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human activin riib receptor actriib  (R&D Systems)


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    R&D Systems human activin riib receptor actriib
    Human Activin Riib Receptor Actriib, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+activin+riib+fc+chimera/Recombinant+Human+Activin+RIIB+Fc+Chimera+(NS0-expressed)/pmc11898274-189-39-56
    Average 93 stars, based on 9 article reviews
    human activin riib receptor actriib - by Bioz Stars, 2026-09
    93/100 stars

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    Control:

    Article Title: Fibronectin based scaffold domain proteins that bind to myostatin
    Article Snippet: .. An exemplary control reaction involves treating cells with myostatin alone or myostatin preincubated with an excess of a benchmark myostatin inhibitor such as Human Activin RIIB Fc Chimera (R&D Systems) or ActRIIb-Fc as described in Morrison et al. (Experimental Neurology 2009; 217:258-68). ..

    Article Title: Fibronectin based scaffold domain proteins that bind to myostatin
    Article Snippet: .. An exemplary control reaction involves treating cells with myostatin alone or myostatin preincubated with an excess of a benchmark myostatin inhibitor such as Human Activin RIIB Fc Chimera (R&D Systems) or ActRIIb-Fc as described in Morrison et al. (Experimental Neurology 2009; 217:258-68). ..

    Article Title: Fibronectin based scaffold domain proteins that bind to myostatin
    Article Snippet: .. An exemplary control reaction involves treating cells with myostatin alone or myostatin preincubated with an excess of a benchmark myostatin inhibitor such as Human Activin RIIB Fc Chimera (R&D Systems) or ActRIIb-Fc as described in Morrison et al. (Experimental Neurology 2009; 217:258-68). ..

    Article Title: Fibronectin based scaffold domain proteins that bind to myostatin
    Article Snippet: .. An exemplary control reaction involves treating cells with myostatin alone or myostatin preincubated with an excess of a benchmark myostatin inhibitor such as Human Activin RIIB Fc Chimera (R&D Systems) or ActRIIb-Fc as described in Morrison et al. (Experimental Neurology 2009; 217:258-68). ..



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    human activin riib receptor actriib  (R&D Systems)
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    R&D Systems human activin riib receptor actriib
    Human Activin Riib Receptor Actriib, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+activin+riib+fc+chimera/Recombinant+Human+Activin+RIIB+Fc+Chimera+(NS0-expressed)/pmc11898274-189-39-56
    Average 93 stars, based on 1 article reviews
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    93/100 stars
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    aiib fc  (R&D Systems)
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    R&D Systems aiib fc
    A Western blot of representative B16F1-mS1 and FurKO#2-ctrl or -βA cell SNs, and ImageJ quantification of the proportions of mature, hemicleaved, and uncleaved Activin-A in independent sample preparations from the indicated cell lines used as inputs to test Activin-A binding to immobilized ActRIIB-Fc by plasmon resonance measurements. The microfluidic chamber used to inject cell SNs on a nanoplasmonic <t>chip</t> <t>functionalized</t> with ActRIIB-Fc on gold nanoparticles is depicted on the right. Drops in signal intensity are induced by Activin-A binding to ActRIIB-Fc. B Binding of the different forms of Activin-A was evaluated by injecting the B16F1-βA or FurKO#2-βA cell SNs analyzed in ( A ). B16F1-mS1, or B16F1-Ctrl cells expressing empty lentivirus served as specificity controls. Error bars, SEM ( n = 3 independent experiments); * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, Student’s t -test. C Schematic of the conversion of hemicleaved Activin-A (A70) to A60 by furin cleavage of the second βA subunit, and strategy to monitor the cleavage using anti-Flag and anti-Activin-A (ActA) antibodies. In this model, an allosteric cystine bond (S–S) links the prodomain (violet) of one βA subunit to the C-terminal region (yellow) in A70 and A60. Prodomain that is not covalently attached (light shading) can be displaced by cognate type II receptors. D Anti-Activin-A (top) or anti-Flag Western blots (bottom) of A70 in SN of FurKO#1 cells expressing Flag-tagged 27F-βA analyzed before (input) and after pull-down by <t>AIIB-Fc.</t> SN of B16-F1 cells, and of mock-transfected FurKO#1 cells served as controls. Arrow, cleaved prodomain; n.s. non-specific. E Anti-Activin-A (top) or anti-Flag (bottom) Western blot of the indicated Flag-tagged Activin-A constructs after pull-down as in ( D ), but on reducing gels. FurKO#1 and B16-F1 control SNs used to pull down Flag-tagged A70 and A60 encoded by 130F-βA or 146-βA were as in Fig. . F LC–MS analysis and spectral counts of peptides mapping to Activin-A in samples collected in ( E ). Data represent two pull-down experiments, one using ActRIIA-Fc and the other using AIIB-Fc. Schemas were created using BioRender.com .
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    recombinant aiib fc receptor  (R&D Systems)
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    R&D Systems recombinant aiib fc receptor
    A Western blot of representative B16F1-mS1 and FurKO#2-ctrl or -βA cell SNs, and ImageJ quantification of the proportions of mature, hemicleaved, and uncleaved Activin-A in independent sample preparations from the indicated cell lines used as inputs to test Activin-A binding to immobilized ActRIIB-Fc by plasmon resonance measurements. The microfluidic chamber used to inject cell SNs on a nanoplasmonic <t>chip</t> <t>functionalized</t> with ActRIIB-Fc on gold nanoparticles is depicted on the right. Drops in signal intensity are induced by Activin-A binding to ActRIIB-Fc. B Binding of the different forms of Activin-A was evaluated by injecting the B16F1-βA or FurKO#2-βA cell SNs analyzed in ( A ). B16F1-mS1, or B16F1-Ctrl cells expressing empty lentivirus served as specificity controls. Error bars, SEM ( n = 3 independent experiments); * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, Student’s t -test. C Schematic of the conversion of hemicleaved Activin-A (A70) to A60 by furin cleavage of the second βA subunit, and strategy to monitor the cleavage using anti-Flag and anti-Activin-A (ActA) antibodies. In this model, an allosteric cystine bond (S–S) links the prodomain (violet) of one βA subunit to the C-terminal region (yellow) in A70 and A60. Prodomain that is not covalently attached (light shading) can be displaced by cognate type II receptors. D Anti-Activin-A (top) or anti-Flag Western blots (bottom) of A70 in SN of FurKO#1 cells expressing Flag-tagged 27F-βA analyzed before (input) and after pull-down by <t>AIIB-Fc.</t> SN of B16-F1 cells, and of mock-transfected FurKO#1 cells served as controls. Arrow, cleaved prodomain; n.s. non-specific. E Anti-Activin-A (top) or anti-Flag (bottom) Western blot of the indicated Flag-tagged Activin-A constructs after pull-down as in ( D ), but on reducing gels. FurKO#1 and B16-F1 control SNs used to pull down Flag-tagged A70 and A60 encoded by 130F-βA or 146-βA were as in Fig. . F LC–MS analysis and spectral counts of peptides mapping to Activin-A in samples collected in ( E ). Data represent two pull-down experiments, one using ActRIIA-Fc and the other using AIIB-Fc. Schemas were created using BioRender.com .
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    activin riib fc  (R&D Systems)
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    A Western blot of representative B16F1-mS1 and FurKO#2-ctrl or -βA cell SNs, and ImageJ quantification of the proportions of mature, hemicleaved, and uncleaved Activin-A in independent sample preparations from the indicated cell lines used as inputs to test Activin-A binding to immobilized ActRIIB-Fc by plasmon resonance measurements. The microfluidic chamber used to inject cell SNs on a nanoplasmonic <t>chip</t> <t>functionalized</t> with ActRIIB-Fc on gold nanoparticles is depicted on the right. Drops in signal intensity are induced by Activin-A binding to ActRIIB-Fc. B Binding of the different forms of Activin-A was evaluated by injecting the B16F1-βA or FurKO#2-βA cell SNs analyzed in ( A ). B16F1-mS1, or B16F1-Ctrl cells expressing empty lentivirus served as specificity controls. Error bars, SEM ( n = 3 independent experiments); * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, Student’s t -test. C Schematic of the conversion of hemicleaved Activin-A (A70) to A60 by furin cleavage of the second βA subunit, and strategy to monitor the cleavage using anti-Flag and anti-Activin-A (ActA) antibodies. In this model, an allosteric cystine bond (S–S) links the prodomain (violet) of one βA subunit to the C-terminal region (yellow) in A70 and A60. Prodomain that is not covalently attached (light shading) can be displaced by cognate type II receptors. D Anti-Activin-A (top) or anti-Flag Western blots (bottom) of A70 in SN of FurKO#1 cells expressing Flag-tagged 27F-βA analyzed before (input) and after pull-down by <t>AIIB-Fc.</t> SN of B16-F1 cells, and of mock-transfected FurKO#1 cells served as controls. Arrow, cleaved prodomain; n.s. non-specific. E Anti-Activin-A (top) or anti-Flag (bottom) Western blot of the indicated Flag-tagged Activin-A constructs after pull-down as in ( D ), but on reducing gels. FurKO#1 and B16-F1 control SNs used to pull down Flag-tagged A70 and A60 encoded by 130F-βA or 146-βA were as in Fig. . F LC–MS analysis and spectral counts of peptides mapping to Activin-A in samples collected in ( E ). Data represent two pull-down experiments, one using ActRIIA-Fc and the other using AIIB-Fc. Schemas were created using BioRender.com .
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    A Western blot of representative B16F1-mS1 and FurKO#2-ctrl or -βA cell SNs, and ImageJ quantification of the proportions of mature, hemicleaved, and uncleaved Activin-A in independent sample preparations from the indicated cell lines used as inputs to test Activin-A binding to immobilized ActRIIB-Fc by plasmon resonance measurements. The microfluidic chamber used to inject cell SNs on a nanoplasmonic <t>chip</t> <t>functionalized</t> with ActRIIB-Fc on gold nanoparticles is depicted on the right. Drops in signal intensity are induced by Activin-A binding to ActRIIB-Fc. B Binding of the different forms of Activin-A was evaluated by injecting the B16F1-βA or FurKO#2-βA cell SNs analyzed in ( A ). B16F1-mS1, or B16F1-Ctrl cells expressing empty lentivirus served as specificity controls. Error bars, SEM ( n = 3 independent experiments); * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, Student’s t -test. C Schematic of the conversion of hemicleaved Activin-A (A70) to A60 by furin cleavage of the second βA subunit, and strategy to monitor the cleavage using anti-Flag and anti-Activin-A (ActA) antibodies. In this model, an allosteric cystine bond (S–S) links the prodomain (violet) of one βA subunit to the C-terminal region (yellow) in A70 and A60. Prodomain that is not covalently attached (light shading) can be displaced by cognate type II receptors. D Anti-Activin-A (top) or anti-Flag Western blots (bottom) of A70 in SN of FurKO#1 cells expressing Flag-tagged 27F-βA analyzed before (input) and after pull-down by <t>AIIB-Fc.</t> SN of B16-F1 cells, and of mock-transfected FurKO#1 cells served as controls. Arrow, cleaved prodomain; n.s. non-specific. E Anti-Activin-A (top) or anti-Flag (bottom) Western blot of the indicated Flag-tagged Activin-A constructs after pull-down as in ( D ), but on reducing gels. FurKO#1 and B16-F1 control SNs used to pull down Flag-tagged A70 and A60 encoded by 130F-βA or 146-βA were as in Fig. . F LC–MS analysis and spectral counts of peptides mapping to Activin-A in samples collected in ( E ). Data represent two pull-down experiments, one using ActRIIA-Fc and the other using AIIB-Fc. Schemas were created using BioRender.com .
    Human Activin Riib Fc Chimera, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+activin+riib+fc+chimera/Recombinant+Human+Activin+RIIB+Fc+Chimera+(NS0-expressed)/us11813315-643-23-28
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    activin ria alk2 fc  (R&D Systems)
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    R&D Systems activin ria alk2 fc
    A Western blot of representative B16F1-mS1 and FurKO#2-ctrl or -βA cell SNs, and ImageJ quantification of the proportions of mature, hemicleaved, and uncleaved Activin-A in independent sample preparations from the indicated cell lines used as inputs to test Activin-A binding to immobilized ActRIIB-Fc by plasmon resonance measurements. The microfluidic chamber used to inject cell SNs on a nanoplasmonic <t>chip</t> <t>functionalized</t> with ActRIIB-Fc on gold nanoparticles is depicted on the right. Drops in signal intensity are induced by Activin-A binding to ActRIIB-Fc. B Binding of the different forms of Activin-A was evaluated by injecting the B16F1-βA or FurKO#2-βA cell SNs analyzed in ( A ). B16F1-mS1, or B16F1-Ctrl cells expressing empty lentivirus served as specificity controls. Error bars, SEM ( n = 3 independent experiments); * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, Student’s t -test. C Schematic of the conversion of hemicleaved Activin-A (A70) to A60 by furin cleavage of the second βA subunit, and strategy to monitor the cleavage using anti-Flag and anti-Activin-A (ActA) antibodies. In this model, an allosteric cystine bond (S–S) links the prodomain (violet) of one βA subunit to the C-terminal region (yellow) in A70 and A60. Prodomain that is not covalently attached (light shading) can be displaced by cognate type II receptors. D Anti-Activin-A (top) or anti-Flag Western blots (bottom) of A70 in SN of FurKO#1 cells expressing Flag-tagged 27F-βA analyzed before (input) and after pull-down by <t>AIIB-Fc.</t> SN of B16-F1 cells, and of mock-transfected FurKO#1 cells served as controls. Arrow, cleaved prodomain; n.s. non-specific. E Anti-Activin-A (top) or anti-Flag (bottom) Western blot of the indicated Flag-tagged Activin-A constructs after pull-down as in ( D ), but on reducing gels. FurKO#1 and B16-F1 control SNs used to pull down Flag-tagged A70 and A60 encoded by 130F-βA or 146-βA were as in Fig. . F LC–MS analysis and spectral counts of peptides mapping to Activin-A in samples collected in ( E ). Data represent two pull-down experiments, one using ActRIIA-Fc and the other using AIIB-Fc. Schemas were created using BioRender.com .
    Activin Ria Alk2 Fc, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    fc fusion construct  (R&D Systems Hematology)
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    A Western blot of representative B16F1-mS1 and FurKO#2-ctrl or -βA cell SNs, and ImageJ quantification of the proportions of mature, hemicleaved, and uncleaved Activin-A in independent sample preparations from the indicated cell lines used as inputs to test Activin-A binding to immobilized ActRIIB-Fc by plasmon resonance measurements. The microfluidic chamber used to inject cell SNs on a nanoplasmonic <t>chip</t> <t>functionalized</t> with ActRIIB-Fc on gold nanoparticles is depicted on the right. Drops in signal intensity are induced by Activin-A binding to ActRIIB-Fc. B Binding of the different forms of Activin-A was evaluated by injecting the B16F1-βA or FurKO#2-βA cell SNs analyzed in ( A ). B16F1-mS1, or B16F1-Ctrl cells expressing empty lentivirus served as specificity controls. Error bars, SEM ( n = 3 independent experiments); * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, Student’s t -test. C Schematic of the conversion of hemicleaved Activin-A (A70) to A60 by furin cleavage of the second βA subunit, and strategy to monitor the cleavage using anti-Flag and anti-Activin-A (ActA) antibodies. In this model, an allosteric cystine bond (S–S) links the prodomain (violet) of one βA subunit to the C-terminal region (yellow) in A70 and A60. Prodomain that is not covalently attached (light shading) can be displaced by cognate type II receptors. D Anti-Activin-A (top) or anti-Flag Western blots (bottom) of A70 in SN of FurKO#1 cells expressing Flag-tagged 27F-βA analyzed before (input) and after pull-down by <t>AIIB-Fc.</t> SN of B16-F1 cells, and of mock-transfected FurKO#1 cells served as controls. Arrow, cleaved prodomain; n.s. non-specific. E Anti-Activin-A (top) or anti-Flag (bottom) Western blot of the indicated Flag-tagged Activin-A constructs after pull-down as in ( D ), but on reducing gels. FurKO#1 and B16-F1 control SNs used to pull down Flag-tagged A70 and A60 encoded by 130F-βA or 146-βA were as in Fig. . F LC–MS analysis and spectral counts of peptides mapping to Activin-A in samples collected in ( E ). Data represent two pull-down experiments, one using ActRIIA-Fc and the other using AIIB-Fc. Schemas were created using BioRender.com .
    Fc Fusion Construct, supplied by R&D Systems Hematology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    actriib fc recombinant human activin riib fc chimera  (R&D Systems)
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    R&D Systems actriib fc recombinant human activin riib fc chimera
    A Western blot of representative B16F1-mS1 and FurKO#2-ctrl or -βA cell SNs, and ImageJ quantification of the proportions of mature, hemicleaved, and uncleaved Activin-A in independent sample preparations from the indicated cell lines used as inputs to test Activin-A binding to immobilized ActRIIB-Fc by plasmon resonance measurements. The microfluidic chamber used to inject cell SNs on a nanoplasmonic <t>chip</t> <t>functionalized</t> with ActRIIB-Fc on gold nanoparticles is depicted on the right. Drops in signal intensity are induced by Activin-A binding to ActRIIB-Fc. B Binding of the different forms of Activin-A was evaluated by injecting the B16F1-βA or FurKO#2-βA cell SNs analyzed in ( A ). B16F1-mS1, or B16F1-Ctrl cells expressing empty lentivirus served as specificity controls. Error bars, SEM ( n = 3 independent experiments); * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, Student’s t -test. C Schematic of the conversion of hemicleaved Activin-A (A70) to A60 by furin cleavage of the second βA subunit, and strategy to monitor the cleavage using anti-Flag and anti-Activin-A (ActA) antibodies. In this model, an allosteric cystine bond (S–S) links the prodomain (violet) of one βA subunit to the C-terminal region (yellow) in A70 and A60. Prodomain that is not covalently attached (light shading) can be displaced by cognate type II receptors. D Anti-Activin-A (top) or anti-Flag Western blots (bottom) of A70 in SN of FurKO#1 cells expressing Flag-tagged 27F-βA analyzed before (input) and after pull-down by <t>AIIB-Fc.</t> SN of B16-F1 cells, and of mock-transfected FurKO#1 cells served as controls. Arrow, cleaved prodomain; n.s. non-specific. E Anti-Activin-A (top) or anti-Flag (bottom) Western blot of the indicated Flag-tagged Activin-A constructs after pull-down as in ( D ), but on reducing gels. FurKO#1 and B16-F1 control SNs used to pull down Flag-tagged A70 and A60 encoded by 130F-βA or 146-βA were as in Fig. . F LC–MS analysis and spectral counts of peptides mapping to Activin-A in samples collected in ( E ). Data represent two pull-down experiments, one using ActRIIA-Fc and the other using AIIB-Fc. Schemas were created using BioRender.com .
    Actriib Fc Recombinant Human Activin Riib Fc Chimera, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    A Western blot of representative B16F1-mS1 and FurKO#2-ctrl or -βA cell SNs, and ImageJ quantification of the proportions of mature, hemicleaved, and uncleaved Activin-A in independent sample preparations from the indicated cell lines used as inputs to test Activin-A binding to immobilized ActRIIB-Fc by plasmon resonance measurements. The microfluidic chamber used to inject cell SNs on a nanoplasmonic chip functionalized with ActRIIB-Fc on gold nanoparticles is depicted on the right. Drops in signal intensity are induced by Activin-A binding to ActRIIB-Fc. B Binding of the different forms of Activin-A was evaluated by injecting the B16F1-βA or FurKO#2-βA cell SNs analyzed in ( A ). B16F1-mS1, or B16F1-Ctrl cells expressing empty lentivirus served as specificity controls. Error bars, SEM ( n = 3 independent experiments); * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, Student’s t -test. C Schematic of the conversion of hemicleaved Activin-A (A70) to A60 by furin cleavage of the second βA subunit, and strategy to monitor the cleavage using anti-Flag and anti-Activin-A (ActA) antibodies. In this model, an allosteric cystine bond (S–S) links the prodomain (violet) of one βA subunit to the C-terminal region (yellow) in A70 and A60. Prodomain that is not covalently attached (light shading) can be displaced by cognate type II receptors. D Anti-Activin-A (top) or anti-Flag Western blots (bottom) of A70 in SN of FurKO#1 cells expressing Flag-tagged 27F-βA analyzed before (input) and after pull-down by AIIB-Fc. SN of B16-F1 cells, and of mock-transfected FurKO#1 cells served as controls. Arrow, cleaved prodomain; n.s. non-specific. E Anti-Activin-A (top) or anti-Flag (bottom) Western blot of the indicated Flag-tagged Activin-A constructs after pull-down as in ( D ), but on reducing gels. FurKO#1 and B16-F1 control SNs used to pull down Flag-tagged A70 and A60 encoded by 130F-βA or 146-βA were as in Fig. . F LC–MS analysis and spectral counts of peptides mapping to Activin-A in samples collected in ( E ). Data represent two pull-down experiments, one using ActRIIA-Fc and the other using AIIB-Fc. Schemas were created using BioRender.com .

    Journal: Communications Biology

    Article Title: Stepwise release of Activin-A from its inhibitory prodomain is modulated by cysteines and requires furin coexpression to promote melanoma growth

    doi: 10.1038/s42003-024-07053-0

    Figure Lengend Snippet: A Western blot of representative B16F1-mS1 and FurKO#2-ctrl or -βA cell SNs, and ImageJ quantification of the proportions of mature, hemicleaved, and uncleaved Activin-A in independent sample preparations from the indicated cell lines used as inputs to test Activin-A binding to immobilized ActRIIB-Fc by plasmon resonance measurements. The microfluidic chamber used to inject cell SNs on a nanoplasmonic chip functionalized with ActRIIB-Fc on gold nanoparticles is depicted on the right. Drops in signal intensity are induced by Activin-A binding to ActRIIB-Fc. B Binding of the different forms of Activin-A was evaluated by injecting the B16F1-βA or FurKO#2-βA cell SNs analyzed in ( A ). B16F1-mS1, or B16F1-Ctrl cells expressing empty lentivirus served as specificity controls. Error bars, SEM ( n = 3 independent experiments); * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, Student’s t -test. C Schematic of the conversion of hemicleaved Activin-A (A70) to A60 by furin cleavage of the second βA subunit, and strategy to monitor the cleavage using anti-Flag and anti-Activin-A (ActA) antibodies. In this model, an allosteric cystine bond (S–S) links the prodomain (violet) of one βA subunit to the C-terminal region (yellow) in A70 and A60. Prodomain that is not covalently attached (light shading) can be displaced by cognate type II receptors. D Anti-Activin-A (top) or anti-Flag Western blots (bottom) of A70 in SN of FurKO#1 cells expressing Flag-tagged 27F-βA analyzed before (input) and after pull-down by AIIB-Fc. SN of B16-F1 cells, and of mock-transfected FurKO#1 cells served as controls. Arrow, cleaved prodomain; n.s. non-specific. E Anti-Activin-A (top) or anti-Flag (bottom) Western blot of the indicated Flag-tagged Activin-A constructs after pull-down as in ( D ), but on reducing gels. FurKO#1 and B16-F1 control SNs used to pull down Flag-tagged A70 and A60 encoded by 130F-βA or 146-βA were as in Fig. . F LC–MS analysis and spectral counts of peptides mapping to Activin-A in samples collected in ( E ). Data represent two pull-down experiments, one using ActRIIA-Fc and the other using AIIB-Fc. Schemas were created using BioRender.com .

    Article Snippet: For plasmon resonance measurements, gold nanohole array plasmonic chips fabricated at EPFL , were functionalized by precoating with anti-Activin-A antibody (BAM050, R&D Systems), or with AIIB-Fc (339-RBB-100).

    Techniques: Western Blot, Binding Assay, Expressing, Transfection, Construct, Control, Liquid Chromatography with Mass Spectroscopy