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bmp6 (R&D Systems)

Name: bmp6
Brand: R&D Systems
Rating: 95 (158 reviews)

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R&D Systems bmp6
Bmp6, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 158 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/bmp6/product/R&D Systems
Average 95 stars, based on 158 article reviews

bmp6 - by Bioz Stars, 2026-02

95/100 stars

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( 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. .

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

( 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.

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.

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

( 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. .

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. .

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

Effects of 5 different BMPs on the osteogenic differentiation of hMDSCs at day 28 (3D pellet culture). A. MicroCT 3D images showed that the mineralized pellets in 5 BMPs groups were larger than the CTL group. Scale bar=1mm. B. Quantification of mineralized pellet volume. All BMPs groups showed higher mineralized pellet volume compared to the CTL group. The mineralized pellet volume of the BMP2 group was significantly higher than the BMP6 and BMP7 groups. *P<0.05, ** P<0.01, ****, P<0.0001. C. Mineralized pellet density quantification. No statistical difference between BMP groups and the CTL group was found. D. Von Kossa staining. Brown-black color indicates mineralization. All pellets have regions peeled off due to high mineralization in the white region of pellets. E. Immunohistochemistry of osteocalcin for osteogenic pellets. Brown color indicates osteocalcin expression. The mineralized parts of the pellets demonstrate crystal purple color intermingled with osteocalcin brown staining. Scale bars=100μm.

Journal: Biomaterials

Article Title: The use of heparin/polycation coacervate sustain release system to compare the bone regenerative potentials of 5 BMPs using a critical sized calvarial bone defect model

doi: 10.1016/j.biomaterials.2022.121708

Figure Lengend Snippet: Effects of 5 different BMPs on the osteogenic differentiation of hMDSCs at day 28 (3D pellet culture). A. MicroCT 3D images showed that the mineralized pellets in 5 BMPs groups were larger than the CTL group. Scale bar=1mm. B. Quantification of mineralized pellet volume. All BMPs groups showed higher mineralized pellet volume compared to the CTL group. The mineralized pellet volume of the BMP2 group was significantly higher than the BMP6 and BMP7 groups. *P<0.05, ** P<0.01, ****, P<0.0001. C. Mineralized pellet density quantification. No statistical difference between BMP groups and the CTL group was found. D. Von Kossa staining. Brown-black color indicates mineralization. All pellets have regions peeled off due to high mineralization in the white region of pellets. E. Immunohistochemistry of osteocalcin for osteogenic pellets. Brown color indicates osteocalcin expression. The mineralized parts of the pellets demonstrate crystal purple color intermingled with osteocalcin brown staining. Scale bars=100μm.

Article Snippet: These included: recombinant human/mouse/rat BMP2 (R&D system, 355-BM-050), recombinant human BMP4 (R&D system, 314-BP-050), recombinant human BMP6 (R&D system, 507-BP, Lot: CTC3816011), recombinant human BMP7 (R&D system, 354-BP-010), and recombinant human BMP9 (R&D system, 3209-BP-010).

Techniques: Staining, Immunohistochemistry, Expressing

Journal: Biomaterials

Article Title: The use of heparin/polycation coacervate sustain release system to compare the bone regenerative potentials of 5 BMPs using a critical sized calvarial bone defect model

doi: 10.1016/j.biomaterials.2022.121708

Figure Lengend Snippet: Coacervate sustained release BMPs kinetics. A. BMP2 release profile. The cumulative release of total loaded protein reached 0.7% at day 15. B. BMP4 release profile: The cumulative release at day 15 reached ~0.7%. C. BMP6 release profile: The cumulative release rate reached 0.6% at day 15. D. BMP7 release profile: The cumulative release of total loaded protein was 3.2% at day 15. E. BMP9 release profile: The cumulative release of total loaded protein reached 5.2%.

Techniques:

Journal: Biomaterials

Article Title: The use of heparin/polycation coacervate sustain release system to compare the bone regenerative potentials of 5 BMPs using a critical sized calvarial bone defect model

doi: 10.1016/j.biomaterials.2022.121708

Figure Lengend Snippet: loading efficiency of different BMPs

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