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bmp2  (R&D Systems)


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    Structured Review

    R&D Systems bmp2
    Bmp2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 96/100, based on 227 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+bmp2/Recombinant+Human%2FMouse%2FRat+BMP-2+Protein/pm42822563-95-0-12
    Average 96 stars, based on 227 article reviews
    bmp2 - by Bioz Stars, 2026-11
    96/100 stars

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    Related Articles

    Enzyme-linked Immunosorbent Assay:

    Article Title: Nanotopography Influences Host-Pathogen Quorum Sensing and Facilitates Selection of Bioactive Metabolites in Mesenchymal Stromal Cells and Pseudomonas aeruginosa Co-Cultures.
    Article Snippet: .. FN and BMP2 levels in the supernatants were calculated using enzyme-linked immunosorbent assay (ELISA) duo-set Human Fibronectin (DY1918, R&D systems), and Human BMP2 (DY355, R&D systems), respectively, following instructions from the manufacturer. ..

    Article Title: Nanotopography Influences Host–Pathogen Quorum Sensing and Facilitates Selection of Bioactive Metabolites in Mesenchymal Stromal Cells and Pseudomonas aeruginosa Co-Cultures
    Article Snippet: .. FN and BMP2 levels in the supernatants were calculated using enzyme-linked immunosorbent assay (ELISA) duo-set Human Fibronectin (DY1918, R&D systems), and Human BMP2 (DY355, R&D systems), respectively, following instructions from the manufacturer. ..

    Binding Assay:

    Article Title: Anti-GDF15 antibodies, compositions and methods of use
    Article Snippet: .. An OctetRED 384 (ForteBio, Menlo Park, Calif.) was used to evaluate off-target binding of monomeric GDF15_001 (CH23LS-GBT-GDF15_001) to ten TGFβ family members including human GDNF (R&D, 212-GD/CF), human Inhibin A (R&D, 8506-AB/CF), human Activin B (R&D, 659-AB/CF) human TGFβ-1 (R&D, 240-B/CF) human BMP2 (R&D, 355-BM/CF), human BMP3b (R&D, 1543-BP/CF), human BMP6 (R&D, 507-BP/CF), human BMP9 (R&D, 3209-BP/CF), human BMP11 (R&D, 1958-CD/CF), human GDF8 (Pfizer, 41075-201) and control human GDF15 (Mu IgG1Fc_Fxa_Hu GDF15). .. The TGFβ family members were diluted to 10 ug/ml in 10 mM Sodium Acetate pH 4.5 and amine coupled onto AR2G biosensors (catalogue #18-5092, ForteBio) according to the manufacturer's instructions.

    Control:

    Article Title: Anti-GDF15 antibodies, compositions and methods of use
    Article Snippet: .. An OctetRED 384 (ForteBio, Menlo Park, Calif.) was used to evaluate off-target binding of monomeric GDF15_001 (CH23LS-GBT-GDF15_001) to ten TGFβ family members including human GDNF (R&D, 212-GD/CF), human Inhibin A (R&D, 8506-AB/CF), human Activin B (R&D, 659-AB/CF) human TGFβ-1 (R&D, 240-B/CF) human BMP2 (R&D, 355-BM/CF), human BMP3b (R&D, 1543-BP/CF), human BMP6 (R&D, 507-BP/CF), human BMP9 (R&D, 3209-BP/CF), human BMP11 (R&D, 1958-CD/CF), human GDF8 (Pfizer, 41075-201) and control human GDF15 (Mu IgG1Fc_Fxa_Hu GDF15). .. The TGFβ family members were diluted to 10 ug/ml in 10 mM Sodium Acetate pH 4.5 and amine coupled onto AR2G biosensors (catalogue #18-5092, ForteBio) according to the manufacturer's instructions.

    Recombinant:

    Article Title: Signaling pathways associated with Lgr6 to regulate osteogenesis
    Article Snippet: Cells were cultured at a density of 3000 cells/cm 2 using alpha-MEM supplemented with 16.5 % FBS (Atlas Biologicals, CO) in standard culture conditions for propagation and used within passage 7. .. Osteoblast differentiation was achieved using BMP stimulation by adding 200 ng/ml of recombinant human BMP2 (R&D Systems, MN) to the cell monolayer using osteopermissive media (serum-free alpha-MEM additionally supplemented with 25 μg/ml l -Ascorbic Acid Phosphate Magnesium Salt n-Hydrate (AA2P) (FUJIFILM Wako Chemicals USA Corp., VA), 5 mM β-glycerophosphate disodium salt hydrate (BGP) (Sigma, MO) and 1× Insulin-transferrin-selenous acid premix (ITS) (Corning, NY))[ 21 , 22 ]. ..

    Article Title: Signaling pathways associated with Lgr6 to regulate osteogenesis.
    Article Snippet: Fracture management largely relies on the bone's inherent healing capabilities and, when necessary, surgical intervention.. Currently, there are limited osteoinductive therapies to promote healing, making targeting skeletal stem/progenitor cells (SSPCs) a promising avenue for therapeutic development.. A limiting factor for this approach is our incomplete understanding of the molecular mechanisms governing SSPCs' behavior.

    Article Title: GWAS-informed data integration and non-coding CRISPRi screen illuminate genetic etiology of bone mineral density
    Article Snippet: .. For osteoblastic differentiation, we plated 15,000 cells/cm 2 in alpha-MEM consisting of 16.5% FBS, 25 μg/ml ascorbic acid-2-phosphate, 5 mM beta-glycerophosphate, and 1% insulin-transferrin-selenous acid (osteogenic media) and stimulated them the next day with recombinant human BMP2 (300 ng/ml) (R&D Systems, MN) in serum-free osteogenic media. ..

    Article Title: GWAS-informed data integration and non-coding CRISPRi screen illuminate genetic etiology of bone mineral density
    Article Snippet: .. For osteoblastic differentiation, we plated 15,000 cells/cm 2 in alpha-MEM consisting of 16.5% FBS, 25 μg/ml Ascorbic acid-2-phosphate, 5 mM beta-glycerophosphate and 1% insulin-transferrin-selenous acid (osteogenic media) and stimulated them the next day with recombinant human BMP2 (300 ng/ml) (R&D Systems, MN) in serum-free osteogenic media. ..



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    Comparative effects of BMP9 and <t>BMP2</t> on osteogenic differentiation and osteoclastogenesis in vitro. (A) Real‐time PCR analysis of key osteogenic genes (Col1, Runx2, ALP, and OCN) in MC3T3‐E1 cells treated with 8 nM of BMP2 or BMP9 for 3, 5, and 7 days. All gene‐expression levels were normalized to GAPDH. (B) Western blot analysis of osteogenic marker proteins in cell lysates harvested after 7 days of treatment with BMP2 or BMP9. GAPDH was used as the loading control. Densitometric quantification of band intensities (integrated density) normalized to GAPDH is shown below the blots and presented as relative protein expression. (C) Western blot showing dose‐dependent p‐Smad1/5/9 in MC3T3‐E1 cells exposed to varying concentrations of BMP2 or BMP9. Phosphorylation was quantified by densitometry and expressed as fold change vs. control after normalization using [(p‐Smad1/5/9)/(total Smad1/5/9)] and further normalized to GAPDH, as shown in the graph below the blots. Asterisks indicate statistical significance for pairwise comparisons between BMP2 and BMP9 at the same concentration (****, p < 0.0001), unless otherwise indicated. (D) ALP activity and representative images of ALP staining in MC3T3‐E1 cultures after 7 days of induction with BMP2 or BMP9. (E) Alizarin Red S staining illustrating mineralized nodule formation after extended culture with BMP2 or BMP9. (F) Representative TRAP‐stained images of RAW 264.7‐derived osteoclasts following treatment with RANKL (3 nM), BMP2 (8 nM), or BMP9 (8 nM) for 5 days. TRAP‐positive multinucleated osteoclasts are indicated by arrows. Scale bar, 20 μm. (G) Quantification of TRAP‐positive multinucleated cells per well. Data are presented as the mean ± SD ( n = 3 independent experiments), and p ‐values were calculated using one‐way analysis of variance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001). BMP, bone morphogenetic protein; PCR, polymerase chain reaction; ALP, alkaline phosphatase; Col1, collagen type I; Runx2, runt‐related transcription factor 2; OCN, osteocalcin; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase.
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    Image Search Results


    Comparative effects of BMP9 and BMP2 on osteogenic differentiation and osteoclastogenesis in vitro. (A) Real‐time PCR analysis of key osteogenic genes (Col1, Runx2, ALP, and OCN) in MC3T3‐E1 cells treated with 8 nM of BMP2 or BMP9 for 3, 5, and 7 days. All gene‐expression levels were normalized to GAPDH. (B) Western blot analysis of osteogenic marker proteins in cell lysates harvested after 7 days of treatment with BMP2 or BMP9. GAPDH was used as the loading control. Densitometric quantification of band intensities (integrated density) normalized to GAPDH is shown below the blots and presented as relative protein expression. (C) Western blot showing dose‐dependent p‐Smad1/5/9 in MC3T3‐E1 cells exposed to varying concentrations of BMP2 or BMP9. Phosphorylation was quantified by densitometry and expressed as fold change vs. control after normalization using [(p‐Smad1/5/9)/(total Smad1/5/9)] and further normalized to GAPDH, as shown in the graph below the blots. Asterisks indicate statistical significance for pairwise comparisons between BMP2 and BMP9 at the same concentration (****, p < 0.0001), unless otherwise indicated. (D) ALP activity and representative images of ALP staining in MC3T3‐E1 cultures after 7 days of induction with BMP2 or BMP9. (E) Alizarin Red S staining illustrating mineralized nodule formation after extended culture with BMP2 or BMP9. (F) Representative TRAP‐stained images of RAW 264.7‐derived osteoclasts following treatment with RANKL (3 nM), BMP2 (8 nM), or BMP9 (8 nM) for 5 days. TRAP‐positive multinucleated osteoclasts are indicated by arrows. Scale bar, 20 μm. (G) Quantification of TRAP‐positive multinucleated cells per well. Data are presented as the mean ± SD ( n = 3 independent experiments), and p ‐values were calculated using one‐way analysis of variance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001). BMP, bone morphogenetic protein; PCR, polymerase chain reaction; ALP, alkaline phosphatase; Col1, collagen type I; Runx2, runt‐related transcription factor 2; OCN, osteocalcin; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase.

    Journal: Clinical Implant Dentistry and Related Research

    Article Title: Bone Morphogenetic Protein ( BMP ) 9 Outperforms BMP2 in Osteogenesis and Osseointegration: In Vitro and In Vivo

    doi: 10.1111/cid.70135

    Figure Lengend Snippet: Comparative effects of BMP9 and BMP2 on osteogenic differentiation and osteoclastogenesis in vitro. (A) Real‐time PCR analysis of key osteogenic genes (Col1, Runx2, ALP, and OCN) in MC3T3‐E1 cells treated with 8 nM of BMP2 or BMP9 for 3, 5, and 7 days. All gene‐expression levels were normalized to GAPDH. (B) Western blot analysis of osteogenic marker proteins in cell lysates harvested after 7 days of treatment with BMP2 or BMP9. GAPDH was used as the loading control. Densitometric quantification of band intensities (integrated density) normalized to GAPDH is shown below the blots and presented as relative protein expression. (C) Western blot showing dose‐dependent p‐Smad1/5/9 in MC3T3‐E1 cells exposed to varying concentrations of BMP2 or BMP9. Phosphorylation was quantified by densitometry and expressed as fold change vs. control after normalization using [(p‐Smad1/5/9)/(total Smad1/5/9)] and further normalized to GAPDH, as shown in the graph below the blots. Asterisks indicate statistical significance for pairwise comparisons between BMP2 and BMP9 at the same concentration (****, p < 0.0001), unless otherwise indicated. (D) ALP activity and representative images of ALP staining in MC3T3‐E1 cultures after 7 days of induction with BMP2 or BMP9. (E) Alizarin Red S staining illustrating mineralized nodule formation after extended culture with BMP2 or BMP9. (F) Representative TRAP‐stained images of RAW 264.7‐derived osteoclasts following treatment with RANKL (3 nM), BMP2 (8 nM), or BMP9 (8 nM) for 5 days. TRAP‐positive multinucleated osteoclasts are indicated by arrows. Scale bar, 20 μm. (G) Quantification of TRAP‐positive multinucleated cells per well. Data are presented as the mean ± SD ( n = 3 independent experiments), and p ‐values were calculated using one‐way analysis of variance (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001). BMP, bone morphogenetic protein; PCR, polymerase chain reaction; ALP, alkaline phosphatase; Col1, collagen type I; Runx2, runt‐related transcription factor 2; OCN, osteocalcin; GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase.

    Article Snippet: Recombinant human BMP2 (R&D Systems, Minneapolis, MN, USA) was used as the control.

    Techniques: In Vitro, Real-time Polymerase Chain Reaction, Gene Expression, Western Blot, Marker, Control, Expressing, Phospho-proteomics, Concentration Assay, Activity Assay, Staining, Derivative Assay, Polymerase Chain Reaction

    Experimental timeline, surgical procedure, and implant stability in the beagle saddle‐type peri‐implant defect model. (A) Timeline of the in vivo study. On the surgery day a saddle‐type peri‐implant defect was created, a dental implant was inserted, and bone grafting was performed with group allocation as follows. Non‐graft, collagenated xenograft matrix only, collagenated xenograft matrix + BMP2, and collagenated xenograft matrix + BMP9. Calcein was injected subcutaneously on day 54. At 8 weeks implant stability was recorded, micro CT was acquired, and animals were sacrificed. (B) Surgical procedure. (C) ISQ measured immediately before sacrifice. Bars show mean ± SD. Asterisks indicate statistical significance as marked in the plot.

    Journal: Clinical Implant Dentistry and Related Research

    Article Title: Bone Morphogenetic Protein ( BMP ) 9 Outperforms BMP2 in Osteogenesis and Osseointegration: In Vitro and In Vivo

    doi: 10.1111/cid.70135

    Figure Lengend Snippet: Experimental timeline, surgical procedure, and implant stability in the beagle saddle‐type peri‐implant defect model. (A) Timeline of the in vivo study. On the surgery day a saddle‐type peri‐implant defect was created, a dental implant was inserted, and bone grafting was performed with group allocation as follows. Non‐graft, collagenated xenograft matrix only, collagenated xenograft matrix + BMP2, and collagenated xenograft matrix + BMP9. Calcein was injected subcutaneously on day 54. At 8 weeks implant stability was recorded, micro CT was acquired, and animals were sacrificed. (B) Surgical procedure. (C) ISQ measured immediately before sacrifice. Bars show mean ± SD. Asterisks indicate statistical significance as marked in the plot.

    Article Snippet: Recombinant human BMP2 (R&D Systems, Minneapolis, MN, USA) was used as the control.

    Techniques: In Vivo, Injection, Micro-CT