sirna duplexes  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc sirna duplexes
    Sirna Duplexes, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    sirna duplexes  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc sirna duplexes
    Sirna Duplexes, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    signal silence ts sirna  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc signal silence ts sirna
    (A) The mRNA levels of TS in 53BP1 transfected MDA-MB-231 and MCF-7 cells. (B) The mRNA levels <t>of</t> <t>DPYD</t> in 53BP1 transfected cells. (C) The protein levels of TS and DPYD in 53BP1 transfected cells. (D) The transfection efficiency of <t>siRNA</t> TS was confirmed by western blot analysis. (E) The transfection efficiency of siRNA DPYD was confirmed by western blot analysis. Results are shown for one of the three independent experiments performed. **p<0.01, ***p<0.001.
    Signal Silence Ts Sirna, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "53BP1 Sensitizes Breast Cancer Cells to 5-Fluorouracil"

    Article Title: 53BP1 Sensitizes Breast Cancer Cells to 5-Fluorouracil

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0074928

    (A) The mRNA levels of TS in 53BP1 transfected MDA-MB-231 and MCF-7 cells. (B) The mRNA levels of DPYD in 53BP1 transfected cells. (C) The protein levels of TS and DPYD in 53BP1 transfected cells. (D) The transfection efficiency of siRNA TS was confirmed by western blot analysis. (E) The transfection efficiency of siRNA DPYD was confirmed by western blot analysis. Results are shown for one of the three independent experiments performed. **p<0.01, ***p<0.001.
    Figure Legend Snippet: (A) The mRNA levels of TS in 53BP1 transfected MDA-MB-231 and MCF-7 cells. (B) The mRNA levels of DPYD in 53BP1 transfected cells. (C) The protein levels of TS and DPYD in 53BP1 transfected cells. (D) The transfection efficiency of siRNA TS was confirmed by western blot analysis. (E) The transfection efficiency of siRNA DPYD was confirmed by western blot analysis. Results are shown for one of the three independent experiments performed. **p<0.01, ***p<0.001.

    Techniques Used: Transfection, Western Blot

    signal silence c myc sirna  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc signal silence c myc sirna
    Signal Silence C Myc Sirna, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    signal silence sirna  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc signal silence sirna
    Signal Silence Sirna, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    cofilin sirna i  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cofilin sirna i
    a Left: Representative F-actin images in control and <t>cofilin-depleted</t> hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Zoomed regions display details of F-actin organization in the apical region of the nucleus. Right: Corresponding quantification of the percentages of hMSCs having an actin cap ( n = 3 experiments per group). b Left: Representative YAP images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Right: Corresponding quantification of YAP nuc/cyto ratios (from left to right n = 62, 58, 68, 72, 65, 68 cells). c Top: Representative pCofilin images in hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Bottom: Corresponding quantification of pCofilin level based on the immunostaining (from left to right n = 107, 136, 118 cells). Data are presented as mean ± s.e.m., and p values were obtained using one-way ANOVA followed by Tukey’s post hoc test ( a – c ). Scale bars: 30 µm ( a – c ). Source data are provided as a Source Data file.
    Cofilin Sirna I, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Programmable integrin and N-cadherin adhesive interactions modulate mechanosensing of mesenchymal stem cells by cofilin phosphorylation"

    Article Title: Programmable integrin and N-cadherin adhesive interactions modulate mechanosensing of mesenchymal stem cells by cofilin phosphorylation

    Journal: Nature Communications

    doi: 10.1038/s41467-022-34424-0

    a Left: Representative F-actin images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Zoomed regions display details of F-actin organization in the apical region of the nucleus. Right: Corresponding quantification of the percentages of hMSCs having an actin cap ( n = 3 experiments per group). b Left: Representative YAP images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Right: Corresponding quantification of YAP nuc/cyto ratios (from left to right n = 62, 58, 68, 72, 65, 68 cells). c Top: Representative pCofilin images in hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Bottom: Corresponding quantification of pCofilin level based on the immunostaining (from left to right n = 107, 136, 118 cells). Data are presented as mean ± s.e.m., and p values were obtained using one-way ANOVA followed by Tukey’s post hoc test ( a – c ). Scale bars: 30 µm ( a – c ). Source data are provided as a Source Data file.
    Figure Legend Snippet: a Left: Representative F-actin images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Zoomed regions display details of F-actin organization in the apical region of the nucleus. Right: Corresponding quantification of the percentages of hMSCs having an actin cap ( n = 3 experiments per group). b Left: Representative YAP images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Right: Corresponding quantification of YAP nuc/cyto ratios (from left to right n = 62, 58, 68, 72, 65, 68 cells). c Top: Representative pCofilin images in hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Bottom: Corresponding quantification of pCofilin level based on the immunostaining (from left to right n = 107, 136, 118 cells). Data are presented as mean ± s.e.m., and p values were obtained using one-way ANOVA followed by Tukey’s post hoc test ( a – c ). Scale bars: 30 µm ( a – c ). Source data are provided as a Source Data file.

    Techniques Used: Immunostaining

    signalsilence cofilin sirna i  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc signalsilence cofilin sirna i
    Increased <t>cofilin-1</t> expression alters actin dynamics in Emery-Dreifuss muscular dystrophy (EDMD) (A) Schematic representation of actin dynamics mechanisms. (B) Immunoblots showing pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. GAPDH is shown as loading control. (C) Quantification of pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein expression level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. ∗∗ p ≤ 0.001 between old WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD. (D) Immunoblots showing cofilin-1protein level in skeletal muscle from EDMD patient carrying LMNA mutation. GAPDH is shown as loading control. Data are represented as mean ± SD. (E) Immunoblot showing G-actin and F-actin protein levels in soleus from old WT (n = 3) and Lmna p.H222P/H222P (H222P) (n = 3) mice.
    Signalsilence Cofilin Sirna I, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies"

    Article Title: The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies

    Journal: Cell Reports

    doi: 10.1016/j.celrep.2021.109601

    Increased cofilin-1 expression alters actin dynamics in Emery-Dreifuss muscular dystrophy (EDMD) (A) Schematic representation of actin dynamics mechanisms. (B) Immunoblots showing pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. GAPDH is shown as loading control. (C) Quantification of pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein expression level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. ∗∗ p ≤ 0.001 between old WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD. (D) Immunoblots showing cofilin-1protein level in skeletal muscle from EDMD patient carrying LMNA mutation. GAPDH is shown as loading control. Data are represented as mean ± SD. (E) Immunoblot showing G-actin and F-actin protein levels in soleus from old WT (n = 3) and Lmna p.H222P/H222P (H222P) (n = 3) mice.
    Figure Legend Snippet: Increased cofilin-1 expression alters actin dynamics in Emery-Dreifuss muscular dystrophy (EDMD) (A) Schematic representation of actin dynamics mechanisms. (B) Immunoblots showing pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. GAPDH is shown as loading control. (C) Quantification of pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein expression level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. ∗∗ p ≤ 0.001 between old WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD. (D) Immunoblots showing cofilin-1protein level in skeletal muscle from EDMD patient carrying LMNA mutation. GAPDH is shown as loading control. Data are represented as mean ± SD. (E) Immunoblot showing G-actin and F-actin protein levels in soleus from old WT (n = 3) and Lmna p.H222P/H222P (H222P) (n = 3) mice.

    Techniques Used: Expressing, Western Blot, Mutagenesis

    Increased cofilin-1 expression is under the control of ERK1/2 signaling (A) Representative immunoblots and quantification of cofilin-1, N-WASP, ARP2, and profilin-1 protein expression in C2C12 cells stably expressing WT (C2-WT) (n = 3) or p.H222P (C2-H222P) (n = 3) lamin A. GAPDH is shown as loading control. C2-H222P cells were either untreated or treated with selumetinib. ∗∗ p ≤ 0.001 between C2-WT and C2-H222P ± selumetinib. Data are represented as mean ± SD. (B) Representative immunoblot and quantification of effects of washout of selumetinib on cofilin-1, N-WASP, ARP2 and profilin-1 protein expression level in C2-H222P cells. Data are represented as mean ± SD. (C) Representative immunoblot showing effects of transfection with ERK2 and MEK1 constructs on cofilin-1 protein expression in C2-WT and C2-H222P cells. GAPDH is shown as loading control. (D) Cycloheximide chase experiment using C2C12 cells stably expressing WT (C2-WT) or p.H222P (C2-H222P) lamin A, treated or not with selumetinib. Cells were treated with 50 μM cycloheximide and lysed at the indicated times for western blot analysis using anti-cofilin-1 antibody. GAPDH was used as a loading control. (E) Quantification of cofilin-1 signal intensity normalized to GAPDH content and expressed as the percent change from time zero, which was set at 100%. Data are represented as mean ± SD. (F) Representative immunoblots showing effects of transfection with different mutated lamin A constructs on cofilin-1 expression in C2C12 cells. (G) Representative immunoblot showing the effect of cofilin-1 siRNA on cofilin-1 expression. GAPDH is shown as a loading control. (H) Representative immunoblot showing the effect of cofilin-1 siRNA on G-actin and F-actin expression in C2-H222P cells. Cytochalasin D (cytoD) induces actin depolymerization.
    Figure Legend Snippet: Increased cofilin-1 expression is under the control of ERK1/2 signaling (A) Representative immunoblots and quantification of cofilin-1, N-WASP, ARP2, and profilin-1 protein expression in C2C12 cells stably expressing WT (C2-WT) (n = 3) or p.H222P (C2-H222P) (n = 3) lamin A. GAPDH is shown as loading control. C2-H222P cells were either untreated or treated with selumetinib. ∗∗ p ≤ 0.001 between C2-WT and C2-H222P ± selumetinib. Data are represented as mean ± SD. (B) Representative immunoblot and quantification of effects of washout of selumetinib on cofilin-1, N-WASP, ARP2 and profilin-1 protein expression level in C2-H222P cells. Data are represented as mean ± SD. (C) Representative immunoblot showing effects of transfection with ERK2 and MEK1 constructs on cofilin-1 protein expression in C2-WT and C2-H222P cells. GAPDH is shown as loading control. (D) Cycloheximide chase experiment using C2C12 cells stably expressing WT (C2-WT) or p.H222P (C2-H222P) lamin A, treated or not with selumetinib. Cells were treated with 50 μM cycloheximide and lysed at the indicated times for western blot analysis using anti-cofilin-1 antibody. GAPDH was used as a loading control. (E) Quantification of cofilin-1 signal intensity normalized to GAPDH content and expressed as the percent change from time zero, which was set at 100%. Data are represented as mean ± SD. (F) Representative immunoblots showing effects of transfection with different mutated lamin A constructs on cofilin-1 expression in C2C12 cells. (G) Representative immunoblot showing the effect of cofilin-1 siRNA on cofilin-1 expression. GAPDH is shown as a loading control. (H) Representative immunoblot showing the effect of cofilin-1 siRNA on G-actin and F-actin expression in C2-H222P cells. Cytochalasin D (cytoD) induces actin depolymerization.

    Techniques Used: Expressing, Western Blot, Stable Transfection, Transfection, Construct

    pERK1/2 protects cofilin-1 from degradation by the ubiquitin-proteasome pathway (A) Immunoblot showing effect of treatment with proteasome inhibitor MG132 on cofilin-1 expression in C2-H222P cells untreated or treated with selumetinib. GAPDH is shown as loading control. (B) Immunoblot showing effect of treatment with proteasome inhibitor MG132 treatment on cofilin-1 expression in C2-WT cells. GAPDH is shown as loading control. (C) Immunoprecipitation of cofilin-1 showing ubiquitination levels in C2-WT and C2-H222P cells untreated or treated with selumetinib. Input is shown as loading control. (D) Proteasome activity in C2-WT and C2-H222P cells untreated or treated with selumetinib. Data are represented as mean ± SD. (E) Immunoblot showing effect of selumetinib and MG132 on ectopically expressed mCherry-tagged cofilin-1, cofilin-1(T25A), and cofilin-1(T25D) in C2-WT cells. GAPDH is shown as loading control. (F) Quantification of mCherry signal intensity normalized to GAPDH content in C2-WT cells treated with the different conditions (n = 3). Data are represented as mean ± SD.
    Figure Legend Snippet: pERK1/2 protects cofilin-1 from degradation by the ubiquitin-proteasome pathway (A) Immunoblot showing effect of treatment with proteasome inhibitor MG132 on cofilin-1 expression in C2-H222P cells untreated or treated with selumetinib. GAPDH is shown as loading control. (B) Immunoblot showing effect of treatment with proteasome inhibitor MG132 treatment on cofilin-1 expression in C2-WT cells. GAPDH is shown as loading control. (C) Immunoprecipitation of cofilin-1 showing ubiquitination levels in C2-WT and C2-H222P cells untreated or treated with selumetinib. Input is shown as loading control. (D) Proteasome activity in C2-WT and C2-H222P cells untreated or treated with selumetinib. Data are represented as mean ± SD. (E) Immunoblot showing effect of selumetinib and MG132 on ectopically expressed mCherry-tagged cofilin-1, cofilin-1(T25A), and cofilin-1(T25D) in C2-WT cells. GAPDH is shown as loading control. (F) Quantification of mCherry signal intensity normalized to GAPDH content in C2-WT cells treated with the different conditions (n = 3). Data are represented as mean ± SD.

    Techniques Used: Western Blot, Expressing, Immunoprecipitation, Activity Assay

    Alteration of sarcomere organization in EDMD (A) Left: immunofluorescence micrographs of sarcomeric α-actinin (green) and sarcomeric α-actin (red) labeled soleus muscle from old, WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 5 μm. Right: immunofluorescence micrographs of titin (green) and sarcomeric α-actinin (red) labeled soleus muscle from old, WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 8 μm. (B) Electron microscopy showing sarcomeric disorganization in soleus muscles from old WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 2 μm. (C) Left: electron microscopy showing sarcomeric disorganization in striated muscles from EDMD patients carrying LMNA mutations. Right: striated muscle from human control. Scale bar, 10 μm (D) Growth rate of single cofilin domains for eGFP-cofilin-1 WT and T25D, observed on individual actin filaments in vitro , in the presence of 200 nM cofilin-1 (n = 10 filaments for each condition). The distributions are plotted as violin plots, with the white dot representing its median. The statistical test was a t test for the means of two independent samples with unequal variance. (E) Single eGFP-cofilin-1 WT or T25D domain severing rate. Time t = 0 is defined for every domain as the frame on which they nucleate. n = 152 and 202 cofilin domains for eGFP-cofilin-1 WT and T25D, respectively.
    Figure Legend Snippet: Alteration of sarcomere organization in EDMD (A) Left: immunofluorescence micrographs of sarcomeric α-actinin (green) and sarcomeric α-actin (red) labeled soleus muscle from old, WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 5 μm. Right: immunofluorescence micrographs of titin (green) and sarcomeric α-actinin (red) labeled soleus muscle from old, WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 8 μm. (B) Electron microscopy showing sarcomeric disorganization in soleus muscles from old WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 2 μm. (C) Left: electron microscopy showing sarcomeric disorganization in striated muscles from EDMD patients carrying LMNA mutations. Right: striated muscle from human control. Scale bar, 10 μm (D) Growth rate of single cofilin domains for eGFP-cofilin-1 WT and T25D, observed on individual actin filaments in vitro , in the presence of 200 nM cofilin-1 (n = 10 filaments for each condition). The distributions are plotted as violin plots, with the white dot representing its median. The statistical test was a t test for the means of two independent samples with unequal variance. (E) Single eGFP-cofilin-1 WT or T25D domain severing rate. Time t = 0 is defined for every domain as the frame on which they nucleate. n = 152 and 202 cofilin domains for eGFP-cofilin-1 WT and T25D, respectively.

    Techniques Used: Immunofluorescence, Labeling, Electron Microscopy, In Vitro

    Cofilin-1 is involved in the muscle force generation in vivo (A) Schematic representation of the experimental procedure followed for transduction with AAV vectors expressing cofilin-1 constructs of soleus muscles in young WT mice. (B) Representative immunoblot of cofilin-1 protein levels in soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. GAPDH is shown as loading control. (C) Representative immunoblot showing the effect of AAV expressing cofilin-1 construct on G-actin and F-actin expression in the soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. (D) Tetanic force of soleus from WT (n = 17), Lmna p.H222P/H222P (H222P) (n = 9) and WT mice injected with either PBS (n = 4) or AAV vectors expressing cofilin-1 (n = 7), cofilin-1(T25A) (n = 3) or cofilin-1(T25D) (n = 3). ∗ p ≤ 0.01 between WT and Lmna p.H222P/H222P (H222P), ∗∗ p ≤ 0.001 between WT and WT AAV vectors expressing cofilin-1, ∗∗∗ p ≤ 0.0001 between WT and WT AAV vectors expressing cofilin-1(T25D). Data are represented as mean ± SD. (E) Sirius Red staining of cross sections of soleus muscles from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. Section of soleus muscle from Lmna p.H222P/H222P (H222P) is shown as control. Scale bar, 50 μm. (F) Expression of fibrosis-related genes ( Col1a2 , Col3a1 , and Ctgf ) in the soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. Quantification of soleus muscle from Lmna p.H222P/H222P (H222P) is shown as control. ∗ p ≤ 0.01 between WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD.
    Figure Legend Snippet: Cofilin-1 is involved in the muscle force generation in vivo (A) Schematic representation of the experimental procedure followed for transduction with AAV vectors expressing cofilin-1 constructs of soleus muscles in young WT mice. (B) Representative immunoblot of cofilin-1 protein levels in soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. GAPDH is shown as loading control. (C) Representative immunoblot showing the effect of AAV expressing cofilin-1 construct on G-actin and F-actin expression in the soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. (D) Tetanic force of soleus from WT (n = 17), Lmna p.H222P/H222P (H222P) (n = 9) and WT mice injected with either PBS (n = 4) or AAV vectors expressing cofilin-1 (n = 7), cofilin-1(T25A) (n = 3) or cofilin-1(T25D) (n = 3). ∗ p ≤ 0.01 between WT and Lmna p.H222P/H222P (H222P), ∗∗ p ≤ 0.001 between WT and WT AAV vectors expressing cofilin-1, ∗∗∗ p ≤ 0.0001 between WT and WT AAV vectors expressing cofilin-1(T25D). Data are represented as mean ± SD. (E) Sirius Red staining of cross sections of soleus muscles from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. Section of soleus muscle from Lmna p.H222P/H222P (H222P) is shown as control. Scale bar, 50 μm. (F) Expression of fibrosis-related genes ( Col1a2 , Col3a1 , and Ctgf ) in the soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. Quantification of soleus muscle from Lmna p.H222P/H222P (H222P) is shown as control. ∗ p ≤ 0.01 between WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD.

    Techniques Used: In Vivo, Transduction, Expressing, Construct, Western Blot, Injection, Plasmid Preparation, Staining

    Schematic representation of the mechanism of pERK1/2-mediated protection of cofilin-1 from proteasome degradation and its consequences on sarcomeric actin depolymerization in striated muscle diseases caused by LMNA mutations
    Figure Legend Snippet: Schematic representation of the mechanism of pERK1/2-mediated protection of cofilin-1 from proteasome degradation and its consequences on sarcomeric actin depolymerization in striated muscle diseases caused by LMNA mutations

    Techniques Used:


    Figure Legend Snippet:

    Techniques Used: Mutagenesis, Recombinant, Activity Assay, In Vivo, SYBR Green Assay, Transfection, Plasmid Preparation, Software, Microarray

    cofilin 1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cofilin 1
    Cofilin 1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    signalsilences control sirna  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc signalsilences control sirna
    Signalsilences Control Sirna, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p cofilin ser3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p cofilin ser3
    LM11A-31 treatment modulates mechanisms regulating tau cleavage and phosphorylation. a – f Western blots of hippocampal extracts (representative examples shown) were quantitated by determining ratios of cleaved to non-cleaved fragments or actin, or ratios of phospho (p)-protein over total protein and normalized to the mean of Ntg-vehicle mice a ratio of ~ 145 kDa α-fodrin calpain cleavage fragments to actin. b Ratio of CDK5 regulatory subunit p25 (active, calpain cleavage product) to full length p35 inactive subunit. c p-JNK T183/Y185 to total JNK. d p-GSK3β S9 to total GSK3β, e p-ERK T202/Y204 to total ERK. f <t>p-cofilin</t> S3 to total cofilin. p-values for the indicated comparisons are shown and statistical significance was determined using an ANOVA with post hoc Sidak’s multiple comparisons test; n = 6–11 mice per group, with two or three independent western blots averaged per animal
    P Cofilin Ser3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Small-molecule modulation of the p75 neurotrophin receptor inhibits a wide range of tau molecular pathologies and their sequelae in P301S tauopathy mice"

    Article Title: Small-molecule modulation of the p75 neurotrophin receptor inhibits a wide range of tau molecular pathologies and their sequelae in P301S tauopathy mice

    Journal: Acta Neuropathologica Communications

    doi: 10.1186/s40478-020-01034-0

    LM11A-31 treatment modulates mechanisms regulating tau cleavage and phosphorylation. a – f Western blots of hippocampal extracts (representative examples shown) were quantitated by determining ratios of cleaved to non-cleaved fragments or actin, or ratios of phospho (p)-protein over total protein and normalized to the mean of Ntg-vehicle mice a ratio of ~ 145 kDa α-fodrin calpain cleavage fragments to actin. b Ratio of CDK5 regulatory subunit p25 (active, calpain cleavage product) to full length p35 inactive subunit. c p-JNK T183/Y185 to total JNK. d p-GSK3β S9 to total GSK3β, e p-ERK T202/Y204 to total ERK. f p-cofilin S3 to total cofilin. p-values for the indicated comparisons are shown and statistical significance was determined using an ANOVA with post hoc Sidak’s multiple comparisons test; n = 6–11 mice per group, with two or three independent western blots averaged per animal
    Figure Legend Snippet: LM11A-31 treatment modulates mechanisms regulating tau cleavage and phosphorylation. a – f Western blots of hippocampal extracts (representative examples shown) were quantitated by determining ratios of cleaved to non-cleaved fragments or actin, or ratios of phospho (p)-protein over total protein and normalized to the mean of Ntg-vehicle mice a ratio of ~ 145 kDa α-fodrin calpain cleavage fragments to actin. b Ratio of CDK5 regulatory subunit p25 (active, calpain cleavage product) to full length p35 inactive subunit. c p-JNK T183/Y185 to total JNK. d p-GSK3β S9 to total GSK3β, e p-ERK T202/Y204 to total ERK. f p-cofilin S3 to total cofilin. p-values for the indicated comparisons are shown and statistical significance was determined using an ANOVA with post hoc Sidak’s multiple comparisons test; n = 6–11 mice per group, with two or three independent western blots averaged per animal

    Techniques Used: Western Blot

    phospho cofilin  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc sirna duplexes
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    (A) The mRNA levels of TS in 53BP1 transfected MDA-MB-231 and MCF-7 cells. (B) The mRNA levels <t>of</t> <t>DPYD</t> in 53BP1 transfected cells. (C) The protein levels of TS and DPYD in 53BP1 transfected cells. (D) The transfection efficiency of <t>siRNA</t> TS was confirmed by western blot analysis. (E) The transfection efficiency of siRNA DPYD was confirmed by western blot analysis. Results are shown for one of the three independent experiments performed. **p<0.01, ***p<0.001.
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    (A) The mRNA levels of TS in 53BP1 transfected MDA-MB-231 and MCF-7 cells. (B) The mRNA levels <t>of</t> <t>DPYD</t> in 53BP1 transfected cells. (C) The protein levels of TS and DPYD in 53BP1 transfected cells. (D) The transfection efficiency of <t>siRNA</t> TS was confirmed by western blot analysis. (E) The transfection efficiency of siRNA DPYD was confirmed by western blot analysis. Results are shown for one of the three independent experiments performed. **p<0.01, ***p<0.001.
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    (A) The mRNA levels of TS in 53BP1 transfected MDA-MB-231 and MCF-7 cells. (B) The mRNA levels <t>of</t> <t>DPYD</t> in 53BP1 transfected cells. (C) The protein levels of TS and DPYD in 53BP1 transfected cells. (D) The transfection efficiency of <t>siRNA</t> TS was confirmed by western blot analysis. (E) The transfection efficiency of siRNA DPYD was confirmed by western blot analysis. Results are shown for one of the three independent experiments performed. **p<0.01, ***p<0.001.
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    Cell Signaling Technology Inc cofilin sirna i
    a Left: Representative F-actin images in control and <t>cofilin-depleted</t> hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Zoomed regions display details of F-actin organization in the apical region of the nucleus. Right: Corresponding quantification of the percentages of hMSCs having an actin cap ( n = 3 experiments per group). b Left: Representative YAP images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Right: Corresponding quantification of YAP nuc/cyto ratios (from left to right n = 62, 58, 68, 72, 65, 68 cells). c Top: Representative pCofilin images in hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Bottom: Corresponding quantification of pCofilin level based on the immunostaining (from left to right n = 107, 136, 118 cells). Data are presented as mean ± s.e.m., and p values were obtained using one-way ANOVA followed by Tukey’s post hoc test ( a – c ). Scale bars: 30 µm ( a – c ). Source data are provided as a Source Data file.
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    Increased <t>cofilin-1</t> expression alters actin dynamics in Emery-Dreifuss muscular dystrophy (EDMD) (A) Schematic representation of actin dynamics mechanisms. (B) Immunoblots showing pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. GAPDH is shown as loading control. (C) Quantification of pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein expression level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. ∗∗ p ≤ 0.001 between old WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD. (D) Immunoblots showing cofilin-1protein level in skeletal muscle from EDMD patient carrying LMNA mutation. GAPDH is shown as loading control. Data are represented as mean ± SD. (E) Immunoblot showing G-actin and F-actin protein levels in soleus from old WT (n = 3) and Lmna p.H222P/H222P (H222P) (n = 3) mice.
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    Cell Signaling Technology Inc cofilin 1
    Increased <t>cofilin-1</t> expression alters actin dynamics in Emery-Dreifuss muscular dystrophy (EDMD) (A) Schematic representation of actin dynamics mechanisms. (B) Immunoblots showing pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. GAPDH is shown as loading control. (C) Quantification of pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein expression level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. ∗∗ p ≤ 0.001 between old WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD. (D) Immunoblots showing cofilin-1protein level in skeletal muscle from EDMD patient carrying LMNA mutation. GAPDH is shown as loading control. Data are represented as mean ± SD. (E) Immunoblot showing G-actin and F-actin protein levels in soleus from old WT (n = 3) and Lmna p.H222P/H222P (H222P) (n = 3) mice.
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    Increased <t>cofilin-1</t> expression alters actin dynamics in Emery-Dreifuss muscular dystrophy (EDMD) (A) Schematic representation of actin dynamics mechanisms. (B) Immunoblots showing pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. GAPDH is shown as loading control. (C) Quantification of pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein expression level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. ∗∗ p ≤ 0.001 between old WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD. (D) Immunoblots showing cofilin-1protein level in skeletal muscle from EDMD patient carrying LMNA mutation. GAPDH is shown as loading control. Data are represented as mean ± SD. (E) Immunoblot showing G-actin and F-actin protein levels in soleus from old WT (n = 3) and Lmna p.H222P/H222P (H222P) (n = 3) mice.
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    LM11A-31 treatment modulates mechanisms regulating tau cleavage and phosphorylation. a – f Western blots of hippocampal extracts (representative examples shown) were quantitated by determining ratios of cleaved to non-cleaved fragments or actin, or ratios of phospho (p)-protein over total protein and normalized to the mean of Ntg-vehicle mice a ratio of ~ 145 kDa α-fodrin calpain cleavage fragments to actin. b Ratio of CDK5 regulatory subunit p25 (active, calpain cleavage product) to full length p35 inactive subunit. c p-JNK T183/Y185 to total JNK. d p-GSK3β S9 to total GSK3β, e p-ERK T202/Y204 to total ERK. f <t>p-cofilin</t> S3 to total cofilin. p-values for the indicated comparisons are shown and statistical significance was determined using an ANOVA with post hoc Sidak’s multiple comparisons test; n = 6–11 mice per group, with two or three independent western blots averaged per animal
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    LM11A-31 treatment modulates mechanisms regulating tau cleavage and phosphorylation. a – f Western blots of hippocampal extracts (representative examples shown) were quantitated by determining ratios of cleaved to non-cleaved fragments or actin, or ratios of phospho (p)-protein over total protein and normalized to the mean of Ntg-vehicle mice a ratio of ~ 145 kDa α-fodrin calpain cleavage fragments to actin. b Ratio of CDK5 regulatory subunit p25 (active, calpain cleavage product) to full length p35 inactive subunit. c p-JNK T183/Y185 to total JNK. d p-GSK3β S9 to total GSK3β, e p-ERK T202/Y204 to total ERK. f <t>p-cofilin</t> S3 to total cofilin. p-values for the indicated comparisons are shown and statistical significance was determined using an ANOVA with post hoc Sidak’s multiple comparisons test; n = 6–11 mice per group, with two or three independent western blots averaged per animal
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    Image Search Results


    (A) The mRNA levels of TS in 53BP1 transfected MDA-MB-231 and MCF-7 cells. (B) The mRNA levels of DPYD in 53BP1 transfected cells. (C) The protein levels of TS and DPYD in 53BP1 transfected cells. (D) The transfection efficiency of siRNA TS was confirmed by western blot analysis. (E) The transfection efficiency of siRNA DPYD was confirmed by western blot analysis. Results are shown for one of the three independent experiments performed. **p<0.01, ***p<0.001.

    Journal: PLoS ONE

    Article Title: 53BP1 Sensitizes Breast Cancer Cells to 5-Fluorouracil

    doi: 10.1371/journal.pone.0074928

    Figure Lengend Snippet: (A) The mRNA levels of TS in 53BP1 transfected MDA-MB-231 and MCF-7 cells. (B) The mRNA levels of DPYD in 53BP1 transfected cells. (C) The protein levels of TS and DPYD in 53BP1 transfected cells. (D) The transfection efficiency of siRNA TS was confirmed by western blot analysis. (E) The transfection efficiency of siRNA DPYD was confirmed by western blot analysis. Results are shown for one of the three independent experiments performed. **p<0.01, ***p<0.001.

    Article Snippet: Signal silence TS siRNA, DPYD siRNA and their control siRNA were purchase from Cell Signaling Technology.

    Techniques: Transfection, Western Blot

    a Left: Representative F-actin images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Zoomed regions display details of F-actin organization in the apical region of the nucleus. Right: Corresponding quantification of the percentages of hMSCs having an actin cap ( n = 3 experiments per group). b Left: Representative YAP images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Right: Corresponding quantification of YAP nuc/cyto ratios (from left to right n = 62, 58, 68, 72, 65, 68 cells). c Top: Representative pCofilin images in hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Bottom: Corresponding quantification of pCofilin level based on the immunostaining (from left to right n = 107, 136, 118 cells). Data are presented as mean ± s.e.m., and p values were obtained using one-way ANOVA followed by Tukey’s post hoc test ( a – c ). Scale bars: 30 µm ( a – c ). Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Programmable integrin and N-cadherin adhesive interactions modulate mechanosensing of mesenchymal stem cells by cofilin phosphorylation

    doi: 10.1038/s41467-022-34424-0

    Figure Lengend Snippet: a Left: Representative F-actin images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Zoomed regions display details of F-actin organization in the apical region of the nucleus. Right: Corresponding quantification of the percentages of hMSCs having an actin cap ( n = 3 experiments per group). b Left: Representative YAP images in control and cofilin-depleted hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Right: Corresponding quantification of YAP nuc/cyto ratios (from left to right n = 62, 58, 68, 72, 65, 68 cells). c Top: Representative pCofilin images in hMSCs on “OFF”, “ON” and “Dual ON” substrates for 1 d. Bottom: Corresponding quantification of pCofilin level based on the immunostaining (from left to right n = 107, 136, 118 cells). Data are presented as mean ± s.e.m., and p values were obtained using one-way ANOVA followed by Tukey’s post hoc test ( a – c ). Scale bars: 30 µm ( a – c ). Source data are provided as a Source Data file.

    Article Snippet: The siRNAs used were cofilin siRNA I (Cell Signaling, 6267) and control siRNA (Cell Signaling, 6568).

    Techniques: Immunostaining

    Increased cofilin-1 expression alters actin dynamics in Emery-Dreifuss muscular dystrophy (EDMD) (A) Schematic representation of actin dynamics mechanisms. (B) Immunoblots showing pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. GAPDH is shown as loading control. (C) Quantification of pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein expression level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. ∗∗ p ≤ 0.001 between old WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD. (D) Immunoblots showing cofilin-1protein level in skeletal muscle from EDMD patient carrying LMNA mutation. GAPDH is shown as loading control. Data are represented as mean ± SD. (E) Immunoblot showing G-actin and F-actin protein levels in soleus from old WT (n = 3) and Lmna p.H222P/H222P (H222P) (n = 3) mice.

    Journal: Cell Reports

    Article Title: The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies

    doi: 10.1016/j.celrep.2021.109601

    Figure Lengend Snippet: Increased cofilin-1 expression alters actin dynamics in Emery-Dreifuss muscular dystrophy (EDMD) (A) Schematic representation of actin dynamics mechanisms. (B) Immunoblots showing pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. GAPDH is shown as loading control. (C) Quantification of pERK1/2, ERK1/2, cofilin-1, profilin-1, ARP2, and N-WASP protein expression level in soleus from old WT (n = 5) and Lmna p.H222P/H222P (H222P) (n = 5) mice. ∗∗ p ≤ 0.001 between old WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD. (D) Immunoblots showing cofilin-1protein level in skeletal muscle from EDMD patient carrying LMNA mutation. GAPDH is shown as loading control. Data are represented as mean ± SD. (E) Immunoblot showing G-actin and F-actin protein levels in soleus from old WT (n = 3) and Lmna p.H222P/H222P (H222P) (n = 3) mice.

    Article Snippet: SignalSilence® Cofilin siRNA I , Cell Signaling , Cat #6267.

    Techniques: Expressing, Western Blot, Mutagenesis

    Increased cofilin-1 expression is under the control of ERK1/2 signaling (A) Representative immunoblots and quantification of cofilin-1, N-WASP, ARP2, and profilin-1 protein expression in C2C12 cells stably expressing WT (C2-WT) (n = 3) or p.H222P (C2-H222P) (n = 3) lamin A. GAPDH is shown as loading control. C2-H222P cells were either untreated or treated with selumetinib. ∗∗ p ≤ 0.001 between C2-WT and C2-H222P ± selumetinib. Data are represented as mean ± SD. (B) Representative immunoblot and quantification of effects of washout of selumetinib on cofilin-1, N-WASP, ARP2 and profilin-1 protein expression level in C2-H222P cells. Data are represented as mean ± SD. (C) Representative immunoblot showing effects of transfection with ERK2 and MEK1 constructs on cofilin-1 protein expression in C2-WT and C2-H222P cells. GAPDH is shown as loading control. (D) Cycloheximide chase experiment using C2C12 cells stably expressing WT (C2-WT) or p.H222P (C2-H222P) lamin A, treated or not with selumetinib. Cells were treated with 50 μM cycloheximide and lysed at the indicated times for western blot analysis using anti-cofilin-1 antibody. GAPDH was used as a loading control. (E) Quantification of cofilin-1 signal intensity normalized to GAPDH content and expressed as the percent change from time zero, which was set at 100%. Data are represented as mean ± SD. (F) Representative immunoblots showing effects of transfection with different mutated lamin A constructs on cofilin-1 expression in C2C12 cells. (G) Representative immunoblot showing the effect of cofilin-1 siRNA on cofilin-1 expression. GAPDH is shown as a loading control. (H) Representative immunoblot showing the effect of cofilin-1 siRNA on G-actin and F-actin expression in C2-H222P cells. Cytochalasin D (cytoD) induces actin depolymerization.

    Journal: Cell Reports

    Article Title: The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies

    doi: 10.1016/j.celrep.2021.109601

    Figure Lengend Snippet: Increased cofilin-1 expression is under the control of ERK1/2 signaling (A) Representative immunoblots and quantification of cofilin-1, N-WASP, ARP2, and profilin-1 protein expression in C2C12 cells stably expressing WT (C2-WT) (n = 3) or p.H222P (C2-H222P) (n = 3) lamin A. GAPDH is shown as loading control. C2-H222P cells were either untreated or treated with selumetinib. ∗∗ p ≤ 0.001 between C2-WT and C2-H222P ± selumetinib. Data are represented as mean ± SD. (B) Representative immunoblot and quantification of effects of washout of selumetinib on cofilin-1, N-WASP, ARP2 and profilin-1 protein expression level in C2-H222P cells. Data are represented as mean ± SD. (C) Representative immunoblot showing effects of transfection with ERK2 and MEK1 constructs on cofilin-1 protein expression in C2-WT and C2-H222P cells. GAPDH is shown as loading control. (D) Cycloheximide chase experiment using C2C12 cells stably expressing WT (C2-WT) or p.H222P (C2-H222P) lamin A, treated or not with selumetinib. Cells were treated with 50 μM cycloheximide and lysed at the indicated times for western blot analysis using anti-cofilin-1 antibody. GAPDH was used as a loading control. (E) Quantification of cofilin-1 signal intensity normalized to GAPDH content and expressed as the percent change from time zero, which was set at 100%. Data are represented as mean ± SD. (F) Representative immunoblots showing effects of transfection with different mutated lamin A constructs on cofilin-1 expression in C2C12 cells. (G) Representative immunoblot showing the effect of cofilin-1 siRNA on cofilin-1 expression. GAPDH is shown as a loading control. (H) Representative immunoblot showing the effect of cofilin-1 siRNA on G-actin and F-actin expression in C2-H222P cells. Cytochalasin D (cytoD) induces actin depolymerization.

    Article Snippet: SignalSilence® Cofilin siRNA I , Cell Signaling , Cat #6267.

    Techniques: Expressing, Western Blot, Stable Transfection, Transfection, Construct

    pERK1/2 protects cofilin-1 from degradation by the ubiquitin-proteasome pathway (A) Immunoblot showing effect of treatment with proteasome inhibitor MG132 on cofilin-1 expression in C2-H222P cells untreated or treated with selumetinib. GAPDH is shown as loading control. (B) Immunoblot showing effect of treatment with proteasome inhibitor MG132 treatment on cofilin-1 expression in C2-WT cells. GAPDH is shown as loading control. (C) Immunoprecipitation of cofilin-1 showing ubiquitination levels in C2-WT and C2-H222P cells untreated or treated with selumetinib. Input is shown as loading control. (D) Proteasome activity in C2-WT and C2-H222P cells untreated or treated with selumetinib. Data are represented as mean ± SD. (E) Immunoblot showing effect of selumetinib and MG132 on ectopically expressed mCherry-tagged cofilin-1, cofilin-1(T25A), and cofilin-1(T25D) in C2-WT cells. GAPDH is shown as loading control. (F) Quantification of mCherry signal intensity normalized to GAPDH content in C2-WT cells treated with the different conditions (n = 3). Data are represented as mean ± SD.

    Journal: Cell Reports

    Article Title: The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies

    doi: 10.1016/j.celrep.2021.109601

    Figure Lengend Snippet: pERK1/2 protects cofilin-1 from degradation by the ubiquitin-proteasome pathway (A) Immunoblot showing effect of treatment with proteasome inhibitor MG132 on cofilin-1 expression in C2-H222P cells untreated or treated with selumetinib. GAPDH is shown as loading control. (B) Immunoblot showing effect of treatment with proteasome inhibitor MG132 treatment on cofilin-1 expression in C2-WT cells. GAPDH is shown as loading control. (C) Immunoprecipitation of cofilin-1 showing ubiquitination levels in C2-WT and C2-H222P cells untreated or treated with selumetinib. Input is shown as loading control. (D) Proteasome activity in C2-WT and C2-H222P cells untreated or treated with selumetinib. Data are represented as mean ± SD. (E) Immunoblot showing effect of selumetinib and MG132 on ectopically expressed mCherry-tagged cofilin-1, cofilin-1(T25A), and cofilin-1(T25D) in C2-WT cells. GAPDH is shown as loading control. (F) Quantification of mCherry signal intensity normalized to GAPDH content in C2-WT cells treated with the different conditions (n = 3). Data are represented as mean ± SD.

    Article Snippet: SignalSilence® Cofilin siRNA I , Cell Signaling , Cat #6267.

    Techniques: Western Blot, Expressing, Immunoprecipitation, Activity Assay

    Alteration of sarcomere organization in EDMD (A) Left: immunofluorescence micrographs of sarcomeric α-actinin (green) and sarcomeric α-actin (red) labeled soleus muscle from old, WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 5 μm. Right: immunofluorescence micrographs of titin (green) and sarcomeric α-actinin (red) labeled soleus muscle from old, WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 8 μm. (B) Electron microscopy showing sarcomeric disorganization in soleus muscles from old WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 2 μm. (C) Left: electron microscopy showing sarcomeric disorganization in striated muscles from EDMD patients carrying LMNA mutations. Right: striated muscle from human control. Scale bar, 10 μm (D) Growth rate of single cofilin domains for eGFP-cofilin-1 WT and T25D, observed on individual actin filaments in vitro , in the presence of 200 nM cofilin-1 (n = 10 filaments for each condition). The distributions are plotted as violin plots, with the white dot representing its median. The statistical test was a t test for the means of two independent samples with unequal variance. (E) Single eGFP-cofilin-1 WT or T25D domain severing rate. Time t = 0 is defined for every domain as the frame on which they nucleate. n = 152 and 202 cofilin domains for eGFP-cofilin-1 WT and T25D, respectively.

    Journal: Cell Reports

    Article Title: The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies

    doi: 10.1016/j.celrep.2021.109601

    Figure Lengend Snippet: Alteration of sarcomere organization in EDMD (A) Left: immunofluorescence micrographs of sarcomeric α-actinin (green) and sarcomeric α-actin (red) labeled soleus muscle from old, WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 5 μm. Right: immunofluorescence micrographs of titin (green) and sarcomeric α-actinin (red) labeled soleus muscle from old, WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 8 μm. (B) Electron microscopy showing sarcomeric disorganization in soleus muscles from old WT and Lmna p.H222P/H222P (H222P) mice. Scale bar, 2 μm. (C) Left: electron microscopy showing sarcomeric disorganization in striated muscles from EDMD patients carrying LMNA mutations. Right: striated muscle from human control. Scale bar, 10 μm (D) Growth rate of single cofilin domains for eGFP-cofilin-1 WT and T25D, observed on individual actin filaments in vitro , in the presence of 200 nM cofilin-1 (n = 10 filaments for each condition). The distributions are plotted as violin plots, with the white dot representing its median. The statistical test was a t test for the means of two independent samples with unequal variance. (E) Single eGFP-cofilin-1 WT or T25D domain severing rate. Time t = 0 is defined for every domain as the frame on which they nucleate. n = 152 and 202 cofilin domains for eGFP-cofilin-1 WT and T25D, respectively.

    Article Snippet: SignalSilence® Cofilin siRNA I , Cell Signaling , Cat #6267.

    Techniques: Immunofluorescence, Labeling, Electron Microscopy, In Vitro

    Cofilin-1 is involved in the muscle force generation in vivo (A) Schematic representation of the experimental procedure followed for transduction with AAV vectors expressing cofilin-1 constructs of soleus muscles in young WT mice. (B) Representative immunoblot of cofilin-1 protein levels in soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. GAPDH is shown as loading control. (C) Representative immunoblot showing the effect of AAV expressing cofilin-1 construct on G-actin and F-actin expression in the soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. (D) Tetanic force of soleus from WT (n = 17), Lmna p.H222P/H222P (H222P) (n = 9) and WT mice injected with either PBS (n = 4) or AAV vectors expressing cofilin-1 (n = 7), cofilin-1(T25A) (n = 3) or cofilin-1(T25D) (n = 3). ∗ p ≤ 0.01 between WT and Lmna p.H222P/H222P (H222P), ∗∗ p ≤ 0.001 between WT and WT AAV vectors expressing cofilin-1, ∗∗∗ p ≤ 0.0001 between WT and WT AAV vectors expressing cofilin-1(T25D). Data are represented as mean ± SD. (E) Sirius Red staining of cross sections of soleus muscles from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. Section of soleus muscle from Lmna p.H222P/H222P (H222P) is shown as control. Scale bar, 50 μm. (F) Expression of fibrosis-related genes ( Col1a2 , Col3a1 , and Ctgf ) in the soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. Quantification of soleus muscle from Lmna p.H222P/H222P (H222P) is shown as control. ∗ p ≤ 0.01 between WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD.

    Journal: Cell Reports

    Article Title: The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies

    doi: 10.1016/j.celrep.2021.109601

    Figure Lengend Snippet: Cofilin-1 is involved in the muscle force generation in vivo (A) Schematic representation of the experimental procedure followed for transduction with AAV vectors expressing cofilin-1 constructs of soleus muscles in young WT mice. (B) Representative immunoblot of cofilin-1 protein levels in soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. GAPDH is shown as loading control. (C) Representative immunoblot showing the effect of AAV expressing cofilin-1 construct on G-actin and F-actin expression in the soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. (D) Tetanic force of soleus from WT (n = 17), Lmna p.H222P/H222P (H222P) (n = 9) and WT mice injected with either PBS (n = 4) or AAV vectors expressing cofilin-1 (n = 7), cofilin-1(T25A) (n = 3) or cofilin-1(T25D) (n = 3). ∗ p ≤ 0.01 between WT and Lmna p.H222P/H222P (H222P), ∗∗ p ≤ 0.001 between WT and WT AAV vectors expressing cofilin-1, ∗∗∗ p ≤ 0.0001 between WT and WT AAV vectors expressing cofilin-1(T25D). Data are represented as mean ± SD. (E) Sirius Red staining of cross sections of soleus muscles from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. Section of soleus muscle from Lmna p.H222P/H222P (H222P) is shown as control. Scale bar, 50 μm. (F) Expression of fibrosis-related genes ( Col1a2 , Col3a1 , and Ctgf ) in the soleus from WT mice non-injected or injected with either PBS or AAV vector expressing cofilin-1 constructs. Quantification of soleus muscle from Lmna p.H222P/H222P (H222P) is shown as control. ∗ p ≤ 0.01 between WT and Lmna p.H222P/H222P (H222P). Data are represented as mean ± SD.

    Article Snippet: SignalSilence® Cofilin siRNA I , Cell Signaling , Cat #6267.

    Techniques: In Vivo, Transduction, Expressing, Construct, Western Blot, Injection, Plasmid Preparation, Staining

    Schematic representation of the mechanism of pERK1/2-mediated protection of cofilin-1 from proteasome degradation and its consequences on sarcomeric actin depolymerization in striated muscle diseases caused by LMNA mutations

    Journal: Cell Reports

    Article Title: The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies

    doi: 10.1016/j.celrep.2021.109601

    Figure Lengend Snippet: Schematic representation of the mechanism of pERK1/2-mediated protection of cofilin-1 from proteasome degradation and its consequences on sarcomeric actin depolymerization in striated muscle diseases caused by LMNA mutations

    Article Snippet: SignalSilence® Cofilin siRNA I , Cell Signaling , Cat #6267.

    Techniques:

    Journal: Cell Reports

    Article Title: The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies

    doi: 10.1016/j.celrep.2021.109601

    Figure Lengend Snippet:

    Article Snippet: SignalSilence® Cofilin siRNA I , Cell Signaling , Cat #6267.

    Techniques: Mutagenesis, Recombinant, Activity Assay, In Vivo, SYBR Green Assay, Transfection, Plasmid Preparation, Software, Microarray

    LM11A-31 treatment modulates mechanisms regulating tau cleavage and phosphorylation. a – f Western blots of hippocampal extracts (representative examples shown) were quantitated by determining ratios of cleaved to non-cleaved fragments or actin, or ratios of phospho (p)-protein over total protein and normalized to the mean of Ntg-vehicle mice a ratio of ~ 145 kDa α-fodrin calpain cleavage fragments to actin. b Ratio of CDK5 regulatory subunit p25 (active, calpain cleavage product) to full length p35 inactive subunit. c p-JNK T183/Y185 to total JNK. d p-GSK3β S9 to total GSK3β, e p-ERK T202/Y204 to total ERK. f p-cofilin S3 to total cofilin. p-values for the indicated comparisons are shown and statistical significance was determined using an ANOVA with post hoc Sidak’s multiple comparisons test; n = 6–11 mice per group, with two or three independent western blots averaged per animal

    Journal: Acta Neuropathologica Communications

    Article Title: Small-molecule modulation of the p75 neurotrophin receptor inhibits a wide range of tau molecular pathologies and their sequelae in P301S tauopathy mice

    doi: 10.1186/s40478-020-01034-0

    Figure Lengend Snippet: LM11A-31 treatment modulates mechanisms regulating tau cleavage and phosphorylation. a – f Western blots of hippocampal extracts (representative examples shown) were quantitated by determining ratios of cleaved to non-cleaved fragments or actin, or ratios of phospho (p)-protein over total protein and normalized to the mean of Ntg-vehicle mice a ratio of ~ 145 kDa α-fodrin calpain cleavage fragments to actin. b Ratio of CDK5 regulatory subunit p25 (active, calpain cleavage product) to full length p35 inactive subunit. c p-JNK T183/Y185 to total JNK. d p-GSK3β S9 to total GSK3β, e p-ERK T202/Y204 to total ERK. f p-cofilin S3 to total cofilin. p-values for the indicated comparisons are shown and statistical significance was determined using an ANOVA with post hoc Sidak’s multiple comparisons test; n = 6–11 mice per group, with two or three independent western blots averaged per animal

    Article Snippet: PHF-1 and MC1 (each 1:1000, gifts from Peter Davies); p-cofilin Ser3 , cofilin, p-JNK Thr183/Tyr185 , JNK, p-GSK3β Ser9 , GSK3β, pERK Thr202/Tyr204 , ERK and Tau (D1M9X) XP ® Rabbit mAb (1:1000, Cell Signaling, Danvers, MA); α-fodrin and p35/p25 (1:1000; Santa Cruz Biotechnology, Santa Cruz, CA); actin (1:10,000; Sigma, St. Louis, MO).

    Techniques: Western Blot