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bmp4 neutralizing antibody (R&D Systems)

Name: bmp4 neutralizing antibody
Brand: R&D Systems
Rating: 90 (65 reviews)

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R&D Systems bmp4 neutralizing antibody

<t>BMP4</t> downregulates the activation of naïve CD4+ T cells. (A) The expression of CD25 on T cells tested by flow cytometer 24 hours after TCR activation with or without BMP4 treatment. (B) The frequency of CD25+ T cells. (C) The gene expression of Il2ra checked by Quantitative real-time PCR. (D) The expression of CD69 on T cells. (E) The frequency of CD69+ T cells. (F) The gene expression of Cd69 checked by Quantitative real-time PCR. (G) The expression of CD44 on T cells. (H) The frequency of CD44+ T cells. (I) The gene expression of Cd44 checked by Quantitative real-time PCR.

Bmp4 Neutralizing Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 65 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 65 article reviews

bmp4 neutralizing antibody - by Bioz Stars, 2026-03

90/100 stars

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1) Product Images from "BMP4 Moderates Glycolysis and Regulates Activation and Interferon-Gamma Production in CD4+ T Cells"

Article Title: BMP4 Moderates Glycolysis and Regulates Activation and Interferon-Gamma Production in CD4+ T Cells

Journal: Frontiers in Immunology

doi: 10.3389/fimmu.2021.702211

BMP4 downregulates the activation of naïve CD4+ T cells. (A) The expression of CD25 on T cells tested by flow cytometer 24 hours after TCR activation with or without BMP4 treatment. (B) The frequency of CD25+ T cells. (C) The gene expression of Il2ra checked by Quantitative real-time PCR. (D) The expression of CD69 on T cells. (E) The frequency of CD69+ T cells. (F) The gene expression of Cd69 checked by Quantitative real-time PCR. (G) The expression of CD44 on T cells. (H) The frequency of CD44+ T cells. (I) The gene expression of Cd44 checked by Quantitative real-time PCR.

Figure Legend Snippet: BMP4 downregulates the activation of naïve CD4+ T cells. (A) The expression of CD25 on T cells tested by flow cytometer 24 hours after TCR activation with or without BMP4 treatment. (B) The frequency of CD25+ T cells. (C) The gene expression of Il2ra checked by Quantitative real-time PCR. (D) The expression of CD69 on T cells. (E) The frequency of CD69+ T cells. (F) The gene expression of Cd69 checked by Quantitative real-time PCR. (G) The expression of CD44 on T cells. (H) The frequency of CD44+ T cells. (I) The gene expression of Cd44 checked by Quantitative real-time PCR.

Techniques Used: Activation Assay, Expressing, Flow Cytometry, Gene Expression, Real-time Polymerase Chain Reaction

BMP4 moderates glycolysis of T cells after activation. (A, B) Extracellular acidification rate of T cells 24 hours after TCR activation with or without BMP4 treatment. (C–H) The gene expression of Hk1, Hk2, Hk3, Pfkl, Myc and Hif1a checked by Quantitative real-time PCR.

Figure Legend Snippet: BMP4 moderates glycolysis of T cells after activation. (A, B) Extracellular acidification rate of T cells 24 hours after TCR activation with or without BMP4 treatment. (C–H) The gene expression of Hk1, Hk2, Hk3, Pfkl, Myc and Hif1a checked by Quantitative real-time PCR.

Techniques Used: Activation Assay, Gene Expression, Real-time Polymerase Chain Reaction

BMP4 downregulates the IFN-γ production of CD4+ T cells without increasing Tregs. (A) The expression of IFN-γ and IL-4 on T cells were tested by flow cytometer 3 days after TCR activation with or without BMP4 treatment. (B) The frequency of IFN-γ+ T cells. (C) The frequency of IL-4+ T cells. (D) The concentration of IFN-γ+ in the supernatant of T cells culture medium 3 days after TCR activation with or without BMP4 treatment. (E) The concentration of IFN-γ+ in the supernatant of T cells culture medium. (F) The gene expression of Ifng checked by Quantitative real-time PCR. (G) The gene expression of Il4 . (H) The expression of FoxP3 on T cells tested by flow cytometer. (I) The frequency of FoxP3+ T cells. (J) The gene expression of Foxp3 .

Figure Legend Snippet: BMP4 downregulates the IFN-γ production of CD4+ T cells without increasing Tregs. (A) The expression of IFN-γ and IL-4 on T cells were tested by flow cytometer 3 days after TCR activation with or without BMP4 treatment. (B) The frequency of IFN-γ+ T cells. (C) The frequency of IL-4+ T cells. (D) The concentration of IFN-γ+ in the supernatant of T cells culture medium 3 days after TCR activation with or without BMP4 treatment. (E) The concentration of IFN-γ+ in the supernatant of T cells culture medium. (F) The gene expression of Ifng checked by Quantitative real-time PCR. (G) The gene expression of Il4 . (H) The expression of FoxP3 on T cells tested by flow cytometer. (I) The frequency of FoxP3+ T cells. (J) The gene expression of Foxp3 .

Techniques Used: Expressing, Flow Cytometry, Activation Assay, Concentration Assay, Gene Expression, Real-time Polymerase Chain Reaction

BMP4 suppresses the IFN-γ production in CD4+ T cells in vivo . (A) OT-II CD4+ T cells were adoptively transferred to CD45.1 transgenic C57BL/6 mice and injected OVA peptides into the footpads. The expression of IFN-γ and IL-4 on T cells from the draining lymph nodes of footpads with or without administration of BMP4 or anti-BMP4 antibody treatment. (B) The frequency of IFN-γ+ T cells. (C) The frequency of IL-4+ T cells. (D–F) The gene expression of Hif1a, Hk2, Pfkl checked by Quantitative real-time PCR.

Figure Legend Snippet: BMP4 suppresses the IFN-γ production in CD4+ T cells in vivo . (A) OT-II CD4+ T cells were adoptively transferred to CD45.1 transgenic C57BL/6 mice and injected OVA peptides into the footpads. The expression of IFN-γ and IL-4 on T cells from the draining lymph nodes of footpads with or without administration of BMP4 or anti-BMP4 antibody treatment. (B) The frequency of IFN-γ+ T cells. (C) The frequency of IL-4+ T cells. (D–F) The gene expression of Hif1a, Hk2, Pfkl checked by Quantitative real-time PCR.

Techniques Used: In Vivo, Transgenic Assay, Injection, Expressing, Gene Expression, Real-time Polymerase Chain Reaction

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Journal: Frontiers in Immunology

Article Title: BMP4 Moderates Glycolysis and Regulates Activation and Interferon-Gamma Production in CD4+ T Cells

doi: 10.3389/fimmu.2021.702211

Figure Lengend Snippet: BMP4 downregulates the activation of naïve CD4+ T cells. (A) The expression of CD25 on T cells tested by flow cytometer 24 hours after TCR activation with or without BMP4 treatment. (B) The frequency of CD25+ T cells. (C) The gene expression of Il2ra checked by Quantitative real-time PCR. (D) The expression of CD69 on T cells. (E) The frequency of CD69+ T cells. (F) The gene expression of Cd69 checked by Quantitative real-time PCR. (G) The expression of CD44 on T cells. (H) The frequency of CD44+ T cells. (I) The gene expression of Cd44 checked by Quantitative real-time PCR.

Article Snippet: BMP4 neutralizing antibody (R&D system) was used in 10mg/kg for i.p.

Techniques: Activation Assay, Expressing, Flow Cytometry, Gene Expression, Real-time Polymerase Chain Reaction

Journal: Frontiers in Immunology

Article Title: BMP4 Moderates Glycolysis and Regulates Activation and Interferon-Gamma Production in CD4+ T Cells

doi: 10.3389/fimmu.2021.702211

Figure Lengend Snippet: BMP4 moderates glycolysis of T cells after activation. (A, B) Extracellular acidification rate of T cells 24 hours after TCR activation with or without BMP4 treatment. (C–H) The gene expression of Hk1, Hk2, Hk3, Pfkl, Myc and Hif1a checked by Quantitative real-time PCR.

Article Snippet: BMP4 neutralizing antibody (R&D system) was used in 10mg/kg for i.p.

Techniques: Activation Assay, Gene Expression, Real-time Polymerase Chain Reaction

Journal: Frontiers in Immunology

Article Title: BMP4 Moderates Glycolysis and Regulates Activation and Interferon-Gamma Production in CD4+ T Cells

doi: 10.3389/fimmu.2021.702211

Figure Lengend Snippet: BMP4 downregulates the IFN-γ production of CD4+ T cells without increasing Tregs. (A) The expression of IFN-γ and IL-4 on T cells were tested by flow cytometer 3 days after TCR activation with or without BMP4 treatment. (B) The frequency of IFN-γ+ T cells. (C) The frequency of IL-4+ T cells. (D) The concentration of IFN-γ+ in the supernatant of T cells culture medium 3 days after TCR activation with or without BMP4 treatment. (E) The concentration of IFN-γ+ in the supernatant of T cells culture medium. (F) The gene expression of Ifng checked by Quantitative real-time PCR. (G) The gene expression of Il4 . (H) The expression of FoxP3 on T cells tested by flow cytometer. (I) The frequency of FoxP3+ T cells. (J) The gene expression of Foxp3 .

Article Snippet: BMP4 neutralizing antibody (R&D system) was used in 10mg/kg for i.p.

Techniques: Expressing, Flow Cytometry, Activation Assay, Concentration Assay, Gene Expression, Real-time Polymerase Chain Reaction

Journal: Frontiers in Immunology

Article Title: BMP4 Moderates Glycolysis and Regulates Activation and Interferon-Gamma Production in CD4+ T Cells

doi: 10.3389/fimmu.2021.702211

Figure Lengend Snippet: BMP4 suppresses the IFN-γ production in CD4+ T cells in vivo . (A) OT-II CD4+ T cells were adoptively transferred to CD45.1 transgenic C57BL/6 mice and injected OVA peptides into the footpads. The expression of IFN-γ and IL-4 on T cells from the draining lymph nodes of footpads with or without administration of BMP4 or anti-BMP4 antibody treatment. (B) The frequency of IFN-γ+ T cells. (C) The frequency of IL-4+ T cells. (D–F) The gene expression of Hif1a, Hk2, Pfkl checked by Quantitative real-time PCR.

Article Snippet: BMP4 neutralizing antibody (R&D system) was used in 10mg/kg for i.p.

Techniques: In Vivo, Transgenic Assay, Injection, Expressing, Gene Expression, Real-time Polymerase Chain Reaction

Bmp4 and Bmper are reciprocally regulated by internalization. MECs were treated with recombinant Bmper (6 nM) and/or Bmp4 (0.6 nM) and their lysates were subjected to the following analysis. (a) A Western blot showing enhanced Bmper and Bmp4 internalization in the presence of one another (lane 4). Addition of a Bmp4 neutralizing antibody prevented their internalization (lane 5). (b) MECs were infected with adenoviruses expressing GFP, wild-type Bmp receptor II (WT), or a tailless form of Bmp receptor II (Tailless) for 24 h before cotreatment with 0.6 nM Bmp4 and 6 nM Bmper for 1.5 h. (c) Kinetic analysis of the effects of Bmper (6 nM) on Bmp4 (0.6 nM) activity and Bmp4 internalization after treating MECs with Bmp4 and/or Bmper for 48 h. (d) A direct comparison of internalized Bmper and Bmp4 after a pulse with recombinant Bmp proteins and a chase with cold media or media containing chloroquine. (e) Cell lysates from MECs pulsed with Bmp4 alone (0.6 nM) and with Bmper (6 nM) for 2, 24, and 48 h were measured by Western analysis for Bmp4 in conditioned media before and after retreating the cells at 22 and 46 h (24p and 48p, respectively). (f) A Western analysis of Bmper, Bmp4, and p-Smad using lysates from MECs treated as follows: HEK-293 conditioned media from untreated cells (UT CM); untransfected HEK-293 cells spiked with 6 nM of recombinant full-length cleaved Bmper (rBmper) and/or 0.6 nM of recombinant Bmp4 (Bmp4); and conditioned media from HEK-293 cells expressing the amino fragment (N terminus), carboxy fragment (C terminus), and a proteolytic cleavage mutant of Bmper (PC mutant).

Journal: The Journal of Cell Biology

Article Title: A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling

doi: 10.1083/jcb.200808064

Figure Lengend Snippet: Bmp4 and Bmper are reciprocally regulated by internalization. MECs were treated with recombinant Bmper (6 nM) and/or Bmp4 (0.6 nM) and their lysates were subjected to the following analysis. (a) A Western blot showing enhanced Bmper and Bmp4 internalization in the presence of one another (lane 4). Addition of a Bmp4 neutralizing antibody prevented their internalization (lane 5). (b) MECs were infected with adenoviruses expressing GFP, wild-type Bmp receptor II (WT), or a tailless form of Bmp receptor II (Tailless) for 24 h before cotreatment with 0.6 nM Bmp4 and 6 nM Bmper for 1.5 h. (c) Kinetic analysis of the effects of Bmper (6 nM) on Bmp4 (0.6 nM) activity and Bmp4 internalization after treating MECs with Bmp4 and/or Bmper for 48 h. (d) A direct comparison of internalized Bmper and Bmp4 after a pulse with recombinant Bmp proteins and a chase with cold media or media containing chloroquine. (e) Cell lysates from MECs pulsed with Bmp4 alone (0.6 nM) and with Bmper (6 nM) for 2, 24, and 48 h were measured by Western analysis for Bmp4 in conditioned media before and after retreating the cells at 22 and 46 h (24p and 48p, respectively). (f) A Western analysis of Bmper, Bmp4, and p-Smad using lysates from MECs treated as follows: HEK-293 conditioned media from untreated cells (UT CM); untransfected HEK-293 cells spiked with 6 nM of recombinant full-length cleaved Bmper (rBmper) and/or 0.6 nM of recombinant Bmp4 (Bmp4); and conditioned media from HEK-293 cells expressing the amino fragment (N terminus), carboxy fragment (C terminus), and a proteolytic cleavage mutant of Bmper (PC mutant).

Article Snippet: The antibodies and recombinant proteins for Bmper, Bmp4, Noggin, Chordin, and Gremlin and monoclonal anti-human Bmp4 neutralizing antibody were purchased from R&D Systems.

Techniques: Recombinant, Western Blot, Infection, Expressing, Activity Assay, Comparison, Mutagenesis

Bmper and Bmp4 internalize through a clathrin-dependent mechanism. (a) MECs were treated with 50 µM chlorpromazine to disrupt internalization into endosomes and 10 mM methyl-β-cyclodextrin to disrupt lipid raft–caveolar internalization. (b) Transmission electron microscopy sequentially captured after cotreatment of MEC with 0.6 nM Bmp4 (detected with 5-nm gold immunoparticles) and 6 nM Bmper (detected with 25-nm gold immunoparticles). Colocalization (arrows) is demonstrated at discreet locations on the cell membrane after a 5-min pulse with Bmp4 and Bmper (i and ii), coalescing along clathrin-coated invaginations (arrow) after a 30-min pulse (iii), and endocytic sorting after 1.5 h of treatment (iv and v).

Journal: The Journal of Cell Biology

Article Title: A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling

doi: 10.1083/jcb.200808064

Figure Lengend Snippet: Bmper and Bmp4 internalize through a clathrin-dependent mechanism. (a) MECs were treated with 50 µM chlorpromazine to disrupt internalization into endosomes and 10 mM methyl-β-cyclodextrin to disrupt lipid raft–caveolar internalization. (b) Transmission electron microscopy sequentially captured after cotreatment of MEC with 0.6 nM Bmp4 (detected with 5-nm gold immunoparticles) and 6 nM Bmper (detected with 25-nm gold immunoparticles). Colocalization (arrows) is demonstrated at discreet locations on the cell membrane after a 5-min pulse with Bmp4 and Bmper (i and ii), coalescing along clathrin-coated invaginations (arrow) after a 30-min pulse (iii), and endocytic sorting after 1.5 h of treatment (iv and v).

Article Snippet: The antibodies and recombinant proteins for Bmper, Bmp4, Noggin, Chordin, and Gremlin and monoclonal anti-human Bmp4 neutralizing antibody were purchased from R&D Systems.

Techniques: Transmission Assay, Electron Microscopy, Membrane

$Bmper and Bmp4 are shuttled to the lysosome through endocytic trafficking. Bmper locates near a caveolin compartment at the cell surface and internalizes into early endosomes. (a) MECs cultured at 4°C and treated with Bmper (6 nM) and Bmp4 (0.6 nM) were analyzed by fluorescent immunoconfocal microscopy. A significant portion of the Bmper protein (green) appears to be localized near a membrane surface caveolin (red) compartment (arrow) and throughout filopodia. (b) After a 4°C incubation, MECs treated with Bmper (6 nM) and Bmp4 (0.6 nM) were permitted to internalize at 37°C. Bmper (green) is detected in a fraction (yellow) of the early endosomes expressing the marker EEA1 (red). (c) The same immunoconfocal analysis was used to characterize late endocytic to lysosomal translocation using the marker Rab7 (bottom, red) to colocalize with Bmper (green) and Bmp4 (red). MECs were treated with 0.6 nM Bmp4 and 6 nM Bmper for 1.5 h before fixing. Significant colocalization of Bmper and Bmp4 overlaps with Bmper and Rab7 colocalization (right panel, yellow).$

Journal: The Journal of Cell Biology

Article Title: A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling

doi: 10.1083/jcb.200808064

Figure Lengend Snippet: Bmper and Bmp4 are shuttled to the lysosome through endocytic trafficking. Bmper locates near a caveolin compartment at the cell surface and internalizes into early endosomes. (a) MECs cultured at 4°C and treated with Bmper (6 nM) and Bmp4 (0.6 nM) were analyzed by fluorescent immunoconfocal microscopy. A significant portion of the Bmper protein (green) appears to be localized near a membrane surface caveolin (red) compartment (arrow) and throughout filopodia. (b) After a 4°C incubation, MECs treated with Bmper (6 nM) and Bmp4 (0.6 nM) were permitted to internalize at 37°C. Bmper (green) is detected in a fraction (yellow) of the early endosomes expressing the marker EEA1 (red). (c) The same immunoconfocal analysis was used to characterize late endocytic to lysosomal translocation using the marker Rab7 (bottom, red) to colocalize with Bmper (green) and Bmp4 (red). MECs were treated with 0.6 nM Bmp4 and 6 nM Bmper for 1.5 h before fixing. Significant colocalization of Bmper and Bmp4 overlaps with Bmper and Rab7 colocalization (right panel, yellow).

Article Snippet: The antibodies and recombinant proteins for Bmper, Bmp4, Noggin, Chordin, and Gremlin and monoclonal anti-human Bmp4 neutralizing antibody were purchased from R&D Systems.

Techniques: Cell Culture, Microscopy, Membrane, Incubation, Expressing, Marker, Translocation Assay

Bmper regulates Bmp4 activity in a concentration-dependent manner. (a) A representative Western blot ( n = 3) of a dose–response experiment using MECs treated over a range of Bmper concentrations (0–100 nM) while holding Bmp4 constant (1 nM). Noggin was used as a positive control for inhibiting Bmp4 activity. The N-terminal fragment of Bmper is presented for the Western analysis. (b) The difference between the effects of Bmper (squares) and Noggin (triangles) on Bmp4 activity in the range of 0.1 to 5 nM was statistically significant (*, P < 0.05). (c) Representative Western blot showing the effects of a low (0.5 nM) and high (50 nM) molar concentration of Bmper on 1.0 nM of Bmp4-mediated cleaved Caspase-3 activity as a readout for apoptosis in primary day 15.5 lung MEFs. (d) Bar Graph showing the quantity of cleaved Caspase-3 activity from panel c. Top bar represents significant statistical difference from the untreated samples (*, P < 0.05). The differences in the effects of low versus high molar concentrations of Bmper on Bmp4-attenuated apoptosis were statistically significant (*, P < 0.05) and are represented by the bottom bar in panel d. Samples were analyzed for statistics as described in Materials and methods.

Journal: The Journal of Cell Biology

Article Title: A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling

doi: 10.1083/jcb.200808064

Figure Lengend Snippet: Bmper regulates Bmp4 activity in a concentration-dependent manner. (a) A representative Western blot ( n = 3) of a dose–response experiment using MECs treated over a range of Bmper concentrations (0–100 nM) while holding Bmp4 constant (1 nM). Noggin was used as a positive control for inhibiting Bmp4 activity. The N-terminal fragment of Bmper is presented for the Western analysis. (b) The difference between the effects of Bmper (squares) and Noggin (triangles) on Bmp4 activity in the range of 0.1 to 5 nM was statistically significant (*, P < 0.05). (c) Representative Western blot showing the effects of a low (0.5 nM) and high (50 nM) molar concentration of Bmper on 1.0 nM of Bmp4-mediated cleaved Caspase-3 activity as a readout for apoptosis in primary day 15.5 lung MEFs. (d) Bar Graph showing the quantity of cleaved Caspase-3 activity from panel c. Top bar represents significant statistical difference from the untreated samples (*, P < 0.05). The differences in the effects of low versus high molar concentrations of Bmper on Bmp4-attenuated apoptosis were statistically significant (*, P < 0.05) and are represented by the bottom bar in panel d. Samples were analyzed for statistics as described in Materials and methods.

Article Snippet: The antibodies and recombinant proteins for Bmper, Bmp4, Noggin, Chordin, and Gremlin and monoclonal anti-human Bmp4 neutralizing antibody were purchased from R&D Systems.

Techniques: Activity Assay, Concentration Assay, Western Blot, Positive Control

Bmp4 endocytosis is mediated by Bmper, Gremlin, and Noggin, but not Chordin. A panel of secreted Bmp factors (6.0 nM) were evaluated for their effects on Bmp4 (0.6 nM) and on Bmper-mediated Bmp4 internalization and signaling at several time points. A Western analysis showing the effects of active recombinant Chordin, Noggin, and Gremlin on the activity of Bmp4 alone or with cleaved full-length Bmper was measured 10 min (a) and 1.5 h (b) after treatment. Protein internalization and Smad activation were measured for each of these Bmp factors: Chordin (top), Noggin (middle), and Gremlin (bottom). (c) Pulse-chase experiment in MECs treated with Bmp4, Bmper, Noggin, and combinations of Bmp4 and Bmper (top), Bmp4 and Noggin (middle), and Bmper and Chordin (bottom). After treating MECs with recombinant protein(s) using the same experimental conditions and protein concentrations used in panel a, MECs were either chased with cold media or cold media containing chloroquine that lack recombinant protein(s). (d) A model of Bmper-mediated Bmp4 internalization.

Journal: The Journal of Cell Biology

Article Title: A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling

doi: 10.1083/jcb.200808064

Figure Lengend Snippet: Bmp4 endocytosis is mediated by Bmper, Gremlin, and Noggin, but not Chordin. A panel of secreted Bmp factors (6.0 nM) were evaluated for their effects on Bmp4 (0.6 nM) and on Bmper-mediated Bmp4 internalization and signaling at several time points. A Western analysis showing the effects of active recombinant Chordin, Noggin, and Gremlin on the activity of Bmp4 alone or with cleaved full-length Bmper was measured 10 min (a) and 1.5 h (b) after treatment. Protein internalization and Smad activation were measured for each of these Bmp factors: Chordin (top), Noggin (middle), and Gremlin (bottom). (c) Pulse-chase experiment in MECs treated with Bmp4, Bmper, Noggin, and combinations of Bmp4 and Bmper (top), Bmp4 and Noggin (middle), and Bmper and Chordin (bottom). After treating MECs with recombinant protein(s) using the same experimental conditions and protein concentrations used in panel a, MECs were either chased with cold media or cold media containing chloroquine that lack recombinant protein(s). (d) A model of Bmper-mediated Bmp4 internalization.

Article Snippet: The antibodies and recombinant proteins for Bmper, Bmp4, Noggin, Chordin, and Gremlin and monoclonal anti-human Bmp4 neutralizing antibody were purchased from R&D Systems.

Techniques: Western Blot, Recombinant, Activity Assay, Activation Assay, Pulse Chase

Bmper inhibits Bmp signaling during lung development. Lung development and Bmp4 activity were evaluated in wild-type (WT) mice versus mice with a heterozygous (HT) inactivation of Bmper at postnatal day 0. (a) Hematoxylin and eosin analysis of heterozygous lungs demonstrated delayed branching morphogenesis and inadequate expanded alveoli, which were separated by expansive interstitial mesenchyme. (b) Staining for the type II epithelial cell marker prosurfactant C (arrows). Bars, 100 µM. Positive staining is brown and counterstaining is blue. Graphical representation of the percentage of prosurfactant C–positive cells in wild-type versus Bmper het lungs. (c) Id1 mRNA expression was measured as a target of downstream Bmp activity by PCR. (d) Representative blots of endogenous Bmp4 in lysates (postnatal day 0) of lung for two individual animals each of wild-type, heterozygous, and knockout (KO) Bmper mice.

Journal: The Journal of Cell Biology

Article Title: A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling

doi: 10.1083/jcb.200808064

Figure Lengend Snippet: Bmper inhibits Bmp signaling during lung development. Lung development and Bmp4 activity were evaluated in wild-type (WT) mice versus mice with a heterozygous (HT) inactivation of Bmper at postnatal day 0. (a) Hematoxylin and eosin analysis of heterozygous lungs demonstrated delayed branching morphogenesis and inadequate expanded alveoli, which were separated by expansive interstitial mesenchyme. (b) Staining for the type II epithelial cell marker prosurfactant C (arrows). Bars, 100 µM. Positive staining is brown and counterstaining is blue. Graphical representation of the percentage of prosurfactant C–positive cells in wild-type versus Bmper het lungs. (c) Id1 mRNA expression was measured as a target of downstream Bmp activity by PCR. (d) Representative blots of endogenous Bmp4 in lysates (postnatal day 0) of lung for two individual animals each of wild-type, heterozygous, and knockout (KO) Bmper mice.

Article Snippet: The antibodies and recombinant proteins for Bmper, Bmp4, Noggin, Chordin, and Gremlin and monoclonal anti-human Bmp4 neutralizing antibody were purchased from R&D Systems.

Techniques: Activity Assay, Staining, Marker, Expressing, Knock-Out

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1) Product Images from "BMP4 Moderates Glycolysis and Regulates Activation and Interferon-Gamma Production in CD4+ T Cells"

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