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fst  (R&D Systems)


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    Structured Review

    R&D Systems fst
    <t>FST</t> overexpression decreased lipid accumulation in FFA-treated LO2 cells. ( A and B ) The efficiency of FST overexpression in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil red O staining and analysis result of control cells (EGFP) and FST-overexpressing LO2 cells treated with 1.0 mM FFA for 24 h (400×, scale bar=50 µm). ( E – G ) The protein levels and analysis results of ACC1, FASN, SREBP1, <t>ChREBP,</t> <t>Akt,</t> Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control cells and FST-overexpressing LO2 cells treated with 1 mM FFA for 24h. β-actin was used as a loading control.
    Fst, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fst/product/R&D Systems
    Average 93 stars, based on 46 article reviews
    fst - by Bioz Stars, 2026-02
    93/100 stars

    Images

    1) Product Images from "Follistatin Alleviates Hepatic Steatosis in NAFLD via the mTOR Dependent Pathway"

    Article Title: Follistatin Alleviates Hepatic Steatosis in NAFLD via the mTOR Dependent Pathway

    Journal: Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy

    doi: 10.2147/DMSO.S380053

    FST overexpression decreased lipid accumulation in FFA-treated LO2 cells. ( A and B ) The efficiency of FST overexpression in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil red O staining and analysis result of control cells (EGFP) and FST-overexpressing LO2 cells treated with 1.0 mM FFA for 24 h (400×, scale bar=50 µm). ( E – G ) The protein levels and analysis results of ACC1, FASN, SREBP1, ChREBP, Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control cells and FST-overexpressing LO2 cells treated with 1 mM FFA for 24h. β-actin was used as a loading control.
    Figure Legend Snippet: FST overexpression decreased lipid accumulation in FFA-treated LO2 cells. ( A and B ) The efficiency of FST overexpression in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil red O staining and analysis result of control cells (EGFP) and FST-overexpressing LO2 cells treated with 1.0 mM FFA for 24 h (400×, scale bar=50 µm). ( E – G ) The protein levels and analysis results of ACC1, FASN, SREBP1, ChREBP, Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control cells and FST-overexpressing LO2 cells treated with 1 mM FFA for 24h. β-actin was used as a loading control.

    Techniques Used: Over Expression, Quantitative RT-PCR, Western Blot, Staining

    FST knockdown aggravated lipid accumulation in LO2 cells and this effect was inhibited by rapamycin. ( A and B ) The efficiency of FST knockdown in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil Red O staining and analysis results of FFA-treated negative control shRNA (NCsh) cells, FFA-treated FST-knockdown (FSTsh) cells, and FFA- and rapamycin-treated FSTsh (FSTsh+RAPA) cells (400×, scale bar: 50 µm). ( E and F ) The protein levels and analysis results of Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in FFA-treated NCsh cells and FFA-treated FSTsh cells. ( G and H ) The protein levels and analysis results of ACC1, FASN, SREBP1, ChREBP, and mTOR in NCsh, FSTsh, FSTsh+RAPA cells. β-actin was used as a loading control.
    Figure Legend Snippet: FST knockdown aggravated lipid accumulation in LO2 cells and this effect was inhibited by rapamycin. ( A and B ) The efficiency of FST knockdown in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil Red O staining and analysis results of FFA-treated negative control shRNA (NCsh) cells, FFA-treated FST-knockdown (FSTsh) cells, and FFA- and rapamycin-treated FSTsh (FSTsh+RAPA) cells (400×, scale bar: 50 µm). ( E and F ) The protein levels and analysis results of Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in FFA-treated NCsh cells and FFA-treated FSTsh cells. ( G and H ) The protein levels and analysis results of ACC1, FASN, SREBP1, ChREBP, and mTOR in NCsh, FSTsh, FSTsh+RAPA cells. β-actin was used as a loading control.

    Techniques Used: Quantitative RT-PCR, Western Blot, Staining, Negative Control, shRNA

    FST overexpression inhibited lipid synthesis and Akt/mTOR pathway in HFD mice. ( A and B ) The protein expression and analysis results of ACC1, FASN, SREBP1, ChREBP, Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control (treated with an AAV vector encoding GFP) and FST-overexpressing (treated with an AAV vector encoding FST288 and FST315) HFD mice. β-actin was used as a loading control. ( C and D ) GTT and ITT results in the control and FST-overexpressing HFD mice. ( E and F ) AUC for GTT and ITT. ( G ) Immunohistochemical staining of hepatic FST in the control and FST-overexpressing HFD mice (400×, scale bar: 50 µm).
    Figure Legend Snippet: FST overexpression inhibited lipid synthesis and Akt/mTOR pathway in HFD mice. ( A and B ) The protein expression and analysis results of ACC1, FASN, SREBP1, ChREBP, Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control (treated with an AAV vector encoding GFP) and FST-overexpressing (treated with an AAV vector encoding FST288 and FST315) HFD mice. β-actin was used as a loading control. ( C and D ) GTT and ITT results in the control and FST-overexpressing HFD mice. ( E and F ) AUC for GTT and ITT. ( G ) Immunohistochemical staining of hepatic FST in the control and FST-overexpressing HFD mice (400×, scale bar: 50 µm).

    Techniques Used: Over Expression, Expressing, Plasmid Preparation, Immunohistochemical staining, Staining



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    EGF signaling drives <t>FST</t> expression via ERK signaling in HNSCC. ( A ) Western blots showing the effects of 4-h stimulation of SCC25 (left) and A253 (right) cells with 50ng of indicated growth factors. Although the downstream signaling cascades of these growth factors were activated in both cell lines, only EGF treatment upregulated FST expression. ( B ) Treatment of A253 and SCC25 cells with 30 ng EGF for 4 h resulted in activation of ERK1/2 but not AKT or STAT3. ( C ) Depletion <t>of</t> <t>p63</t> prevented EGF-mediated FST expression in A253 and SCC25 cells. ( D ) Inhibition of ERK phosphorylation via Selumetinib (ADZ6244) reduced basal levels of FST expression. ( E ) Inhibition of ERK activation by ADZ6244 blocks the EGF-mediated increase in FST expression in both A253 and SCC25 cells.
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    EGF signaling drives <t>FST</t> expression via ERK signaling in HNSCC. ( A ) Western blots showing the effects of 4-h stimulation of SCC25 (left) and A253 (right) cells with 50ng of indicated growth factors. Although the downstream signaling cascades of these growth factors were activated in both cell lines, only EGF treatment upregulated FST expression. ( B ) Treatment of A253 and SCC25 cells with 30 ng EGF for 4 h resulted in activation of ERK1/2 but not AKT or STAT3. ( C ) Depletion <t>of</t> <t>p63</t> prevented EGF-mediated FST expression in A253 and SCC25 cells. ( D ) Inhibition of ERK phosphorylation via Selumetinib (ADZ6244) reduced basal levels of FST expression. ( E ) Inhibition of ERK activation by ADZ6244 blocks the EGF-mediated increase in FST expression in both A253 and SCC25 cells.
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    EGF signaling drives <t>FST</t> expression via ERK signaling in HNSCC. ( A ) Western blots showing the effects of 4-h stimulation of SCC25 (left) and A253 (right) cells with 50ng of indicated growth factors. Although the downstream signaling cascades of these growth factors were activated in both cell lines, only EGF treatment upregulated FST expression. ( B ) Treatment of A253 and SCC25 cells with 30 ng EGF for 4 h resulted in activation of ERK1/2 but not AKT or STAT3. ( C ) Depletion <t>of</t> <t>p63</t> prevented EGF-mediated FST expression in A253 and SCC25 cells. ( D ) Inhibition of ERK phosphorylation via Selumetinib (ADZ6244) reduced basal levels of FST expression. ( E ) Inhibition of ERK activation by ADZ6244 blocks the EGF-mediated increase in FST expression in both A253 and SCC25 cells.
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    <t>FST</t> overexpression decreased lipid accumulation in FFA-treated LO2 cells. ( A and B ) The efficiency of FST overexpression in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil red O staining and analysis result of control cells (EGFP) and FST-overexpressing LO2 cells treated with 1.0 mM FFA for 24 h (400×, scale bar=50 µm). ( E – G ) The protein levels and analysis results of ACC1, FASN, SREBP1, <t>ChREBP,</t> <t>Akt,</t> Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control cells and FST-overexpressing LO2 cells treated with 1 mM FFA for 24h. β-actin was used as a loading control.
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    <t>FST</t> overexpression decreased lipid accumulation in FFA-treated LO2 cells. ( A and B ) The efficiency of FST overexpression in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil red O staining and analysis result of control cells (EGFP) and FST-overexpressing LO2 cells treated with 1.0 mM FFA for 24 h (400×, scale bar=50 µm). ( E – G ) The protein levels and analysis results of ACC1, FASN, SREBP1, <t>ChREBP,</t> <t>Akt,</t> Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control cells and FST-overexpressing LO2 cells treated with 1 mM FFA for 24h. β-actin was used as a loading control.
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    Image Search Results


    EGF signaling drives FST expression via ERK signaling in HNSCC. ( A ) Western blots showing the effects of 4-h stimulation of SCC25 (left) and A253 (right) cells with 50ng of indicated growth factors. Although the downstream signaling cascades of these growth factors were activated in both cell lines, only EGF treatment upregulated FST expression. ( B ) Treatment of A253 and SCC25 cells with 30 ng EGF for 4 h resulted in activation of ERK1/2 but not AKT or STAT3. ( C ) Depletion of p63 prevented EGF-mediated FST expression in A253 and SCC25 cells. ( D ) Inhibition of ERK phosphorylation via Selumetinib (ADZ6244) reduced basal levels of FST expression. ( E ) Inhibition of ERK activation by ADZ6244 blocks the EGF-mediated increase in FST expression in both A253 and SCC25 cells.

    Journal: NAR Cancer

    Article Title: An integrated genomic approach identifies follistatin as a target of the p63-epidermal growth factor receptor oncogenic network in head and neck squamous cell carcinoma

    doi: 10.1093/narcan/zcad038

    Figure Lengend Snippet: EGF signaling drives FST expression via ERK signaling in HNSCC. ( A ) Western blots showing the effects of 4-h stimulation of SCC25 (left) and A253 (right) cells with 50ng of indicated growth factors. Although the downstream signaling cascades of these growth factors were activated in both cell lines, only EGF treatment upregulated FST expression. ( B ) Treatment of A253 and SCC25 cells with 30 ng EGF for 4 h resulted in activation of ERK1/2 but not AKT or STAT3. ( C ) Depletion of p63 prevented EGF-mediated FST expression in A253 and SCC25 cells. ( D ) Inhibition of ERK phosphorylation via Selumetinib (ADZ6244) reduced basal levels of FST expression. ( E ) Inhibition of ERK activation by ADZ6244 blocks the EGF-mediated increase in FST expression in both A253 and SCC25 cells.

    Article Snippet: Proteins were then electro-transferred to Immunoblot polyvinylidene difluoride membranes (Bio-Rad), which were incubated with the following antibodies: p63 4A4, FST (sc-365003 [Santa Cruz Biotechnology] or EPR10903 [Abcam]), pAKT ser-473 (66444-I-Ig; Proteintech), pAKT Thr-308 (29163-1-AP; Proteintech), pSTAT3 (Epitomics), STAT3 (2281-1; Epitomics), AKT1 (10176-2-AP; Proteintech), pERK1/2 (sc-7883; Santa Cruz Biotechnology), ERK1/2 (sc-66192-1-Ig [Proteintech] or sc-514302 [Santa Cruz Biotechnology]), GAPDH (MAB374; EMD Millipore), pSMAD2 (GTX13364; GeneTex), SMAD2 (GTX111075; GeneTex), pSMAD1/5 (41D10; Cell Signaling), and SMAD1 (D49D7; Cell Signaling).

    Techniques: Expressing, Western Blot, Activation Assay, Inhibition, Phospho-proteomics

    Epithelial cells are the primary producers of FST in the tumor microenvironment. ( A ) UMAP plot showing the identities of the various cellular clusters identified in the HNSCC single-cell RNA-seq data reported by Puram et al. . ( B ) Expression of FST by cells in the different clusters showing predominantly epithelial cell-specific expression. ( C ) UMAP plot showing that expression of TP63 is predominantly in epithelial cells. ( D ) EGFR expression in the different cellular clusters.

    Journal: NAR Cancer

    Article Title: An integrated genomic approach identifies follistatin as a target of the p63-epidermal growth factor receptor oncogenic network in head and neck squamous cell carcinoma

    doi: 10.1093/narcan/zcad038

    Figure Lengend Snippet: Epithelial cells are the primary producers of FST in the tumor microenvironment. ( A ) UMAP plot showing the identities of the various cellular clusters identified in the HNSCC single-cell RNA-seq data reported by Puram et al. . ( B ) Expression of FST by cells in the different clusters showing predominantly epithelial cell-specific expression. ( C ) UMAP plot showing that expression of TP63 is predominantly in epithelial cells. ( D ) EGFR expression in the different cellular clusters.

    Article Snippet: Proteins were then electro-transferred to Immunoblot polyvinylidene difluoride membranes (Bio-Rad), which were incubated with the following antibodies: p63 4A4, FST (sc-365003 [Santa Cruz Biotechnology] or EPR10903 [Abcam]), pAKT ser-473 (66444-I-Ig; Proteintech), pAKT Thr-308 (29163-1-AP; Proteintech), pSTAT3 (Epitomics), STAT3 (2281-1; Epitomics), AKT1 (10176-2-AP; Proteintech), pERK1/2 (sc-7883; Santa Cruz Biotechnology), ERK1/2 (sc-66192-1-Ig [Proteintech] or sc-514302 [Santa Cruz Biotechnology]), GAPDH (MAB374; EMD Millipore), pSMAD2 (GTX13364; GeneTex), SMAD2 (GTX111075; GeneTex), pSMAD1/5 (41D10; Cell Signaling), and SMAD1 (D49D7; Cell Signaling).

    Techniques: RNA Sequencing, Expressing

    FST , EGFR and TP63 expression correlates with immune cell infiltration. FST , EGFR and TP63 expression correlated negatively with tumor suppressive T-lymphocyte infiltration ( A ) and positively with tumor-promoting myeloid suppressor cells ( B ) in HNSCC tissues. ( C ) Kaplan–Meier plot showing overall survival of cohorts of patients with high and low FST expression levels.

    Journal: NAR Cancer

    Article Title: An integrated genomic approach identifies follistatin as a target of the p63-epidermal growth factor receptor oncogenic network in head and neck squamous cell carcinoma

    doi: 10.1093/narcan/zcad038

    Figure Lengend Snippet: FST , EGFR and TP63 expression correlates with immune cell infiltration. FST , EGFR and TP63 expression correlated negatively with tumor suppressive T-lymphocyte infiltration ( A ) and positively with tumor-promoting myeloid suppressor cells ( B ) in HNSCC tissues. ( C ) Kaplan–Meier plot showing overall survival of cohorts of patients with high and low FST expression levels.

    Article Snippet: Proteins were then electro-transferred to Immunoblot polyvinylidene difluoride membranes (Bio-Rad), which were incubated with the following antibodies: p63 4A4, FST (sc-365003 [Santa Cruz Biotechnology] or EPR10903 [Abcam]), pAKT ser-473 (66444-I-Ig; Proteintech), pAKT Thr-308 (29163-1-AP; Proteintech), pSTAT3 (Epitomics), STAT3 (2281-1; Epitomics), AKT1 (10176-2-AP; Proteintech), pERK1/2 (sc-7883; Santa Cruz Biotechnology), ERK1/2 (sc-66192-1-Ig [Proteintech] or sc-514302 [Santa Cruz Biotechnology]), GAPDH (MAB374; EMD Millipore), pSMAD2 (GTX13364; GeneTex), SMAD2 (GTX111075; GeneTex), pSMAD1/5 (41D10; Cell Signaling), and SMAD1 (D49D7; Cell Signaling).

    Techniques: Expressing

    FST overexpression decreased lipid accumulation in FFA-treated LO2 cells. ( A and B ) The efficiency of FST overexpression in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil red O staining and analysis result of control cells (EGFP) and FST-overexpressing LO2 cells treated with 1.0 mM FFA for 24 h (400×, scale bar=50 µm). ( E – G ) The protein levels and analysis results of ACC1, FASN, SREBP1, ChREBP, Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control cells and FST-overexpressing LO2 cells treated with 1 mM FFA for 24h. β-actin was used as a loading control.

    Journal: Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy

    Article Title: Follistatin Alleviates Hepatic Steatosis in NAFLD via the mTOR Dependent Pathway

    doi: 10.2147/DMSO.S380053

    Figure Lengend Snippet: FST overexpression decreased lipid accumulation in FFA-treated LO2 cells. ( A and B ) The efficiency of FST overexpression in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil red O staining and analysis result of control cells (EGFP) and FST-overexpressing LO2 cells treated with 1.0 mM FFA for 24 h (400×, scale bar=50 µm). ( E – G ) The protein levels and analysis results of ACC1, FASN, SREBP1, ChREBP, Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control cells and FST-overexpressing LO2 cells treated with 1 mM FFA for 24h. β-actin was used as a loading control.

    Article Snippet: The primary antibodies were β-actin (#AC026) and ChREBP (#A7360) from Abclonal Technology; SREBP1 (#ab28481) from Abcam Technology; mTOR (#T55306) and p-mTOR (#T55996) from Abmart Technology; ACC1 (#4190), FASN (#3180), Akt-Thr308 (#13038), Akt-Ser473 (#4060), and Akt (#9272) from Cell Signaling Technology; and FST (#AF669) from R&D Technology.

    Techniques: Over Expression, Quantitative RT-PCR, Western Blot, Staining

    FST knockdown aggravated lipid accumulation in LO2 cells and this effect was inhibited by rapamycin. ( A and B ) The efficiency of FST knockdown in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil Red O staining and analysis results of FFA-treated negative control shRNA (NCsh) cells, FFA-treated FST-knockdown (FSTsh) cells, and FFA- and rapamycin-treated FSTsh (FSTsh+RAPA) cells (400×, scale bar: 50 µm). ( E and F ) The protein levels and analysis results of Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in FFA-treated NCsh cells and FFA-treated FSTsh cells. ( G and H ) The protein levels and analysis results of ACC1, FASN, SREBP1, ChREBP, and mTOR in NCsh, FSTsh, FSTsh+RAPA cells. β-actin was used as a loading control.

    Journal: Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy

    Article Title: Follistatin Alleviates Hepatic Steatosis in NAFLD via the mTOR Dependent Pathway

    doi: 10.2147/DMSO.S380053

    Figure Lengend Snippet: FST knockdown aggravated lipid accumulation in LO2 cells and this effect was inhibited by rapamycin. ( A and B ) The efficiency of FST knockdown in LO2 cells was demonstrated by RT-qPCR and Western blotting. ( C and D ) Oil Red O staining and analysis results of FFA-treated negative control shRNA (NCsh) cells, FFA-treated FST-knockdown (FSTsh) cells, and FFA- and rapamycin-treated FSTsh (FSTsh+RAPA) cells (400×, scale bar: 50 µm). ( E and F ) The protein levels and analysis results of Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in FFA-treated NCsh cells and FFA-treated FSTsh cells. ( G and H ) The protein levels and analysis results of ACC1, FASN, SREBP1, ChREBP, and mTOR in NCsh, FSTsh, FSTsh+RAPA cells. β-actin was used as a loading control.

    Article Snippet: The primary antibodies were β-actin (#AC026) and ChREBP (#A7360) from Abclonal Technology; SREBP1 (#ab28481) from Abcam Technology; mTOR (#T55306) and p-mTOR (#T55996) from Abmart Technology; ACC1 (#4190), FASN (#3180), Akt-Thr308 (#13038), Akt-Ser473 (#4060), and Akt (#9272) from Cell Signaling Technology; and FST (#AF669) from R&D Technology.

    Techniques: Quantitative RT-PCR, Western Blot, Staining, Negative Control, shRNA

    FST overexpression inhibited lipid synthesis and Akt/mTOR pathway in HFD mice. ( A and B ) The protein expression and analysis results of ACC1, FASN, SREBP1, ChREBP, Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control (treated with an AAV vector encoding GFP) and FST-overexpressing (treated with an AAV vector encoding FST288 and FST315) HFD mice. β-actin was used as a loading control. ( C and D ) GTT and ITT results in the control and FST-overexpressing HFD mice. ( E and F ) AUC for GTT and ITT. ( G ) Immunohistochemical staining of hepatic FST in the control and FST-overexpressing HFD mice (400×, scale bar: 50 µm).

    Journal: Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy

    Article Title: Follistatin Alleviates Hepatic Steatosis in NAFLD via the mTOR Dependent Pathway

    doi: 10.2147/DMSO.S380053

    Figure Lengend Snippet: FST overexpression inhibited lipid synthesis and Akt/mTOR pathway in HFD mice. ( A and B ) The protein expression and analysis results of ACC1, FASN, SREBP1, ChREBP, Akt, Akt-Thr308, Akt-Ser473, p-mTOR, and mTOR in the control (treated with an AAV vector encoding GFP) and FST-overexpressing (treated with an AAV vector encoding FST288 and FST315) HFD mice. β-actin was used as a loading control. ( C and D ) GTT and ITT results in the control and FST-overexpressing HFD mice. ( E and F ) AUC for GTT and ITT. ( G ) Immunohistochemical staining of hepatic FST in the control and FST-overexpressing HFD mice (400×, scale bar: 50 µm).

    Article Snippet: The primary antibodies were β-actin (#AC026) and ChREBP (#A7360) from Abclonal Technology; SREBP1 (#ab28481) from Abcam Technology; mTOR (#T55306) and p-mTOR (#T55996) from Abmart Technology; ACC1 (#4190), FASN (#3180), Akt-Thr308 (#13038), Akt-Ser473 (#4060), and Akt (#9272) from Cell Signaling Technology; and FST (#AF669) from R&D Technology.

    Techniques: Over Expression, Expressing, Plasmid Preparation, Immunohistochemical staining, Staining