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bmpr ii (R&D Systems)

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R&D Systems bmpr ii

Figure 6. Receptor expressions <t>of</t> <t>ALK2,</t> ALK4, ALK6, ALK5, ALK7, <t>BMPR-II</t> in pASC. Grouped representation of the respective receptor expression in the course of osteogenic differentiation (OM +/−BMP-2). From day 19, there is a significant induction of ALK 2, ALK 6, and ALK 5 with the addition of BMP-2. BMPR-II expression in the OM group decreased in OM and tended to stay increased under BMP-2 supplementation from day 19, but was not considered significant (* p ≤0.05, ** p ≤0.01; n = 6, BMP-2 450 ng/mL).

Bmpr Ii, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/antibody+af811/Human+BMPR-II+Antibody/pm40563862-64-40-45
Average 93 stars, based on 26 article reviews

bmpr ii - by Bioz Stars, 2026-09

93/100 stars

Images

1) Product Images from "BMP-2-Driven Osteogenesis: A Comparative Analysis of Porcine BMSCs and ASCs and the Role of TGF-β and FGF Signaling."

Article Title: BMP-2-Driven Osteogenesis: A Comparative Analysis of Porcine BMSCs and ASCs and the Role of TGF-β and FGF Signaling.

Journal: Biology

doi: 10.3390/biology14060610

Figure 6. Receptor expressions of ALK2, ALK4, ALK6, ALK5, ALK7, BMPR-II in pASC. Grouped representation of the respective receptor expression in the course of osteogenic differentiation (OM +/−BMP-2). From day 19, there is a significant induction of ALK 2, ALK 6, and ALK 5 with the addition of BMP-2. BMPR-II expression in the OM group decreased in OM and tended to stay increased under BMP-2 supplementation from day 19, but was not considered significant (* p ≤0.05, ** p ≤0.01; n = 6, BMP-2 450 ng/mL).

Figure Legend Snippet: Figure 6. Receptor expressions of ALK2, ALK4, ALK6, ALK5, ALK7, BMPR-II in pASC. Grouped representation of the respective receptor expression in the course of osteogenic differentiation (OM +/−BMP-2). From day 19, there is a significant induction of ALK 2, ALK 6, and ALK 5 with the addition of BMP-2. BMPR-II expression in the OM group decreased in OM and tended to stay increased under BMP-2 supplementation from day 19, but was not considered significant (* p ≤0.05, ** p ≤0.01; n = 6, BMP-2 450 ng/mL).

Techniques Used: Expressing

Western Blot:

Article Title: Identification of a common Wnt-associated genetic signature across multiple cell types in pulmonary arterial hypertension
Article Snippet: .. Western blot analysis was performed to evaluate the levels of BMPR2 protein expression in cells exposed to the primary antibody AF811 (R & D Systems, Minneapolis, MN) for 1 h and the secondary antibody 111-035-003 (Jackson ImmunoResearch, West Grove, PA). table ft1 table-wrap mode=article t1 Table 1. caption a4 Characterization of patient samples iPS cell reprogramming and characterization. .. To study the primary effects of BMPR2 mutation without concern for the pressure- or flow-mediated changes in vascular cell function (or other in vivo milieu variables), transgene-free iPS cells were generated from a control patient with no known BMPR2 mutation (WT) and a HPAH patient with a known BMPR2 mutation (BMPR2mut iPS) using the excisable polycistronic lentiviral vector (EF1a-hSTEMCCA-loxP) encoding the four reprogramming factors (Oct3/4, Sox2, Klf4, and c-Myc), as described elsewhere ( 60 ).

Article Title: Role of BMPR2 Alternative Splicing in HPAH Penetrance
Article Snippet: .. 34 , 35 Western blot (WB) analysis Membranes were probed with primary antibody AF811 (R&D Systems Inc., Minneapolis, MN) for 1 hour and with secondary antibody 111-035-003 (Jackson ImmunoResearch, West Grove, PA) for an additional hour. .. Detection was done using the Immobilon Chemiluminescent HRP substrate (Millipore, Billerica, Massachusetts). β-Actin was used as a loading control.

Article Title: Transcripts from a novel BMPR2 termination mutation escape nonsense mediated decay by downstream translation re-initiation: implications for treating pulmonary hypertension
Article Snippet: Samples were then analyzed by capillary electrophoresis using a 3100 Genetic Analyzer (Applied Biosystems). .. Western blot analysis Membranes were probed with primary antibody AF811 (R&D Systems Inc., Minneapolis, MN) for 1 h and with secondary antibody 111-035-003 (Jackson ImmunoResearch, West Grove, PA) for an additional 1 h. Detection was done using the Immobilon Chemiluminescent HRP substrate (Millipore, Billerica, MA). β -Actin was used as a loading control. .. For BMPR-II signaling analysis we used phospho-Smad1/Smad5/Smad8 antibody #9511 and Smad1 antibody #9743 (both from Cell Signaling Technology).

Article Title: Identification of a common Wnt-associated genetic signature across multiple cell types in pulmonary arterial hypertension
Article Snippet: .. Western blot analysis was performed to evaluate the levels of BMPR2 protein expression in cells exposed to the primary antibody AF811 (R & D Systems, Minneapolis, MN) for 1 h and the secondary antibody 111-035-003 (Jackson ImmunoResearch, West Grove, PA). table ft1 table-wrap mode=article t1 Table 1. caption a4 Characterization of patient samples .. To study the primary effects of BMPR2 mutation without concern for the pressure- or flow-mediated changes in vascular cell function (or other in vivo milieu variables), transgene-free iPS cells were generated from a control patient with no known BMPR2 mutation (WT) and a HPAH patient with a known BMPR2 mutation (BMPR2mut iPS) using the excisable polycistronic lentiviral vector (EF1a-hSTEMCCA-loxP) encoding the four reprogramming factors (Oct3/4, Sox2, Klf4, and c-Myc), as described elsewhere ( 60 ).

Expressing:

Article Title: Identification of a common Wnt-associated genetic signature across multiple cell types in pulmonary arterial hypertension
Article Snippet: .. Western blot analysis was performed to evaluate the levels of BMPR2 protein expression in cells exposed to the primary antibody AF811 (R & D Systems, Minneapolis, MN) for 1 h and the secondary antibody 111-035-003 (Jackson ImmunoResearch, West Grove, PA). table ft1 table-wrap mode=article t1 Table 1. caption a4 Characterization of patient samples .. To study the primary effects of BMPR2 mutation without concern for the pressure- or flow-mediated changes in vascular cell function (or other in vivo milieu variables), transgene-free iPS cells were generated from a control patient with no known BMPR2 mutation (WT) and a HPAH patient with a known BMPR2 mutation (BMPR2mut iPS) using the excisable polycistronic lentiviral vector (EF1a-hSTEMCCA-loxP) encoding the four reprogramming factors (Oct3/4, Sox2, Klf4, and c-Myc), as described elsewhere ( 60 ).

Control:

Article Title: Transcripts from a novel BMPR2 termination mutation escape nonsense mediated decay by downstream translation re-initiation: implications for treating pulmonary hypertension
Article Snippet: Samples were then analyzed by capillary electrophoresis using a 3100 Genetic Analyzer (Applied Biosystems). .. Membranes were probed with primary antibody AF811 (R&D Systems Inc., Minneapolis, MN) for 1 h and with secondary antibody 111-035-003 (Jackson ImmunoResearch, West Grove, PA) for an additional 1 h. Detection was done using the Immobilon Chemiluminescent HRP substrate (Millipore, Billerica, MA). β -Actin was used as a loading control. .. For BMPR-II signaling analysis we used phospho-Smad1/Smad5/Smad8 antibody #9511 and Smad1 antibody #9743 (both from Cell Signaling Technology).

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Journal: Biology

Article Title: BMP-2-Driven Osteogenesis: A Comparative Analysis of Porcine BMSCs and ASCs and the Role of TGF-β and FGF Signaling.

doi: 10.3390/biology14060610

Figure Lengend Snippet: Figure 6. Receptor expressions of ALK2, ALK4, ALK6, ALK5, ALK7, BMPR-II in pASC. Grouped representation of the respective receptor expression in the course of osteogenic differentiation (OM +/−BMP-2). From day 19, there is a significant induction of ALK 2, ALK 6, and ALK 5 with the addition of BMP-2. BMPR-II expression in the OM group decreased in OM and tended to stay increased under BMP-2 supplementation from day 19, but was not considered significant (* p ≤0.05, ** p ≤0.01; n = 6, BMP-2 450 ng/mL).

Article Snippet: The respective conjugated antibodies were used for the expressions of ALK3 (Cat. No.: AF436), ALK 5 (Cat. No.: FAB5871), ALK6 (Cat. No.: FAB5051A), TGF-β2-RII (Cat. No.: FAB532P), ALK7 (Cat. No.: FAB77491A), ALK2 (Cat. No.: AF637), ALK4 (Cat. No.: MAB2221), and BMPR-II (Cat. No.: AF811) (by R&D Systems, Minneapolis, MN, USA), and the pASCs and pBMSCs were compared for their expressions of the specific surface antigens CD45 (Cat. No.: MCA1568GA, BioRad, Hercules, CA, USA), HLA-DR (human leukocyte antigen–antigen D-related surface molecule) (Cat. No.: MCA2314F, Bio-Rad, Hercules, CA, USA), CD29 (Cat. No.: 561,496, BD Pharmingen, Franklin Lakes, NJ, USA), CD79alpha (Bio-Rad, Cat. No.: MCA2538GA), CD14 (Cat. No.: MCA1568GA, Bio-Rad, Hercules, CA, USA), CD31 (Cat. No.: AF3387, R&D Systems, Minneapolis, MN, USA), CD105 (Cat. No.: NB110-58718APC, Novus Biologicals, Minneapolis, MN, USA), CD26 (, Cat. No.: NB600-552APC, Novus Biologicals, Minneapolis, MN, USA), CD73 (, Cat. No.: AF4488, R&D Systems, Minneapolis, MN, USA), CD90 (Cat. No.: 559,869, BD Pharmingen, Franklin Lakes, NJ, USA), CD34 (Cat. No.: 81289, abcam, Cambridge, UK), and CD44 (Cat. No.: 5531, BD Pharmingen, Franklin Lakes, NJ, USA).

Techniques: Expressing

miR-100-3p targets to the BMPR2. a , b qRT-PCR showed the expression of BMPR2 after transfection of miR-100-3p mimic or inhibitor. c Western blot indicated the protein expression of BMPR2 after miR-100-3p overexpression or inhibition. (D) Conserved binding site of BMPR2 and miR-100-3p. e Luciferase activity assay confirmed the interaction between BMPR2 and miR-100-3p (**p < 0.01, ****p < 0.001)

Journal: Cancer Cell International

Article Title: miR-100-3p inhibits cell proliferation and induces apoptosis in human gastric cancer through targeting to BMPR2

doi: 10.1186/s12935-019-1060-2

Figure Lengend Snippet: miR-100-3p targets to the BMPR2. a , b qRT-PCR showed the expression of BMPR2 after transfection of miR-100-3p mimic or inhibitor. c Western blot indicated the protein expression of BMPR2 after miR-100-3p overexpression or inhibition. (D) Conserved binding site of BMPR2 and miR-100-3p. e Luciferase activity assay confirmed the interaction between BMPR2 and miR-100-3p (**p < 0.01, ****p < 0.001)

Article Snippet: The following antibodies were purchased from Cell Signaling Technology, Proteintech or AbcamThe antibodies used in this study were following: BMPR2 (CST, 6979); BMPR2 (R&D, AF811-SP); p-smad1/5/9 (CST, 13820); smad1/5/9 (Abcam, ab66737); caspase 3 (CST, 9662); bax (CST, 5023); bcl-2 (CST, 15071); p-Erk1/2 (CST, 4377); Erk1/2 (CST catalogue no., 4696); p-AKT (CST, 5012); AKT (CST, 2920); β-actin (Proteintech, 66009-1-Ig); anti-goat HRP-DAB Cell & Tissue Staining Kit (Brown, CTS008).

Techniques: Quantitative RT-PCR, Expressing, Transfection, Western Blot, Over Expression, Inhibition, Binding Assay, Luciferase, Activity Assay

BMPR2 was up-regulated in most of the fresh specimens from GC patients; higher expression BMPR2 has lower survival. a 42 cases of fresh GC and corresponding normal tissues; b the BMPR2 mRNA expression level is correlation with the pathological type of GC, the worse the differentiation, the high the expression level. GADPH was used as an internal control. c Higher expression BMPR2 has lower survival (*p < 0.05 ** p < 0.01)

Journal: Cancer Cell International

Article Title: miR-100-3p inhibits cell proliferation and induces apoptosis in human gastric cancer through targeting to BMPR2

doi: 10.1186/s12935-019-1060-2

Figure Lengend Snippet: BMPR2 was up-regulated in most of the fresh specimens from GC patients; higher expression BMPR2 has lower survival. a 42 cases of fresh GC and corresponding normal tissues; b the BMPR2 mRNA expression level is correlation with the pathological type of GC, the worse the differentiation, the high the expression level. GADPH was used as an internal control. c Higher expression BMPR2 has lower survival (*p < 0.05 ** p < 0.01)

Techniques: Expressing, Control

miR-100-3p functioned through BMPR2 in inhibiting Smad1/5/9、ERK-AKT and Bcl-2 signaling. a Western blotting for Smad1/5/9, p-smad1/5/9, Bcl-2, Bax, Caspase3, ERK1/2, p-EKR1/2, AKT and p-AK in AGS cells transfected with Lv-miR-100-3p mimic-control (Lv-miR-100-3p mimic-ctrl) and over-expression BMPR2 plasmid control(over-expression BMPR2 control-ctrl), Lv-miR-100-3p mimic-ctrl and over-expression BMPR2 plasmid, Lv-miR-100-3p mimic and over-expression BMPR2-ctrl, or Lv-miR-100-3p mimic and over-expression BMPR2 plasmid. b MGC-803 cells transfected with Lv-miR-100-3p inhibitor-control (inhibitor-ctrl) and BMPR2 shRNA control (shRNA-ctrl), Lv-miR-100-3p inhibitor-ctrl and BMPR2 shRNA, Lv-miR-100-3p inhibitor and BMPR2 shRNA-ctrl, or Lv-miR-100-3p inhibitor and BMPR2 shRNA. Protein expression was quantified by band intensity and normalized to β-actin. **p < 0.01

Journal: Cancer Cell International

Article Title: miR-100-3p inhibits cell proliferation and induces apoptosis in human gastric cancer through targeting to BMPR2

doi: 10.1186/s12935-019-1060-2

Figure Lengend Snippet: miR-100-3p functioned through BMPR2 in inhibiting Smad1/5/9、ERK-AKT and Bcl-2 signaling. a Western blotting for Smad1/5/9, p-smad1/5/9, Bcl-2, Bax, Caspase3, ERK1/2, p-EKR1/2, AKT and p-AK in AGS cells transfected with Lv-miR-100-3p mimic-control (Lv-miR-100-3p mimic-ctrl) and over-expression BMPR2 plasmid control(over-expression BMPR2 control-ctrl), Lv-miR-100-3p mimic-ctrl and over-expression BMPR2 plasmid, Lv-miR-100-3p mimic and over-expression BMPR2-ctrl, or Lv-miR-100-3p mimic and over-expression BMPR2 plasmid. b MGC-803 cells transfected with Lv-miR-100-3p inhibitor-control (inhibitor-ctrl) and BMPR2 shRNA control (shRNA-ctrl), Lv-miR-100-3p inhibitor-ctrl and BMPR2 shRNA, Lv-miR-100-3p inhibitor and BMPR2 shRNA-ctrl, or Lv-miR-100-3p inhibitor and BMPR2 shRNA. Protein expression was quantified by band intensity and normalized to β-actin. **p < 0.01

Techniques: Western Blot, Transfection, Control, Over Expression, Plasmid Preparation, shRNA, Expressing

Knockdown of BMPR2 expression neutralized the effect of the miR-100-3p inhibitor; also over-expression of BMPR2 neutralized the effect of the miR-100-3p over-expression. BMPR2 reversed the effect induced by miR-100-3p dysregulation. a , b Proliferation of AGS cells transfected with Lv-miR-100-3p mimic-control (Lv-miR-100-3p mimic-ctrl) and over-expression BMPR2 plasmid control (over-expression BMPR2 control-ctrl), Lv-miR-100-3p mimic-ctrl and over-expression BMPR2 plasmid, Lv-miR-100-3p mimic and over-expression BMPR2-ctrl, or Lv-miR-100-3p mimic and over-expression BMPR2 plasmid. MGC-803 cells transfected with Lv-miR-100-3p inhibitor-control (inhibitor-ctrl) and BMPR2 shRNA control (shRNA-ctrl), Lv-miR-100-3p inhibitor-ctrl and BMPR2 shRNA, Lv-miR-100-3p inhibitor and BMPR2 shRNA-ctrl, or Lv-miR-100-3p inhibitor and BMPR2 shRNA was examined by MTT assay c , d Flow analysis revealed the apoptosis of AGS and MGC-803 cells with or without DDP supplementation (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001)

Journal: Cancer Cell International

Article Title: miR-100-3p inhibits cell proliferation and induces apoptosis in human gastric cancer through targeting to BMPR2

doi: 10.1186/s12935-019-1060-2

Figure Lengend Snippet: Knockdown of BMPR2 expression neutralized the effect of the miR-100-3p inhibitor; also over-expression of BMPR2 neutralized the effect of the miR-100-3p over-expression. BMPR2 reversed the effect induced by miR-100-3p dysregulation. a , b Proliferation of AGS cells transfected with Lv-miR-100-3p mimic-control (Lv-miR-100-3p mimic-ctrl) and over-expression BMPR2 plasmid control (over-expression BMPR2 control-ctrl), Lv-miR-100-3p mimic-ctrl and over-expression BMPR2 plasmid, Lv-miR-100-3p mimic and over-expression BMPR2-ctrl, or Lv-miR-100-3p mimic and over-expression BMPR2 plasmid. MGC-803 cells transfected with Lv-miR-100-3p inhibitor-control (inhibitor-ctrl) and BMPR2 shRNA control (shRNA-ctrl), Lv-miR-100-3p inhibitor-ctrl and BMPR2 shRNA, Lv-miR-100-3p inhibitor and BMPR2 shRNA-ctrl, or Lv-miR-100-3p inhibitor and BMPR2 shRNA was examined by MTT assay c , d Flow analysis revealed the apoptosis of AGS and MGC-803 cells with or without DDP supplementation (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001)

Techniques: Knockdown, Expressing, Over Expression, Transfection, Control, Plasmid Preparation, shRNA, MTT Assay

miR-100-3p inhibited tumor growth through BMPR2 in vivo. a , b represented figure indicated the tumor growth after miR-100 overexpresison or inhibition. c , d immune staining indicated the expression of BMPR2 and Ki-67, scale bar = 200 μm

Journal: Cancer Cell International

Article Title: miR-100-3p inhibits cell proliferation and induces apoptosis in human gastric cancer through targeting to BMPR2

doi: 10.1186/s12935-019-1060-2

Figure Lengend Snippet: miR-100-3p inhibited tumor growth through BMPR2 in vivo. a , b represented figure indicated the tumor growth after miR-100 overexpresison or inhibition. c , d immune staining indicated the expression of BMPR2 and Ki-67, scale bar = 200 μm

Techniques: In Vivo, Inhibition, Staining, Expressing

Review

bmpr ii (R&D Systems)

Structured Review

Images

1) Product Images from "BMP-2-Driven Osteogenesis: A Comparative Analysis of Porcine BMSCs and ASCs and the Role of TGF-β and FGF Signaling."

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