 nM), BMP6 (18 nM), BMP9 (3 nM), BMP15 (18 nM), or Activin B (4 nM), followed by either immunoblot analysis 1 h post stimulation or RNA extraction from cell lysates and RT-qPCR 6 h post stimulation. GAPDH transcript levels were used for normalization. ( C ) Immunoblot analysis of HFF-1 upon stimulation to determine phosphorylation levels of respective signaling components. ( D ) Transcript levels of the BMP-responsive genes Id1 and Id3 upon stimulation with the indicated ligands. ( E ) Transcript levels of the ISGs Isg15 , Irf9 , Ifi6 , and Stat2 upon stimulation with the indicated ligands. Data information: ( A , B ) The Experiment was performed two independent times, one representative is shown. ( D , E) The experiment was performed three independent times, one representative is shown. Data are shown as mean ± SD. .

Article Snippet: Recombinant human BMP4 (#314-BP-010), human BMP6 (#507-BP-020), human BMP9 (#3209-BP-010), human BMP15 (#5096-BM-005), human Activin B (#659-AB-005), and the human/mouse anti-BMP9 antibody (#AF3209) were purchased from R&D Systems.

Techniques: Quantitative RT-PCR, Western Blot, RNA Extraction, Phospho-proteomics

Journal: EMBO Reports

Article Title: Novel role of bone morphogenetic protein 9 in innate host responses to HCMV infection

doi: 10.1038/s44319-024-00072-2

Figure Lengend Snippet: ( A ) Presence of type I (ALK1, ALK2, ALK3) and type II (BMPR2) receptors in HFF-1 and 293T was verified by immunoblotting with the respective antibodies. Detection of GAPDH protein served as loading control. ( B ) Relative transcript levels of type I (ALK1, ALK2, ALK3, ALK6) and type II (BMPR2, ACVR2A, ACVR2B) BMP receptors in 293T were determined by RT-qPCR. ( C ) 293T were co-transfected with expression plasmids for the BRE-Luciferase reporter and a Renilla luciferase normalization control (EF1α-Renilla). 24 h post transfection, 293T were either stimulated with BMP9 (3 nM), or BMP9 (3 nM) incubated for 15 min at RT with an α-BMP9 antibody (1 µg/ml or 5 µg/ml) for 16 h, followed by a dual-luciferase assay readout. ( D ) 293T were co-transfected as in ( B ). 24 h post transfection, 293 T were either stimulated with BMP4 (18 nM), BMP6 (18 nM), BMP9 (3 nM), BMP15 (18 nM), or Activin B (4 nM), or with the ligands incubated for 15 min at RT with an α-BMP9 antibody (1 µg/ml) for 16 h, followed by a dual-luciferase assay readout. ( E ) HFF-1 were either mock, DMSO, Ruxolitinib (10 µM) or DMH1 (10 µM) treated for 2 h, followed by stimulation with IFNβ (5 ng/ml) or BMP4 (18 nM) for 2 h. Cells were lysed and lysates were subjected to immunoblot analysis with p-STAT1, STAT1, p-SMAD1/5/9, SMAD1, p-p38, p38, p-p44/42, p44/42, and Calnexin-specific antibodies. Data information: ( A – E ) Experiments were performed two independent times, one representative is shown. Luciferase fold induction was calculated by dividing Renilla-normalized values from stimulated samples by the corresponding values from unstimulated samples.

Article Snippet: Recombinant human BMP4 (#314-BP-010), human BMP6 (#507-BP-020), human BMP9 (#3209-BP-010), human BMP15 (#5096-BM-005), human Activin B (#659-AB-005), and the human/mouse anti-BMP9 antibody (#AF3209) were purchased from R&D Systems.

Techniques: Western Blot, Control, Quantitative RT-PCR, Transfection, Expressing, Luciferase, Incubation

Journal: EMBO Reports

Article Title: Novel role of bone morphogenetic protein 9 in innate host responses to HCMV infection

doi: 10.1038/s44319-024-00072-2

Figure Lengend Snippet: ( A ) Schematic representation of the workflow. After 2 h of serum starvation, HFF-1 were stimulated for 6 h with BMP4 (18 nM), BMP6 (18 nM), BMP9 (3 nM), BMP15 (18 nM), or Activin B (4 nM), or co-stimulated with IFNβ (5 ng/ml), followed by HCMV infection (MOI 0.5) for 16 h. Cells were fixed, nuclei were stained and cells were labeled for HCMV IE1 + cells as a readout for infection. ( B ) HCMV IE1 + cells normalized to total cell numbers and the untreated control (white column) in BMP/Activin stimulated samples (left panel) or with IFNβ co-stimulated samples (right panel). ( C ) HCMV IE1 + cells normalized to total cell numbers in cells pre-stimulated with either low (0.25 nM) or high (3 nM) concentrations of BMP9 (green symbols) or IFNβ co-stimulated with low and high concentrations of BMP9 (beige symbols). ( D ) HFF-1 were infected by centrifugal enhancement with HCMV WT (MOI 0.5) and supernatants of infected cells were collected in 6 h increments. 293T were co-transfected with expression plasmids for the BRE-Luciferase reporter and a Renilla luciferase normalization control. Twenty-four hours post transfection, 293T were either stimulated with supernatants from HCMV-infected cells, or supernatants from HCMV-infected cells incubated for 15 min at RT with an α-BMP9 antibody, for 16 h, followed by a dual-luciferase assay readout. Luciferase fold induction was calculated by dividing Renilla-normalized values from stimulated samples by the corresponding values from unstimulated samples. Data information: ( B ) Experiment was performed three independent times, one representative is shown. ( C , D ) Data are combined from two independent experiments. Student’s t test (unpaired, two-tailed), n.s. not significant, * P < 0.05, ** P < 0.01, *** P < 0.001. Data are shown as mean ± SD. .

Article Snippet: Recombinant human BMP4 (#314-BP-010), human BMP6 (#507-BP-020), human BMP9 (#3209-BP-010), human BMP15 (#5096-BM-005), human Activin B (#659-AB-005), and the human/mouse anti-BMP9 antibody (#AF3209) were purchased from R&D Systems.

Techniques: Infection, Staining, Labeling, Control, Transfection, Expressing, Luciferase, Incubation, Two Tailed Test

Journal: EMBO Reports

Article Title: Novel role of bone morphogenetic protein 9 in innate host responses to HCMV infection

doi: 10.1038/s44319-024-00072-2

Figure Lengend Snippet: ( A ) Schematic representation of the workflow. After 2 h of serum starvation, HFF-1 were stimulated for 6 h with either IFNβ (5 ng/ml) or BMP9 (3 nM) alone, or co-stimulated with IFNβ and BMP9, followed by RNA extraction from cell lysates and RT-qPCR. ( B ) Transcript levels of BMP receptors Acvrl1 (ALK1, type I receptor) and Bmpr2 (type II receptor), which are the main receptors for BMP9, and the BMP-responsive gene Id1 . ( C ) Transcript levels of the ISGs Isg15 , Irf7 , Ifi6 , Irf9 , Stat2 , and Irf1 . ( D ) Transcript levels of the negative regulators Usp18 and Smurf1 . ( E ) HFF-1 were incubated with either Ruxolitinib or DMH1 for 1 h, then stimulated for 6 h with either IFNβ (5 ng/ml) or BMP9 (3 nM) alone, or co-stimulated with IFNβ and BMP9, followed by RNA extraction from cell lysates and RT-qPCR for transcript levels of Id3 , Stat2 , and Irf9 . Data information: ( B – D ) Data are combined from three independent experiments with the exception of Ifi6 transcript levels where three independent experiments were performed and data was combined from two independent experiments. ( E ) The experiment was performed two independent times, one representative is shown. Student’s t test (unpaired, two-tailed), n.s. not significant, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Data are shown as mean ± SD. .

Article Snippet: Recombinant human BMP4 (#314-BP-010), human BMP6 (#507-BP-020), human BMP9 (#3209-BP-010), human BMP15 (#5096-BM-005), human Activin B (#659-AB-005), and the human/mouse anti-BMP9 antibody (#AF3209) were purchased from R&D Systems.

Techniques: RNA Extraction, Quantitative RT-PCR, Incubation, Two Tailed Test

Journal: EMBO Reports

Article Title: Novel role of bone morphogenetic protein 9 in innate host responses to HCMV infection

doi: 10.1038/s44319-024-00072-2

Figure Lengend Snippet: ( A ) After 2 h of serum starvation, HFF-1 were stimulated for either one or 8 h with IFNβ (5 ng/ml) or BMP9 (3 nM) alone, or were co-stimulated with IFNβ and BMP9, followed by cell lysis and immunoblot analysis with antibodies for phospho-STAT1, STAT1, phospho-SMAD1/5/9, and β-Actin. Phospho-STAT1 band intensities were first normalized to corresponding total STAT1 levels, then to IFNβ stimulation only, and are shown below. ( B ) After 2 h of serum starvation, HFF-1 were stimulated for 1 h with either IFNα2 (5 ng/ml), IFNγ (5 ng/ml), or BMP9 (3 nM) alone, or co-stimulated with IFNα2 or IFNγ and BMP9, followed by cell lysis, immunoblot analysis and quantification as in ( A ). ( C ) After 2 h of serum starvation, HFF-1 were stimulated for 6 h with either IFNα2 (5 ng/ml), IFNβ (5 ng/ml), IFNγ (5 ng/ml), or BMP9 (3 nM) alone, or co-stimulated with IFNα2, IFNβ, IFNγ, and BMP9, followed by RNA extraction from cell lysates and RT-qPCR for Irf9 , Stat2 , Irf1 , and Id3 transcripts. Data information: ( A , B ) Experiment was performed three independent times, one representative immunoblot is shown. Quantified data for the STAT1 phosphorylation levels are combined from three independent experiments. ( C ) Data are combined from three independent experiments. Student’s t test (unpaired, two-tailed), n.s. not significant, * P < 0.05, ** P < 0.01, **** P < 0.0001. Data are shown as mean ± SD. .

Article Snippet: Recombinant human BMP4 (#314-BP-010), human BMP6 (#507-BP-020), human BMP9 (#3209-BP-010), human BMP15 (#5096-BM-005), human Activin B (#659-AB-005), and the human/mouse anti-BMP9 antibody (#AF3209) were purchased from R&D Systems.

Techniques: Lysis, Western Blot, RNA Extraction, Quantitative RT-PCR, Phospho-proteomics, Two Tailed Test

Journal: EMBO Reports

Article Title: Novel role of bone morphogenetic protein 9 in innate host responses to HCMV infection

doi: 10.1038/s44319-024-00072-2

Figure Lengend Snippet: ( A ) 293T were co-transfected with expression plasmids for empty vector (EV) or V5-tagged US18, US20, or M27 (a known inhibitor of IFNAR signaling), together with either a BRE-Luciferase or MX1-Luciferase reporter and a Renilla luciferase normalization control. Twenty-four hours post transfection, 293T were stimulated for 16 h with either IFNβ (5 ng/ml) or BMP9 (3 nM) alone, co-stimulated with IFNβ and BMP9, or left unstimulated, followed by cell lysis and a Dual-luciferase assay readout. ( B ) Results from the Dual-luciferase assay with the BRE-Luciferase (top panel) and MX1-Luciferase (bottom panel) reporter. ( C ) Cell lysates from ( B ) were analyzed by immunoblot for the expression of M27, US18 and US20 with a V5-specific antibody, β-Actin served as loading control. ( D ) 293T were co-transfected with expression plasmids for the BRE-Luciferase and Renilla reporters as in ( A ), together with V5-tagged US18, US20 or co-transfected with US18 and US20 in combination. 24 h post transfection 293 T were stimulated for 16 h with BMP9 (3 nM), or left unstimulated, followed by cell lysis and a Dual-luciferase assay readout. ( E ) 293T were co-transfected with expression plasmids for either Cherry-STING and cGAS-GFP (left panel), RIG-I N (middle panel), or IRF3-5D (a constitutively activate IRF3 mutant; right panel), together with the murine IFNβ-luciferase reporter (IFNβ-Luc) and the Renilla reporter as normalization control. Cells were additionally transfected with expression plasmids for EV, V5-tagged M35 (a known inhibitor of PRR-mediated signaling pathways, (Chan et al, ), US18 or US20. Twenty hours post-transfection, cells were lysed and a dual-luciferase assay was performed. Immunoblot analysis of cell lysates from the respective experiments for M35, US18, and US20 detected with a V5-specific antibody, and β-Actin as a loading control, are shown below. Data information: ( B – E ) Data are combined from three independent experiments, for the immunoblots one representative is shown. Student’s t test (unpaired, two-tailed), n.s. not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Data are shown as mean ± SD. Luciferase fold induction was calculated by dividing Renilla-normalized values from stimulated samples by the corresponding values from unstimulated samples. .

Article Snippet: Recombinant human BMP4 (#314-BP-010), human BMP6 (#507-BP-020), human BMP9 (#3209-BP-010), human BMP15 (#5096-BM-005), human Activin B (#659-AB-005), and the human/mouse anti-BMP9 antibody (#AF3209) were purchased from R&D Systems.

Techniques: Transfection, Expressing, Plasmid Preparation, Luciferase, Control, Lysis, Western Blot, Mutagenesis, Protein-Protein interactions, Two Tailed Test

Journal: EMBO Reports

Article Title: Novel role of bone morphogenetic protein 9 in innate host responses to HCMV infection

doi: 10.1038/s44319-024-00072-2

Figure Lengend Snippet: ( A ) HFF-1 with doxycycline-inducible expression of US18-V5, US20-HA, or US18-V5 and US20-HA with corresponding control cell lines (EV1, EV2, EV1 + 2) were generated. Protein expression was induced with 1 µg/ml doxycycline for 20 h prior stimulation and verified by immunoblot with V5- and HA-specific antibodies, and β-Actin as a loading control. ( B ) HFF-1 US18-V5, HFF-1 US20-HA, or HFF-1 US18-V5 US20-HA were left untreated or protein expression was induced with 1 µg/ml doxycycline to the medium for 20 h. Cell lysates were either left untreated or treated with PNGase F for 3 h at 37 °C, followed by immunoblot analysis with V5-, HA-, and Calnexin-specific antibodies. ( C , D ) Indicated HFF-1 lines were treated with 1 µg/ml doxycycline to induce protein expression for 18 h, followed by 2 h of serum starvation. ( C ) Cells were stimulated for 1 h with BMP9 (3 nM), followed by cell lysis and immunoblot analysis with phospho-SMAD1/5/9, SMAD1, V5, HA, and Calnexin antibodies. ( D ) Cells were stimulated for 6 h with either IFNβ (5 ng/ml) or BMP9 (3 nM) alone, or co-stimulated with IFNβ and BMP9, followed by RNA extraction from cell lysates and RT-qPCR for Id3 and Stat2 transcripts. Data information: ( A – C ) Experiment was performed three independent times, one representative is shown. ( D ) Data are combined from three independent experiments. Student’s t test (unpaired, two-tailed), n.s. not significant, * P < 0.05, ** P < 0.01. Data are shown as mean ± SD. .

Article Snippet: Recombinant human BMP4 (#314-BP-010), human BMP6 (#507-BP-020), human BMP9 (#3209-BP-010), human BMP15 (#5096-BM-005), human Activin B (#659-AB-005), and the human/mouse anti-BMP9 antibody (#AF3209) were purchased from R&D Systems.

Techniques: Expressing, Control, Generated, Western Blot, Lysis, RNA Extraction, Quantitative RT-PCR, Two Tailed Test

Journal: EMBO Reports

Article Title: Novel role of bone morphogenetic protein 9 in innate host responses to HCMV infection

doi: 10.1038/s44319-024-00072-2

Figure Lengend Snippet: ( A ) Schematic representation of the workflow. Recombinant HCMV US18stop, HCMV US20stop, and HCMV US18/20stop were constructed by introducing a 16 base pair (bp) stop cassette within the respective coding region. HFF-1 were infected by centrifugal enhancement with HCMV WT, HCMV US18stop, HCMV US20stop, or HCMV US18/20stop (MOI 4 for the 3 h time point, MOI 0.5 for the 48 h time point). Three or 48 h post infection, cells were stimulated with BMP9 (3 nM) for (1) 2 h, followed by cell lysis and immunoblot analysis, or (2) 6 h, followed by RNA extraction from cell lysates and RT-qPCR. ( B , C ) Cell lysates from ( A ) were subjected to immunoblot analysis with p-SMAD1/5/9, SMAD1, HCMV UL35, and GAPDH-specific antibodies (top panel), and transcript levels of Id3 and Stat2 are shown below. Data information: ( B , C ) Data are combined from three independent experiments. Student’s t test (unpaired, two-tailed), n.s. not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Data are shown as mean ± SD. .

Article Snippet: Recombinant human BMP4 (#314-BP-010), human BMP6 (#507-BP-020), human BMP9 (#3209-BP-010), human BMP15 (#5096-BM-005), human Activin B (#659-AB-005), and the human/mouse anti-BMP9 antibody (#AF3209) were purchased from R&D Systems.

Techniques: Recombinant, Construct, Infection, Lysis, Western Blot, RNA Extraction, Quantitative RT-PCR, Two Tailed Test

Journal: EMBO Reports

Article Title: Novel role of bone morphogenetic protein 9 in innate host responses to HCMV infection

doi: 10.1038/s44319-024-00072-2

Figure Lengend Snippet: ( A ) HFF-1 were infected by centrifugal enhancement with HCMV WT or HCMV US18/20stop (MOI 4). Three hours post infection, cells were stimulated with IFNβ (1 ng/ml) or BMP9 (3 nM) alone, or co-stimulated with IFNβ and BMP9 for 6 h, followed by RNA extraction from cell lysates and RT-qPCR. ( B – D ) Transcript levels of Id3 ( B ), the ISGs Irf9 and Stat2 ( C ), and HCMV transcripts HCMV IE1 and HCMV UL44 ( D ). Data information: Three independent experiments with similar results were performed and data shown is combined from two of the three independent experiments. Student’s t test (unpaired, two-tailed), n.s. not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Data are shown as mean ± SD. .

Article Snippet: Recombinant human BMP4 (#314-BP-010), human BMP6 (#507-BP-020), human BMP9 (#3209-BP-010), human BMP15 (#5096-BM-005), human Activin B (#659-AB-005), and the human/mouse anti-BMP9 antibody (#AF3209) were purchased from R&D Systems.

Techniques: Infection, RNA Extraction, Quantitative RT-PCR, Two Tailed Test

Journal: Biochimica et biophysica acta. Molecular basis of disease

Article Title: Targeting secreted cytokine BMP9 gates the attenuation of hepatic fibrosis.

doi: 10.1016/j.bbadis.2017.12.008

Figure Lengend Snippet: Figure 1 BMP9 is overexpressed in human patients

Article Snippet: IHC staining Liver slides were labeled with a monoclonal antibody against mouse BMP9 (Abcam, UK) using a BOND-MAX IHC and ISH staining system (Leica, Buffalo Grove, USA) at the Department of Pathology of Shanghai Ninth People’s Hospital (Shanghai, China)[29].

Techniques:

Journal: Biochimica et biophysica acta. Molecular basis of disease

Article Title: Targeting secreted cytokine BMP9 gates the attenuation of hepatic fibrosis.

doi: 10.1016/j.bbadis.2017.12.008

Figure Lengend Snippet: Figure 3 Adenovirus-mediated Bmp9 knockdown attenuates liver fibrosis

Article Snippet: IHC staining Liver slides were labeled with a monoclonal antibody against mouse BMP9 (Abcam, UK) using a BOND-MAX IHC and ISH staining system (Leica, Buffalo Grove, USA) at the Department of Pathology of Shanghai Ninth People’s Hospital (Shanghai, China)[29].

Techniques: Knockdown