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Neurescence inc growth differentiation factor 11
Growth Differentiation Factor 11, supplied by Neurescence inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/growth differentiation factor 11/product/Neurescence inc
Average 90 stars, based on 1 article reviews
growth differentiation factor 11 - by Bioz Stars, 2026-06
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Figure 5 Myostatin-specific inhibition by myostatin-b. HeLa cells cotransfected with Luc and Gal plasmids were treated with recombinant myostatin at concentrations of 0, 20, 40 and 60 ng/mL (A); recombinant growth differentiation factor 11 <t>(GDF11)</t> at concentrations of 0, 10, 20 and 30 ng/mL (B); recombinant transforming growth factor β1 (TGF-β1) at concentrations of 0, 0.5, 1 and 2 ng/mL (C); and activin A at concentrations of 0, 10, 20 and 30 ng/mL (D). In addition, the myostatin-b plasmid was cotransfected into each treated cell. The results of luciferase activity are shown. Myostatin-b inhibited myostatin signalling induced only by recombinant myostatin but not by recombinant GDF11, recombinant TGF-β1 or recombinant activin A (red bars). The data are expressed as the mean ± SEM of three independent experiments. **P < 0.01, ***P < 0.001. RLU, relative luminescence unit.
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Versican binds with <t>Nodal</t> growth differentiation factor (NODAL) and growth differentiation factor 11 (GDF11). (A) Enzyme-linked immunosorbent assays (ELISAs) were performed to detect the concentration of versican in the culture medium of human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) after 72 <t>h</t> <t>recombinant</t> human hyaluronan and proteoglycan link protein 1 (rhHapln1) treatment. (B) Proteins with validated/potential interactions with versican. (C) Gene Oncology (GO)/Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the genes encoding the proteins in panel B. (D) Binding of versican to selective chemokines. Anti-versican, anti-chondroitin sulfate (anti-CS) mAb CS56, or selective chemokines (5–100 ng/spot) were spotted onto nitrocellulose membranes. After blocking, biotinylated versican (3 μg/mL) was applied to the membrane. The binding of biotinylated versican was detected in immunoblotting. (E) Binding of NODAL or GDF11 to immobilized versican. Serial dilutions of NODAL or GDF11 (0–3 μg/mL) were added to the versican (300 ng/well)-coated wells and incubated for 2 h. After washing, the binding of chemokines to versican was measured by ELISAs. (F) Versican binds NODAL and GDF11 through glycosaminoglycan chains. Versican (300 ng/well) was coated onto the wells of an ELISA plate. After blocking, the wells were untreated or treated with chondroitinase ABC (C’ABC), chondroitinase B (C’B), or keratanase (KerR) overnight at 37 °C. After washing, binding of Nodal (1 μg/mL), anti-versican core protein mAb (3 μg/mL), or anti-CS mAb (1:500 dilution) was detected. Values are expressed as the percentage of specific binding compared with the control. (G) Western blotting assays were conducted to investigate the effect of Hapln1 on the expression of GDF11 in hiPSC-CMs (2 and 4 weeks (W)), with or without the treatment of rhHapln1 (100 ng/mL) for 72 h. One-way analysis of variance (ANOVA) with Turkey post hoc tests was conducted for multiple group comparisons ( n = 3). ∗ P < 0.05 and ∗∗ P < 0.01.
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Figure 5 Myostatin-specific inhibition by myostatin-b. HeLa cells cotransfected with Luc and Gal plasmids were treated with recombinant myostatin at concentrations of 0, 20, 40 and 60 ng/mL (A); recombinant growth differentiation factor 11 (GDF11) at concentrations of 0, 10, 20 and 30 ng/mL (B); recombinant transforming growth factor β1 (TGF-β1) at concentrations of 0, 0.5, 1 and 2 ng/mL (C); and activin A at concentrations of 0, 10, 20 and 30 ng/mL (D). In addition, the myostatin-b plasmid was cotransfected into each treated cell. The results of luciferase activity are shown. Myostatin-b inhibited myostatin signalling induced only by recombinant myostatin but not by recombinant GDF11, recombinant TGF-β1 or recombinant activin A (red bars). The data are expressed as the mean ± SEM of three independent experiments. **P < 0.01, ***P < 0.001. RLU, relative luminescence unit.

Journal: Journal of cachexia, sarcopenia and muscle

Article Title: A novel splice variant of the human MSTN gene encodes a myostatin-specific myostatin inhibitor.

doi: 10.1002/jcsm.13314

Figure Lengend Snippet: Figure 5 Myostatin-specific inhibition by myostatin-b. HeLa cells cotransfected with Luc and Gal plasmids were treated with recombinant myostatin at concentrations of 0, 20, 40 and 60 ng/mL (A); recombinant growth differentiation factor 11 (GDF11) at concentrations of 0, 10, 20 and 30 ng/mL (B); recombinant transforming growth factor β1 (TGF-β1) at concentrations of 0, 0.5, 1 and 2 ng/mL (C); and activin A at concentrations of 0, 10, 20 and 30 ng/mL (D). In addition, the myostatin-b plasmid was cotransfected into each treated cell. The results of luciferase activity are shown. Myostatin-b inhibited myostatin signalling induced only by recombinant myostatin but not by recombinant GDF11, recombinant TGF-β1 or recombinant activin A (red bars). The data are expressed as the mean ± SEM of three independent experiments. **P < 0.01, ***P < 0.001. RLU, relative luminescence unit.

Article Snippet: After 24 h, the medium was replaced with serum-free RPMI 1640 or DMEM containing recombinant myostatin (788-G8, R&D Systems), recombinant growth differentiation factor 11 (GDF11) (1958-GD, R&D Systems), recombinant TGF-β1 (240-B/CF, R&D Systems) or recombinant activin A (338-AC/CF, R&D Systems).

Techniques: Inhibition, Recombinant, Plasmid Preparation, Luciferase, Activity Assay

Versican binds with Nodal growth differentiation factor (NODAL) and growth differentiation factor 11 (GDF11). (A) Enzyme-linked immunosorbent assays (ELISAs) were performed to detect the concentration of versican in the culture medium of human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) after 72 h recombinant human hyaluronan and proteoglycan link protein 1 (rhHapln1) treatment. (B) Proteins with validated/potential interactions with versican. (C) Gene Oncology (GO)/Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the genes encoding the proteins in panel B. (D) Binding of versican to selective chemokines. Anti-versican, anti-chondroitin sulfate (anti-CS) mAb CS56, or selective chemokines (5–100 ng/spot) were spotted onto nitrocellulose membranes. After blocking, biotinylated versican (3 μg/mL) was applied to the membrane. The binding of biotinylated versican was detected in immunoblotting. (E) Binding of NODAL or GDF11 to immobilized versican. Serial dilutions of NODAL or GDF11 (0–3 μg/mL) were added to the versican (300 ng/well)-coated wells and incubated for 2 h. After washing, the binding of chemokines to versican was measured by ELISAs. (F) Versican binds NODAL and GDF11 through glycosaminoglycan chains. Versican (300 ng/well) was coated onto the wells of an ELISA plate. After blocking, the wells were untreated or treated with chondroitinase ABC (C’ABC), chondroitinase B (C’B), or keratanase (KerR) overnight at 37 °C. After washing, binding of Nodal (1 μg/mL), anti-versican core protein mAb (3 μg/mL), or anti-CS mAb (1:500 dilution) was detected. Values are expressed as the percentage of specific binding compared with the control. (G) Western blotting assays were conducted to investigate the effect of Hapln1 on the expression of GDF11 in hiPSC-CMs (2 and 4 weeks (W)), with or without the treatment of rhHapln1 (100 ng/mL) for 72 h. One-way analysis of variance (ANOVA) with Turkey post hoc tests was conducted for multiple group comparisons ( n = 3). ∗ P < 0.05 and ∗∗ P < 0.01.

Journal: Journal of Pharmaceutical Analysis

Article Title: Hapln1 promotes dedifferentiation and proliferation of iPSC-derived cardiomyocytes by promoting versican-based GDF11 trapping

doi: 10.1016/j.jpha.2023.09.013

Figure Lengend Snippet: Versican binds with Nodal growth differentiation factor (NODAL) and growth differentiation factor 11 (GDF11). (A) Enzyme-linked immunosorbent assays (ELISAs) were performed to detect the concentration of versican in the culture medium of human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) after 72 h recombinant human hyaluronan and proteoglycan link protein 1 (rhHapln1) treatment. (B) Proteins with validated/potential interactions with versican. (C) Gene Oncology (GO)/Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the genes encoding the proteins in panel B. (D) Binding of versican to selective chemokines. Anti-versican, anti-chondroitin sulfate (anti-CS) mAb CS56, or selective chemokines (5–100 ng/spot) were spotted onto nitrocellulose membranes. After blocking, biotinylated versican (3 μg/mL) was applied to the membrane. The binding of biotinylated versican was detected in immunoblotting. (E) Binding of NODAL or GDF11 to immobilized versican. Serial dilutions of NODAL or GDF11 (0–3 μg/mL) were added to the versican (300 ng/well)-coated wells and incubated for 2 h. After washing, the binding of chemokines to versican was measured by ELISAs. (F) Versican binds NODAL and GDF11 through glycosaminoglycan chains. Versican (300 ng/well) was coated onto the wells of an ELISA plate. After blocking, the wells were untreated or treated with chondroitinase ABC (C’ABC), chondroitinase B (C’B), or keratanase (KerR) overnight at 37 °C. After washing, binding of Nodal (1 μg/mL), anti-versican core protein mAb (3 μg/mL), or anti-CS mAb (1:500 dilution) was detected. Values are expressed as the percentage of specific binding compared with the control. (G) Western blotting assays were conducted to investigate the effect of Hapln1 on the expression of GDF11 in hiPSC-CMs (2 and 4 weeks (W)), with or without the treatment of rhHapln1 (100 ng/mL) for 72 h. One-way analysis of variance (ANOVA) with Turkey post hoc tests was conducted for multiple group comparisons ( n = 3). ∗ P < 0.05 and ∗∗ P < 0.01.

Article Snippet: Recombinant mouse HAPLN1 (rmHAPLN1), human growth differentiation factor 11 (GDF11), and human Nodal growth differentiation factor (NODAL) protein were obtained from CUSABIO (CSB-EP010130MO, CSB-EP009344HU, and CSB-EP850428HU; Wuhan, China).

Techniques: Concentration Assay, Derivative Assay, Recombinant, Binding Assay, Blocking Assay, Membrane, Western Blot, Incubation, Enzyme-linked Immunosorbent Assay, Control, Expressing

NODAL and GDF11 mRNA expression in fetal human hearts at the single-cell level. (A, C) Uniform manifold approximation and projection (UMAP) plot indicating the individual cells with GDF11 (A) or NODAL (C) expression in the human fetal heart (left) and the cell type distribution (right). (B, D) Boxplots comparing different types of fetal cardiac cells with (B) GDF11 or (D) NODAL expression. Images were generated with access provided by Single Cell Portal ( https://singlecell.broadinstitute.org/single_cell ).

Journal: Journal of Pharmaceutical Analysis

Article Title: Hapln1 promotes dedifferentiation and proliferation of iPSC-derived cardiomyocytes by promoting versican-based GDF11 trapping

doi: 10.1016/j.jpha.2023.09.013

Figure Lengend Snippet: NODAL and GDF11 mRNA expression in fetal human hearts at the single-cell level. (A, C) Uniform manifold approximation and projection (UMAP) plot indicating the individual cells with GDF11 (A) or NODAL (C) expression in the human fetal heart (left) and the cell type distribution (right). (B, D) Boxplots comparing different types of fetal cardiac cells with (B) GDF11 or (D) NODAL expression. Images were generated with access provided by Single Cell Portal ( https://singlecell.broadinstitute.org/single_cell ).

Article Snippet: Recombinant mouse HAPLN1 (rmHAPLN1), human growth differentiation factor 11 (GDF11), and human Nodal growth differentiation factor (NODAL) protein were obtained from CUSABIO (CSB-EP010130MO, CSB-EP009344HU, and CSB-EP850428HU; Wuhan, China).

Techniques: Expressing, Generated