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anti gdf11 primary antibody  (R&D Systems)


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    R&D Systems anti gdf11 primary antibody
    Anti Gdf11 Primary Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+gdf11/pm41637825-94-14-19?v=R%26D+Systems
    Average 93 stars, based on 18 article reviews
    anti gdf11 primary antibody - by Bioz Stars, 2026-08
    93/100 stars

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    R&D Systems recombinant growth differentiation factor 11 gdf11
    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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    PeproTech gdf11 recombinant human gdf11 (rgdf11)
    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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    R&D Systems recombinant human gdf11 aa299 407
    FIGURE 1 An acute bout of endurance exercise (90 min run) modified the levels of <t>GDF11</t> in cerebrospinal fluid but not in circulation of healthy trained volunteers. GDF11 levels were assessed by immunoblotting, using three different primary antibodies: (A) GDF11-specific N-terminus antibody (CSF, n=12/12, B/R, p=0.046); (B) GDF11-specific C-terminus antibody (CSF, n=13/13, B/R, p=0.008); (C) GDF11/8 antibody (CSF, n=12/12, B/R, p=0.065); (D) GDF11-specific N-terminus antibody (serum, n= 14/14/14, B/0/R); (E) GDF11-C-terminus antibody (plasma, n=13/13/13, B/0/R); (F) GDF11- specific N-terminus antibody (plasma, n=14/14/13, B/0/R); Due to the lack of space, molecular weight ladders are not visible in Figures 1D–F and therefore, the molecular weights of GDF11 are in this case approximate, based on our validation studies of antibodies. B, Basal, before run; R, after run; A.U., signal intensity; GDF, Growth Differentiation Factor. Immunoblotting of all samples was performed under identical conditions. Statistical differences were analysed using paired Student’s t-test. *p<0.05, **p<0.01, #p<0.1 (A–C).
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    Information of antibodies

    Journal: Journal of Neuroinflammation

    Article Title: Stabilizing histamine release in gut mast cells mitigates peripheral and central inflammation after stroke

    doi: 10.1186/s12974-023-02887-7

    Figure Lengend Snippet: Information of antibodies

    Article Snippet: Recombinant Human GDF11 protein (ab50159) , abcam ab50159 , 1:1000.

    Techniques: Recombinant

    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

    FIGURE 1 An acute bout of endurance exercise (90 min run) modified the levels of GDF11 in cerebrospinal fluid but not in circulation of healthy trained volunteers. GDF11 levels were assessed by immunoblotting, using three different primary antibodies: (A) GDF11-specific N-terminus antibody (CSF, n=12/12, B/R, p=0.046); (B) GDF11-specific C-terminus antibody (CSF, n=13/13, B/R, p=0.008); (C) GDF11/8 antibody (CSF, n=12/12, B/R, p=0.065); (D) GDF11-specific N-terminus antibody (serum, n= 14/14/14, B/0/R); (E) GDF11-C-terminus antibody (plasma, n=13/13/13, B/0/R); (F) GDF11- specific N-terminus antibody (plasma, n=14/14/13, B/0/R); Due to the lack of space, molecular weight ladders are not visible in Figures 1D–F and therefore, the molecular weights of GDF11 are in this case approximate, based on our validation studies of antibodies. B, Basal, before run; R, after run; A.U., signal intensity; GDF, Growth Differentiation Factor. Immunoblotting of all samples was performed under identical conditions. Statistical differences were analysed using paired Student’s t-test. *p<0.05, **p<0.01, #p<0.1 (A–C).

    Journal: Frontiers in endocrinology

    Article Title: Acute endurance exercise modulates growth differentiation factor 11 in cerebrospinal fluid of healthy young adults.

    doi: 10.3389/fendo.2023.1137048

    Figure Lengend Snippet: FIGURE 1 An acute bout of endurance exercise (90 min run) modified the levels of GDF11 in cerebrospinal fluid but not in circulation of healthy trained volunteers. GDF11 levels were assessed by immunoblotting, using three different primary antibodies: (A) GDF11-specific N-terminus antibody (CSF, n=12/12, B/R, p=0.046); (B) GDF11-specific C-terminus antibody (CSF, n=13/13, B/R, p=0.008); (C) GDF11/8 antibody (CSF, n=12/12, B/R, p=0.065); (D) GDF11-specific N-terminus antibody (serum, n= 14/14/14, B/0/R); (E) GDF11-C-terminus antibody (plasma, n=13/13/13, B/0/R); (F) GDF11- specific N-terminus antibody (plasma, n=14/14/13, B/0/R); Due to the lack of space, molecular weight ladders are not visible in Figures 1D–F and therefore, the molecular weights of GDF11 are in this case approximate, based on our validation studies of antibodies. B, Basal, before run; R, after run; A.U., signal intensity; GDF, Growth Differentiation Factor. Immunoblotting of all samples was performed under identical conditions. Statistical differences were analysed using paired Student’s t-test. *p<0.05, **p<0.01, #p<0.1 (A–C).

    Article Snippet: To corroborate the findings, GDF11 C-terminus specific monoclonal antibody was used (recombinant human GDF11 aa299-407, 1:1000, R&D systems, MAB19581, USA) (sample set B, n=13; overlap between A & B sample sets: n=7, Supplementary Figure 1B).

    Techniques: Western Blot, Clinical Proteomics, Molecular Weight, Biomarker Discovery

    FIGURE 2 Running-induced decrease of blood-brain barrier permeability (CSF/serum albumin ratio). n=17. (albumin values were not measured in CSF of one individual, and two individuals had CSF available only after the run) (A); its association with CSF/serum GDF11 ratio (B); and CSF/serum GDF11/8 ratio (C). CSF, Cerebrospinal Fluid; GDF, Growth Differentiation Factor. ***p<0.001; Open circles - before run; Full circles - after run.

    Journal: Frontiers in endocrinology

    Article Title: Acute endurance exercise modulates growth differentiation factor 11 in cerebrospinal fluid of healthy young adults.

    doi: 10.3389/fendo.2023.1137048

    Figure Lengend Snippet: FIGURE 2 Running-induced decrease of blood-brain barrier permeability (CSF/serum albumin ratio). n=17. (albumin values were not measured in CSF of one individual, and two individuals had CSF available only after the run) (A); its association with CSF/serum GDF11 ratio (B); and CSF/serum GDF11/8 ratio (C). CSF, Cerebrospinal Fluid; GDF, Growth Differentiation Factor. ***p<0.001; Open circles - before run; Full circles - after run.

    Article Snippet: To corroborate the findings, GDF11 C-terminus specific monoclonal antibody was used (recombinant human GDF11 aa299-407, 1:1000, R&D systems, MAB19581, USA) (sample set B, n=13; overlap between A & B sample sets: n=7, Supplementary Figure 1B).

    Techniques: Permeability

    FIGURE 3 Heat map depicting associations between levels of GDF11 and clinical parameters, as well as their running-induced changes. Data were analyzed using GDF11-specific N-terminus antibody (paired serum samples n=14; paired CSF samples n=12, unpaired CSF samples available only after run n=2). BMI, body mass index; CSF, cerebrospinal fluid; GDF, Growth Differentiation Factor; HRmax, maximal heart rate; S-CK, serum creatinkinase; R, correlation coefficient; VO2max, maximal aerobic capacity. Coefficients of significant correlations (p<0.05) or trends (p<0.1) are presented in numbers.

    Journal: Frontiers in endocrinology

    Article Title: Acute endurance exercise modulates growth differentiation factor 11 in cerebrospinal fluid of healthy young adults.

    doi: 10.3389/fendo.2023.1137048

    Figure Lengend Snippet: FIGURE 3 Heat map depicting associations between levels of GDF11 and clinical parameters, as well as their running-induced changes. Data were analyzed using GDF11-specific N-terminus antibody (paired serum samples n=14; paired CSF samples n=12, unpaired CSF samples available only after run n=2). BMI, body mass index; CSF, cerebrospinal fluid; GDF, Growth Differentiation Factor; HRmax, maximal heart rate; S-CK, serum creatinkinase; R, correlation coefficient; VO2max, maximal aerobic capacity. Coefficients of significant correlations (p<0.05) or trends (p<0.1) are presented in numbers.

    Article Snippet: To corroborate the findings, GDF11 C-terminus specific monoclonal antibody was used (recombinant human GDF11 aa299-407, 1:1000, R&D systems, MAB19581, USA) (sample set B, n=13; overlap between A & B sample sets: n=7, Supplementary Figure 1B).

    Techniques: