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acvr1b mab222  (R&D Systems)


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    Structured Review

    R&D Systems acvr1b mab222
    The canonical activin A pathway. Activin A is composed of inhibin βA subunits (βA) and binds to activin receptor type II and IIB (ACVR2/2B). Inhibin, composed of a βA and α subunit, competitively binds and sequesters ACVR2/2B, ultimately inhibiting the activin axis. Contrariwise, activin binding ultimately forms a Smad transcriptions complex (comprised of Smad 2, 3 and 4), the phosphorylation of activin receptor type IB <t>(ACVR1B)</t> subsequently stimulating and activating the Smad transcription complex, thereby eliciting downstream cellular behaviors such as proliferation inhibition, apoptosis, and epithelial mesenchymal transition. Of note, activin may have proliferative effects outside of this axis, as described in the introduction and discussion.
    Acvr1b Mab222, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+acvr1b/Human+Activin+RIB%2FALK-4+Antibody/pmc11285815-6-0-5
    Average 91 stars, based on 7 article reviews
    acvr1b mab222 - by Bioz Stars, 2026-09
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    Images

    1) Product Images from "Potential roles of activin in head and neck squamous cell carcinoma progression in epithelial-mesenchymal transition, metastasis, and mortality"

    Article Title: Potential roles of activin in head and neck squamous cell carcinoma progression in epithelial-mesenchymal transition, metastasis, and mortality

    Journal: Anticancer research

    doi: 10.21873/anticanres.16733

    The canonical activin A pathway. Activin A is composed of inhibin βA subunits (βA) and binds to activin receptor type II and IIB (ACVR2/2B). Inhibin, composed of a βA and α subunit, competitively binds and sequesters ACVR2/2B, ultimately inhibiting the activin axis. Contrariwise, activin binding ultimately forms a Smad transcriptions complex (comprised of Smad 2, 3 and 4), the phosphorylation of activin receptor type IB (ACVR1B) subsequently stimulating and activating the Smad transcription complex, thereby eliciting downstream cellular behaviors such as proliferation inhibition, apoptosis, and epithelial mesenchymal transition. Of note, activin may have proliferative effects outside of this axis, as described in the introduction and discussion.
    Figure Legend Snippet: The canonical activin A pathway. Activin A is composed of inhibin βA subunits (βA) and binds to activin receptor type II and IIB (ACVR2/2B). Inhibin, composed of a βA and α subunit, competitively binds and sequesters ACVR2/2B, ultimately inhibiting the activin axis. Contrariwise, activin binding ultimately forms a Smad transcriptions complex (comprised of Smad 2, 3 and 4), the phosphorylation of activin receptor type IB (ACVR1B) subsequently stimulating and activating the Smad transcription complex, thereby eliciting downstream cellular behaviors such as proliferation inhibition, apoptosis, and epithelial mesenchymal transition. Of note, activin may have proliferative effects outside of this axis, as described in the introduction and discussion.

    Techniques Used: Binding Assay, Phospho-proteomics, Inhibition

    Immunohistochemistry expression of inhibin subunits (INHA, INHBA, INHBB) and activin receptors  (ACVR1B,  ACVR2, ACVR2B) in five normal, 15 oral premalignant (OPL) and 12 HNSCC tumor tissue samples. Chi-square tests were employed for analysis with p <0.05 being significant; diffuse and focal positivity were scored as positive. Premalignant and malignant lesions demonstrated a statistically significant increase in the prevalence of ligand inhibin βA (INHBA) (χ 2 (2, N = 32) = 18.98, p < .0001) (Row 6) as well as ACVR1B (χ 2 (2, N = 32) = 11.52, p < .0032) (Row 11). There was also a decreased prevalence of ACVR2B among pre-malignant and malignant lesions in comparison to normal mucosa (χ 2 (2, N = 32) = 0.0018, p < .0018) (Row 13).
    Figure Legend Snippet: Immunohistochemistry expression of inhibin subunits (INHA, INHBA, INHBB) and activin receptors (ACVR1B, ACVR2, ACVR2B) in five normal, 15 oral premalignant (OPL) and 12 HNSCC tumor tissue samples. Chi-square tests were employed for analysis with p <0.05 being significant; diffuse and focal positivity were scored as positive. Premalignant and malignant lesions demonstrated a statistically significant increase in the prevalence of ligand inhibin βA (INHBA) (χ 2 (2, N = 32) = 18.98, p < .0001) (Row 6) as well as ACVR1B (χ 2 (2, N = 32) = 11.52, p < .0032) (Row 11). There was also a decreased prevalence of ACVR2B among pre-malignant and malignant lesions in comparison to normal mucosa (χ 2 (2, N = 32) = 0.0018, p < .0018) (Row 13).

    Techniques Used: Immunohistochemistry, Expressing, Comparison

    Immunohistochemistry
    Figure Legend Snippet: Immunohistochemistry

    Techniques Used:

    Related Articles

    other:

    Article Title: M2 microglia/macrophages drive oligodendrocyte differentiation during CNS remyelination
    Article Snippet: Antibodies against activin-A or its receptors include goat anti-activin-A (AF338), anti-Acvr1B (AF1477), anti-Acvr2A (AF340), and anti-Acvr2B (AF339) (all from R & D Systems, 1:40).



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    IGFBP7 and Activin A. ( A ) The histogram shows the percentage of (P) cycling, (Q) quiescent, (St) stressed, and (Sen) senescent cells in MSCs cultures incubated with Activin A (ACV) and/or IGFBP7 and/or antibodies targeting Activin A receptors (AbαACVR1, AbαACVR1B). Data are expressed with standard deviation (n = 3 biological replicates). The symbol ** p < 0.01 represents statistical significance between the control and treated samples. The symbols ### p < 0.001 and ## p < 0.01 represent statistical significance between the indicated samples. On the right, immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7 and Activin A. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-Activin A antibody. Input: western blot performed on proteins present in culture medium; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. ( B ) SMAD pathways. Representative western blot analysis of nuclear and cytoplasmic levels of phosphorylated-SMAD2/3 (pSMAD2/3), SMAD2/3, phosphorylated-SMAD1/5 (pSMAD1/5), SMAD1/5 in cells incubated with IGFBP7 and/or Activin A. GAPDH and Histone 4 (H4) were used as cytoplasmic and nuclear markers, respectively. The histograms show the cytoplasmic and nuclear pSMAD2-3/SMAD2-3 and pSMAD1-5/SMAD1-5 ratios in the different experimental conditions. Data are expressed with standard deviation (n = 3 biological replicates). In the histograms, the symbols on the white bars *** p < 0.001 and ** p < 0.01 represent a statistical significance between the control and treated samples; the symbols on the blue bars ### p < 0.001 and ## p < 0.01 represent a statistical significance between the control and treated samples. ( C ) On the left, representative immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-ACVR1 and <t>anti-ACVR1B</t> antibodies. Input: western blot performed on proteins present in secretome; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. On the right, representative images of Duolink assay to identify physical proximity between IGFBP7 and ACVR1 and <t>ACVR1B.</t> The red dots represent a close interaction between IGFBP7 and ACVR1 or ACVR1B. The nuclei were DAPI stained with (blue). The scale bar corresponds to 100 microns
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    The canonical activin A pathway. Activin A is composed of inhibin βA subunits (βA) and binds to activin receptor type II and IIB (ACVR2/2B). Inhibin, composed of a βA and α subunit, competitively binds and sequesters ACVR2/2B, ultimately inhibiting the activin axis. Contrariwise, activin binding ultimately forms a Smad transcriptions complex (comprised of Smad 2, 3 and 4), the phosphorylation of activin receptor type IB <t>(ACVR1B)</t> subsequently stimulating and activating the Smad transcription complex, thereby eliciting downstream cellular behaviors such as proliferation inhibition, apoptosis, and epithelial mesenchymal transition. Of note, activin may have proliferative effects outside of this axis, as described in the introduction and discussion.
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    The canonical activin A pathway. Activin A is composed of inhibin βA subunits (βA) and binds to activin receptor type II and IIB (ACVR2/2B). Inhibin, composed of a βA and α subunit, competitively binds and sequesters ACVR2/2B, ultimately inhibiting the activin axis. Contrariwise, activin binding ultimately forms a Smad transcriptions complex (comprised of Smad 2, 3 and 4), the phosphorylation of activin receptor type IB <t>(ACVR1B)</t> subsequently stimulating and activating the Smad transcription complex, thereby eliciting downstream cellular behaviors such as proliferation inhibition, apoptosis, and epithelial mesenchymal transition. Of note, activin may have proliferative effects outside of this axis, as described in the introduction and discussion.
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    Image Search Results


    Primers used for RT-qPCR.

    Journal: Frontiers in Molecular Biosciences

    Article Title: Expression and distribution of activin-follistatin-inhibin axis in the urinary bladder

    doi: 10.3389/fmolb.2025.1519977

    Figure Lengend Snippet: Primers used for RT-qPCR.

    Article Snippet: Acvr1b , BIOSS , Bs-6018R , IF, 1:100.

    Techniques: Sequencing

    Antibody list.

    Journal: Frontiers in Molecular Biosciences

    Article Title: Expression and distribution of activin-follistatin-inhibin axis in the urinary bladder

    doi: 10.3389/fmolb.2025.1519977

    Figure Lengend Snippet: Antibody list.

    Article Snippet: Acvr1b , BIOSS , Bs-6018R , IF, 1:100.

    Techniques:

    mRNA expression of AFI axis family members in the bladder of male and female mice. (A) Differences in mRNA expression of Inha, Inhba, Inhbb, Inhbc, Inhbe, and Fst in the bladder of male and female mice. (B) Differences in mRNA expression of Acvr1, Acvr1b, Acvr1c, Acvr2a, and Acvr2b in the bladder of male and female mice (n = 3, Data were analyzed with the use of Student’s t-test, **p < 0.01, ***p < 0.001).

    Journal: Frontiers in Molecular Biosciences

    Article Title: Expression and distribution of activin-follistatin-inhibin axis in the urinary bladder

    doi: 10.3389/fmolb.2025.1519977

    Figure Lengend Snippet: mRNA expression of AFI axis family members in the bladder of male and female mice. (A) Differences in mRNA expression of Inha, Inhba, Inhbb, Inhbc, Inhbe, and Fst in the bladder of male and female mice. (B) Differences in mRNA expression of Acvr1, Acvr1b, Acvr1c, Acvr2a, and Acvr2b in the bladder of male and female mice (n = 3, Data were analyzed with the use of Student’s t-test, **p < 0.01, ***p < 0.001).

    Article Snippet: Acvr1b , BIOSS , Bs-6018R , IF, 1:100.

    Techniques: Expressing

    Protein expression of AFI axis family members in the bladder of male and female mice. (A–G) Western blot analysis of INHA (A) , INHBA (B) , INHBE (C) , FST (D) , ACVR1 (E) , ACVR1B (F) , ACVR2B (G) in both male and female mouse bladder (25 μg protein loaded). (H) Differences in protein expression of AFI axis family members in the bladder of male and female mice. (n = 4, molecular values of major detected protein species are indicated at the right of each panel. Data were analyzed with the use of a two-tailed Student’s t-test, **p < 0.01, ***p < 0.001).

    Journal: Frontiers in Molecular Biosciences

    Article Title: Expression and distribution of activin-follistatin-inhibin axis in the urinary bladder

    doi: 10.3389/fmolb.2025.1519977

    Figure Lengend Snippet: Protein expression of AFI axis family members in the bladder of male and female mice. (A–G) Western blot analysis of INHA (A) , INHBA (B) , INHBE (C) , FST (D) , ACVR1 (E) , ACVR1B (F) , ACVR2B (G) in both male and female mouse bladder (25 μg protein loaded). (H) Differences in protein expression of AFI axis family members in the bladder of male and female mice. (n = 4, molecular values of major detected protein species are indicated at the right of each panel. Data were analyzed with the use of a two-tailed Student’s t-test, **p < 0.01, ***p < 0.001).

    Article Snippet: Acvr1b , BIOSS , Bs-6018R , IF, 1:100.

    Techniques: Expressing, Western Blot, Two Tailed Test

    Localization of ACVR1B in mouse bladder. Cryosections of mouse bladder tissue were labeled with ACVR1B antibody (green) and ALPL (A) , or antibodies to ENTPD3 (B) or KRT5 (C) ; all displayed in red. Nuclei were labeled with DAPI (blue). Far right : merged images. L, bladder lumen. U, urothelium. Scale bars = 10 μm.

    Journal: Frontiers in Molecular Biosciences

    Article Title: Expression and distribution of activin-follistatin-inhibin axis in the urinary bladder

    doi: 10.3389/fmolb.2025.1519977

    Figure Lengend Snippet: Localization of ACVR1B in mouse bladder. Cryosections of mouse bladder tissue were labeled with ACVR1B antibody (green) and ALPL (A) , or antibodies to ENTPD3 (B) or KRT5 (C) ; all displayed in red. Nuclei were labeled with DAPI (blue). Far right : merged images. L, bladder lumen. U, urothelium. Scale bars = 10 μm.

    Article Snippet: Acvr1b , BIOSS , Bs-6018R , IF, 1:100.

    Techniques: Labeling

    Location and possible mode of action of AFI family members in the bladder. Possible modes of action of 7 family members in the normal (A) and injured (B) uroepithelium. In normal urothelium, a layer of myofibroblasts under the FST barrier further separates activin A from urothelial cells. In injured urothelium, the FST and myofibroblast barriers may be disrupted, allowing activin A to cross the barrier and act as a paracrine signal to activate the ACVR2B/ACVR1B receptor complex in urothelium.

    Journal: Frontiers in Molecular Biosciences

    Article Title: Expression and distribution of activin-follistatin-inhibin axis in the urinary bladder

    doi: 10.3389/fmolb.2025.1519977

    Figure Lengend Snippet: Location and possible mode of action of AFI family members in the bladder. Possible modes of action of 7 family members in the normal (A) and injured (B) uroepithelium. In normal urothelium, a layer of myofibroblasts under the FST barrier further separates activin A from urothelial cells. In injured urothelium, the FST and myofibroblast barriers may be disrupted, allowing activin A to cross the barrier and act as a paracrine signal to activate the ACVR2B/ACVR1B receptor complex in urothelium.

    Article Snippet: Acvr1b , BIOSS , Bs-6018R , IF, 1:100.

    Techniques:

    GDF-9 activates ACVR1B, resulting in SMAD2 phosphorylation in the nucleus, ultimately rescuing ovarian function.

    Journal: Science Advances

    Article Title: Repair of female reproductive function by GDF-9–overexpressing extracellular vesicles via ACVR1B/SMAD2 regulation in ovarian granulosa

    doi: 10.1126/sciadv.adw9006

    Figure Lengend Snippet: GDF-9 activates ACVR1B, resulting in SMAD2 phosphorylation in the nucleus, ultimately rescuing ovarian function.

    Article Snippet: Following this, the tissue sections were incubated at 4°C for 16 hours with primary antibodies targeting ACVR1B (Proteintech, 83026-6-RR), FSHR (Invitrogen, PA5-50963), or SMAD2 (Invitrogen, 51-1300).

    Techniques: Phospho-proteomics

    ( A ) Schematic illustration of rat DO models, sampled and analyzed by total RNA-seq. ( B ) KEGG pathway enrichment analysis revealing the cytokine-cytokine receptor interaction signaling pathway. ( C ) Volcano plot of RNA-seq analysis. ( D and E ) Western blot detection of GDF-9, ACVR1B, SMAD2, and the phosphorylation status of SMAD2. ( F and G ) Western blot analysis showing that inhibition of GDF-9 gene expression prevents EVs from stimulating GDF-9 signaling, leading to decreased protein levels of ACVR1B and SMAD2/p-SMAD2. n = 3. Data are presented as means ± SD. * P < 0.0.5, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. This figure was created in part using BioRender.com . Created in BioRender. Zhang, S. (2025) https://BioRender.com/k36cu40 .

    Journal: Science Advances

    Article Title: Repair of female reproductive function by GDF-9–overexpressing extracellular vesicles via ACVR1B/SMAD2 regulation in ovarian granulosa

    doi: 10.1126/sciadv.adw9006

    Figure Lengend Snippet: ( A ) Schematic illustration of rat DO models, sampled and analyzed by total RNA-seq. ( B ) KEGG pathway enrichment analysis revealing the cytokine-cytokine receptor interaction signaling pathway. ( C ) Volcano plot of RNA-seq analysis. ( D and E ) Western blot detection of GDF-9, ACVR1B, SMAD2, and the phosphorylation status of SMAD2. ( F and G ) Western blot analysis showing that inhibition of GDF-9 gene expression prevents EVs from stimulating GDF-9 signaling, leading to decreased protein levels of ACVR1B and SMAD2/p-SMAD2. n = 3. Data are presented as means ± SD. * P < 0.0.5, ** P < 0.01, *** P < 0.001, **** P < 0.0001; ns, not significant. This figure was created in part using BioRender.com . Created in BioRender. Zhang, S. (2025) https://BioRender.com/k36cu40 .

    Article Snippet: Following this, the tissue sections were incubated at 4°C for 16 hours with primary antibodies targeting ACVR1B (Proteintech, 83026-6-RR), FSHR (Invitrogen, PA5-50963), or SMAD2 (Invitrogen, 51-1300).

    Techniques: RNA Sequencing, Western Blot, Phospho-proteomics, Inhibition, Gene Expression

    ( A and B ) IHC and IF detection of ACVR1B expression in GCs within ovaries. Representative sections are shown in the top row; black or white boxes indicate magnified regions. Scale bars, 100 μm (A) and 10 μm (B). ( C and D ) Quantification of ACVR1B expression by IHC and average fluorescence intensity of ACVR1B in control, DO, and GOE treatment groups. n = 3. Data are presented as means ± SD. **** P < 0.0001; ns, not significant.

    Journal: Science Advances

    Article Title: Repair of female reproductive function by GDF-9–overexpressing extracellular vesicles via ACVR1B/SMAD2 regulation in ovarian granulosa

    doi: 10.1126/sciadv.adw9006

    Figure Lengend Snippet: ( A and B ) IHC and IF detection of ACVR1B expression in GCs within ovaries. Representative sections are shown in the top row; black or white boxes indicate magnified regions. Scale bars, 100 μm (A) and 10 μm (B). ( C and D ) Quantification of ACVR1B expression by IHC and average fluorescence intensity of ACVR1B in control, DO, and GOE treatment groups. n = 3. Data are presented as means ± SD. **** P < 0.0001; ns, not significant.

    Article Snippet: Following this, the tissue sections were incubated at 4°C for 16 hours with primary antibodies targeting ACVR1B (Proteintech, 83026-6-RR), FSHR (Invitrogen, PA5-50963), or SMAD2 (Invitrogen, 51-1300).

    Techniques: Expressing, Fluorescence, Control

    ( A ) IF detection of FSHR expression in GCs within ovaries. Scale bar, 50 μm. ( B ) IF detection of ACVR1B expression in GCs within ovaries. Scale bar, 50 μm. ( C ) Codetection of FSHR and ACVR1B expression in GCs within ovaries. Scale bar, 5 μm. ( D and E ) Quantification of average fluorescence intensity for FSHR, ACVR1B, and coexpression of both markers in control, DO, and GOE treatment groups. n = 3. Data are presented as means ± SD. * P < 0.0.5, *** P < 0.001, **** P < 0.0001; ns, not significant.

    Journal: Science Advances

    Article Title: Repair of female reproductive function by GDF-9–overexpressing extracellular vesicles via ACVR1B/SMAD2 regulation in ovarian granulosa

    doi: 10.1126/sciadv.adw9006

    Figure Lengend Snippet: ( A ) IF detection of FSHR expression in GCs within ovaries. Scale bar, 50 μm. ( B ) IF detection of ACVR1B expression in GCs within ovaries. Scale bar, 50 μm. ( C ) Codetection of FSHR and ACVR1B expression in GCs within ovaries. Scale bar, 5 μm. ( D and E ) Quantification of average fluorescence intensity for FSHR, ACVR1B, and coexpression of both markers in control, DO, and GOE treatment groups. n = 3. Data are presented as means ± SD. * P < 0.0.5, *** P < 0.001, **** P < 0.0001; ns, not significant.

    Article Snippet: Following this, the tissue sections were incubated at 4°C for 16 hours with primary antibodies targeting ACVR1B (Proteintech, 83026-6-RR), FSHR (Invitrogen, PA5-50963), or SMAD2 (Invitrogen, 51-1300).

    Techniques: Expressing, Fluorescence, Control

    IGFBP7 and Activin A. ( A ) The histogram shows the percentage of (P) cycling, (Q) quiescent, (St) stressed, and (Sen) senescent cells in MSCs cultures incubated with Activin A (ACV) and/or IGFBP7 and/or antibodies targeting Activin A receptors (AbαACVR1, AbαACVR1B). Data are expressed with standard deviation (n = 3 biological replicates). The symbol ** p < 0.01 represents statistical significance between the control and treated samples. The symbols ### p < 0.001 and ## p < 0.01 represent statistical significance between the indicated samples. On the right, immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7 and Activin A. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-Activin A antibody. Input: western blot performed on proteins present in culture medium; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. ( B ) SMAD pathways. Representative western blot analysis of nuclear and cytoplasmic levels of phosphorylated-SMAD2/3 (pSMAD2/3), SMAD2/3, phosphorylated-SMAD1/5 (pSMAD1/5), SMAD1/5 in cells incubated with IGFBP7 and/or Activin A. GAPDH and Histone 4 (H4) were used as cytoplasmic and nuclear markers, respectively. The histograms show the cytoplasmic and nuclear pSMAD2-3/SMAD2-3 and pSMAD1-5/SMAD1-5 ratios in the different experimental conditions. Data are expressed with standard deviation (n = 3 biological replicates). In the histograms, the symbols on the white bars *** p < 0.001 and ** p < 0.01 represent a statistical significance between the control and treated samples; the symbols on the blue bars ### p < 0.001 and ## p < 0.01 represent a statistical significance between the control and treated samples. ( C ) On the left, representative immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-ACVR1 and anti-ACVR1B antibodies. Input: western blot performed on proteins present in secretome; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. On the right, representative images of Duolink assay to identify physical proximity between IGFBP7 and ACVR1 and ACVR1B. The red dots represent a close interaction between IGFBP7 and ACVR1 or ACVR1B. The nuclei were DAPI stained with (blue). The scale bar corresponds to 100 microns

    Journal: Cell Communication and Signaling : CCS

    Article Title: IGFBP7 is a key component of the senescence-associated secretory phenotype (SASP) that induces senescence in healthy cells by modulating the insulin, IGF, and activin A pathways

    doi: 10.1186/s12964-024-01921-2

    Figure Lengend Snippet: IGFBP7 and Activin A. ( A ) The histogram shows the percentage of (P) cycling, (Q) quiescent, (St) stressed, and (Sen) senescent cells in MSCs cultures incubated with Activin A (ACV) and/or IGFBP7 and/or antibodies targeting Activin A receptors (AbαACVR1, AbαACVR1B). Data are expressed with standard deviation (n = 3 biological replicates). The symbol ** p < 0.01 represents statistical significance between the control and treated samples. The symbols ### p < 0.001 and ## p < 0.01 represent statistical significance between the indicated samples. On the right, immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7 and Activin A. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-Activin A antibody. Input: western blot performed on proteins present in culture medium; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. ( B ) SMAD pathways. Representative western blot analysis of nuclear and cytoplasmic levels of phosphorylated-SMAD2/3 (pSMAD2/3), SMAD2/3, phosphorylated-SMAD1/5 (pSMAD1/5), SMAD1/5 in cells incubated with IGFBP7 and/or Activin A. GAPDH and Histone 4 (H4) were used as cytoplasmic and nuclear markers, respectively. The histograms show the cytoplasmic and nuclear pSMAD2-3/SMAD2-3 and pSMAD1-5/SMAD1-5 ratios in the different experimental conditions. Data are expressed with standard deviation (n = 3 biological replicates). In the histograms, the symbols on the white bars *** p < 0.001 and ** p < 0.01 represent a statistical significance between the control and treated samples; the symbols on the blue bars ### p < 0.001 and ## p < 0.01 represent a statistical significance between the control and treated samples. ( C ) On the left, representative immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-ACVR1 and anti-ACVR1B antibodies. Input: western blot performed on proteins present in secretome; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. On the right, representative images of Duolink assay to identify physical proximity between IGFBP7 and ACVR1 and ACVR1B. The red dots represent a close interaction between IGFBP7 and ACVR1 or ACVR1B. The nuclei were DAPI stained with (blue). The scale bar corresponds to 100 microns

    Article Snippet: The Duolink assay was performed according to the manufacturer’s instructions (Sigma Aldrich, MO, USA), using IGFBP7 (Elabscience, TX, USA) with either ACVR1 (Elabscience, TX, USA) or ACVR1B (E-AB-93398, Elabscience, TX, USA) as primary antibodies.

    Techniques: Incubation, Standard Deviation, Control, Immunoprecipitation, Western Blot, Staining

    IGFBP7 Signaling Associated with Senescence. The diagram presents a proposed model of pathways involved in senescence induced by IGFBP7 signaling. The IGFBP7 protein may interact with Insulin, preventing its interaction with cognate receptors and thereby inhibiting Insulin’s anti-senescence and proliferative activities. IGFBP7 may also bind to the IGF1R receptor, redirecting IGF-II to IGF2R, which is associated with IGF-II-induced senescence. Additionally, IGFBP7 and Activin A may bind to each other, mutually blocking their respective pro-senescence activities. In the absence of Activin A, IGFBP7 may bind to ACVR1 and ACVR1B, promoting the onset of senescence

    Journal: Cell Communication and Signaling : CCS

    Article Title: IGFBP7 is a key component of the senescence-associated secretory phenotype (SASP) that induces senescence in healthy cells by modulating the insulin, IGF, and activin A pathways

    doi: 10.1186/s12964-024-01921-2

    Figure Lengend Snippet: IGFBP7 Signaling Associated with Senescence. The diagram presents a proposed model of pathways involved in senescence induced by IGFBP7 signaling. The IGFBP7 protein may interact with Insulin, preventing its interaction with cognate receptors and thereby inhibiting Insulin’s anti-senescence and proliferative activities. IGFBP7 may also bind to the IGF1R receptor, redirecting IGF-II to IGF2R, which is associated with IGF-II-induced senescence. Additionally, IGFBP7 and Activin A may bind to each other, mutually blocking their respective pro-senescence activities. In the absence of Activin A, IGFBP7 may bind to ACVR1 and ACVR1B, promoting the onset of senescence

    Article Snippet: The Duolink assay was performed according to the manufacturer’s instructions (Sigma Aldrich, MO, USA), using IGFBP7 (Elabscience, TX, USA) with either ACVR1 (Elabscience, TX, USA) or ACVR1B (E-AB-93398, Elabscience, TX, USA) as primary antibodies.

    Techniques: Blocking Assay

    IGFBP7 and Activin A. ( A ) The histogram shows the percentage of (P) cycling, (Q) quiescent, (St) stressed, and (Sen) senescent cells in MSCs cultures incubated with Activin A (ACV) and/or IGFBP7 and/or antibodies targeting Activin A receptors (AbαACVR1, AbαACVR1B). Data are expressed with standard deviation (n = 3 biological replicates). The symbol ** p < 0.01 represents statistical significance between the control and treated samples. The symbols ### p < 0.001 and ## p < 0.01 represent statistical significance between the indicated samples. On the right, immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7 and Activin A. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-Activin A antibody. Input: western blot performed on proteins present in culture medium; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. ( B ) SMAD pathways. Representative western blot analysis of nuclear and cytoplasmic levels of phosphorylated-SMAD2/3 (pSMAD2/3), SMAD2/3, phosphorylated-SMAD1/5 (pSMAD1/5), SMAD1/5 in cells incubated with IGFBP7 and/or Activin A. GAPDH and Histone 4 (H4) were used as cytoplasmic and nuclear markers, respectively. The histograms show the cytoplasmic and nuclear pSMAD2-3/SMAD2-3 and pSMAD1-5/SMAD1-5 ratios in the different experimental conditions. Data are expressed with standard deviation (n = 3 biological replicates). In the histograms, the symbols on the white bars *** p < 0.001 and ** p < 0.01 represent a statistical significance between the control and treated samples; the symbols on the blue bars ### p < 0.001 and ## p < 0.01 represent a statistical significance between the control and treated samples. ( C ) On the left, representative immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-ACVR1 and anti-ACVR1B antibodies. Input: western blot performed on proteins present in secretome; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. On the right, representative images of Duolink assay to identify physical proximity between IGFBP7 and ACVR1 and ACVR1B. The red dots represent a close interaction between IGFBP7 and ACVR1 or ACVR1B. The nuclei were DAPI stained with (blue). The scale bar corresponds to 100 microns

    Journal: Cell Communication and Signaling : CCS

    Article Title: IGFBP7 is a key component of the senescence-associated secretory phenotype (SASP) that induces senescence in healthy cells by modulating the insulin, IGF, and activin A pathways

    doi: 10.1186/s12964-024-01921-2

    Figure Lengend Snippet: IGFBP7 and Activin A. ( A ) The histogram shows the percentage of (P) cycling, (Q) quiescent, (St) stressed, and (Sen) senescent cells in MSCs cultures incubated with Activin A (ACV) and/or IGFBP7 and/or antibodies targeting Activin A receptors (AbαACVR1, AbαACVR1B). Data are expressed with standard deviation (n = 3 biological replicates). The symbol ** p < 0.01 represents statistical significance between the control and treated samples. The symbols ### p < 0.001 and ## p < 0.01 represent statistical significance between the indicated samples. On the right, immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7 and Activin A. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-Activin A antibody. Input: western blot performed on proteins present in culture medium; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. ( B ) SMAD pathways. Representative western blot analysis of nuclear and cytoplasmic levels of phosphorylated-SMAD2/3 (pSMAD2/3), SMAD2/3, phosphorylated-SMAD1/5 (pSMAD1/5), SMAD1/5 in cells incubated with IGFBP7 and/or Activin A. GAPDH and Histone 4 (H4) were used as cytoplasmic and nuclear markers, respectively. The histograms show the cytoplasmic and nuclear pSMAD2-3/SMAD2-3 and pSMAD1-5/SMAD1-5 ratios in the different experimental conditions. Data are expressed with standard deviation (n = 3 biological replicates). In the histograms, the symbols on the white bars *** p < 0.001 and ** p < 0.01 represent a statistical significance between the control and treated samples; the symbols on the blue bars ### p < 0.001 and ## p < 0.01 represent a statistical significance between the control and treated samples. ( C ) On the left, representative immunoprecipitation experiment performed on secretome of cells incubated with IGFBP7. The proteins were immunoprecipitated with anti-IGFBP7 antibody and western blot was performed with anti-ACVR1 and anti-ACVR1B antibodies. Input: western blot performed on proteins present in secretome; SUP and IP indicate the supernatant and the immunoprecipitated components of immunoreaction, respectively. On the right, representative images of Duolink assay to identify physical proximity between IGFBP7 and ACVR1 and ACVR1B. The red dots represent a close interaction between IGFBP7 and ACVR1 or ACVR1B. The nuclei were DAPI stained with (blue). The scale bar corresponds to 100 microns

    Article Snippet: MSC cultures were incubated at 37 °C for 30 min with each of the following inhibitors separately: 1 μM U0126 (ERK inhibitor, Sigma-Aldrich), 1 μM GSK690693 (AKT inhibitor, Sigma-Aldrich), 2 μg/ml anti-ACVR1 antibody (Elabscience), or 2 μg/ml anti-ACVR1B antibody (Elabscience).

    Techniques: Incubation, Standard Deviation, Control, Immunoprecipitation, Western Blot, Staining

    IGFBP7 Signaling Associated with Senescence. The diagram presents a proposed model of pathways involved in senescence induced by IGFBP7 signaling. The IGFBP7 protein may interact with Insulin, preventing its interaction with cognate receptors and thereby inhibiting Insulin’s anti-senescence and proliferative activities. IGFBP7 may also bind to the IGF1R receptor, redirecting IGF-II to IGF2R, which is associated with IGF-II-induced senescence. Additionally, IGFBP7 and Activin A may bind to each other, mutually blocking their respective pro-senescence activities. In the absence of Activin A, IGFBP7 may bind to ACVR1 and ACVR1B, promoting the onset of senescence

    Journal: Cell Communication and Signaling : CCS

    Article Title: IGFBP7 is a key component of the senescence-associated secretory phenotype (SASP) that induces senescence in healthy cells by modulating the insulin, IGF, and activin A pathways

    doi: 10.1186/s12964-024-01921-2

    Figure Lengend Snippet: IGFBP7 Signaling Associated with Senescence. The diagram presents a proposed model of pathways involved in senescence induced by IGFBP7 signaling. The IGFBP7 protein may interact with Insulin, preventing its interaction with cognate receptors and thereby inhibiting Insulin’s anti-senescence and proliferative activities. IGFBP7 may also bind to the IGF1R receptor, redirecting IGF-II to IGF2R, which is associated with IGF-II-induced senescence. Additionally, IGFBP7 and Activin A may bind to each other, mutually blocking their respective pro-senescence activities. In the absence of Activin A, IGFBP7 may bind to ACVR1 and ACVR1B, promoting the onset of senescence

    Article Snippet: MSC cultures were incubated at 37 °C for 30 min with each of the following inhibitors separately: 1 μM U0126 (ERK inhibitor, Sigma-Aldrich), 1 μM GSK690693 (AKT inhibitor, Sigma-Aldrich), 2 μg/ml anti-ACVR1 antibody (Elabscience), or 2 μg/ml anti-ACVR1B antibody (Elabscience).

    Techniques: Blocking Assay

    The canonical activin A pathway. Activin A is composed of inhibin βA subunits (βA) and binds to activin receptor type II and IIB (ACVR2/2B). Inhibin, composed of a βA and α subunit, competitively binds and sequesters ACVR2/2B, ultimately inhibiting the activin axis. Contrariwise, activin binding ultimately forms a Smad transcriptions complex (comprised of Smad 2, 3 and 4), the phosphorylation of activin receptor type IB (ACVR1B) subsequently stimulating and activating the Smad transcription complex, thereby eliciting downstream cellular behaviors such as proliferation inhibition, apoptosis, and epithelial mesenchymal transition. Of note, activin may have proliferative effects outside of this axis, as described in the introduction and discussion.

    Journal: Anticancer research

    Article Title: Potential roles of activin in head and neck squamous cell carcinoma progression in epithelial-mesenchymal transition, metastasis, and mortality

    doi: 10.21873/anticanres.16733

    Figure Lengend Snippet: The canonical activin A pathway. Activin A is composed of inhibin βA subunits (βA) and binds to activin receptor type II and IIB (ACVR2/2B). Inhibin, composed of a βA and α subunit, competitively binds and sequesters ACVR2/2B, ultimately inhibiting the activin axis. Contrariwise, activin binding ultimately forms a Smad transcriptions complex (comprised of Smad 2, 3 and 4), the phosphorylation of activin receptor type IB (ACVR1B) subsequently stimulating and activating the Smad transcription complex, thereby eliciting downstream cellular behaviors such as proliferation inhibition, apoptosis, and epithelial mesenchymal transition. Of note, activin may have proliferative effects outside of this axis, as described in the introduction and discussion.

    Article Snippet: ACVR1B (MAB222) , Monoclonal , R & D Systems , 1:200.

    Techniques: Binding Assay, Phospho-proteomics, Inhibition

    Immunohistochemistry expression of inhibin subunits (INHA, INHBA, INHBB) and activin receptors  (ACVR1B,  ACVR2, ACVR2B) in five normal, 15 oral premalignant (OPL) and 12 HNSCC tumor tissue samples. Chi-square tests were employed for analysis with p <0.05 being significant; diffuse and focal positivity were scored as positive. Premalignant and malignant lesions demonstrated a statistically significant increase in the prevalence of ligand inhibin βA (INHBA) (χ 2 (2, N = 32) = 18.98, p < .0001) (Row 6) as well as ACVR1B (χ 2 (2, N = 32) = 11.52, p < .0032) (Row 11). There was also a decreased prevalence of ACVR2B among pre-malignant and malignant lesions in comparison to normal mucosa (χ 2 (2, N = 32) = 0.0018, p < .0018) (Row 13).

    Journal: Anticancer research

    Article Title: Potential roles of activin in head and neck squamous cell carcinoma progression in epithelial-mesenchymal transition, metastasis, and mortality

    doi: 10.21873/anticanres.16733

    Figure Lengend Snippet: Immunohistochemistry expression of inhibin subunits (INHA, INHBA, INHBB) and activin receptors (ACVR1B, ACVR2, ACVR2B) in five normal, 15 oral premalignant (OPL) and 12 HNSCC tumor tissue samples. Chi-square tests were employed for analysis with p <0.05 being significant; diffuse and focal positivity were scored as positive. Premalignant and malignant lesions demonstrated a statistically significant increase in the prevalence of ligand inhibin βA (INHBA) (χ 2 (2, N = 32) = 18.98, p < .0001) (Row 6) as well as ACVR1B (χ 2 (2, N = 32) = 11.52, p < .0032) (Row 11). There was also a decreased prevalence of ACVR2B among pre-malignant and malignant lesions in comparison to normal mucosa (χ 2 (2, N = 32) = 0.0018, p < .0018) (Row 13).

    Article Snippet: ACVR1B (MAB222) , Monoclonal , R & D Systems , 1:200.

    Techniques: Immunohistochemistry, Expressing, Comparison

    Immunohistochemistry

    Journal: Anticancer research

    Article Title: Potential roles of activin in head and neck squamous cell carcinoma progression in epithelial-mesenchymal transition, metastasis, and mortality

    doi: 10.21873/anticanres.16733

    Figure Lengend Snippet: Immunohistochemistry

    Article Snippet: ACVR1B (MAB222) , Monoclonal , R & D Systems , 1:200.

    Techniques: