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rabbit anti β actin polyclonal antibody  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc rabbit anti β actin polyclonal antibody
    BMM were infected or not (NI) with either (A) L. donovani or (B) L. amazonensis metacyclic promastigotes and at the indicated times points, the distribution of CLIMP-63 (red) was assessed by confocal immunofluorescence microscopy. DNA is in blue. White arrowheads denote internalized parasites. 5X-enlarged insets of representative localization of CLIMP-63 are shown. Controls for the specificity of the anti-CLIMP-63 antibody were performed using BMM pretreated with siRNA to CLIMP-63 and infected for 6 h with either L. donovani or L. amazonensis metacyclic promastigotes. Results are representative of at least three independent experiments. (C) Lysates of uninfected BMM (NI) and of BMM infected with either L. donovani or L. amazonensis metacyclic promastigotes were prepared at the indicated time points in lysis buffer containing 10 mM 1,10-phenanthroline. Levels and integrity of CLIMP-63 were assessed by Western blot analysis. <t>β-actin</t> was used a loading control. Immunoblots shown are representative of at least three independent experiments.
    Rabbit Anti β Actin Polyclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 30801 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+%CE%B2+actin/bio_rxiv__64898__2026__03__19__712868-129-47-53?v=Cell+Signaling+Technology+Inc
    Average 99 stars, based on 30801 article reviews
    rabbit anti β actin polyclonal antibody - by Bioz Stars, 2026-07
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    Images

    1) Product Images from "Leishmania exploits the macrophage endoplasmic reticulum-shaping protein CLIMP-63 to modulate mitochondrial biogenesis and bioenergetics"

    Article Title: Leishmania exploits the macrophage endoplasmic reticulum-shaping protein CLIMP-63 to modulate mitochondrial biogenesis and bioenergetics

    Journal: bioRxiv

    doi: 10.64898/2026.03.19.712868

    BMM were infected or not (NI) with either (A) L. donovani or (B) L. amazonensis metacyclic promastigotes and at the indicated times points, the distribution of CLIMP-63 (red) was assessed by confocal immunofluorescence microscopy. DNA is in blue. White arrowheads denote internalized parasites. 5X-enlarged insets of representative localization of CLIMP-63 are shown. Controls for the specificity of the anti-CLIMP-63 antibody were performed using BMM pretreated with siRNA to CLIMP-63 and infected for 6 h with either L. donovani or L. amazonensis metacyclic promastigotes. Results are representative of at least three independent experiments. (C) Lysates of uninfected BMM (NI) and of BMM infected with either L. donovani or L. amazonensis metacyclic promastigotes were prepared at the indicated time points in lysis buffer containing 10 mM 1,10-phenanthroline. Levels and integrity of CLIMP-63 were assessed by Western blot analysis. β-actin was used a loading control. Immunoblots shown are representative of at least three independent experiments.
    Figure Legend Snippet: BMM were infected or not (NI) with either (A) L. donovani or (B) L. amazonensis metacyclic promastigotes and at the indicated times points, the distribution of CLIMP-63 (red) was assessed by confocal immunofluorescence microscopy. DNA is in blue. White arrowheads denote internalized parasites. 5X-enlarged insets of representative localization of CLIMP-63 are shown. Controls for the specificity of the anti-CLIMP-63 antibody were performed using BMM pretreated with siRNA to CLIMP-63 and infected for 6 h with either L. donovani or L. amazonensis metacyclic promastigotes. Results are representative of at least three independent experiments. (C) Lysates of uninfected BMM (NI) and of BMM infected with either L. donovani or L. amazonensis metacyclic promastigotes were prepared at the indicated time points in lysis buffer containing 10 mM 1,10-phenanthroline. Levels and integrity of CLIMP-63 were assessed by Western blot analysis. β-actin was used a loading control. Immunoblots shown are representative of at least three independent experiments.

    Techniques Used: Infection, Immunofluorescence, Microscopy, Lysis, Western Blot, Control



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    BMM were infected or not (NI) with either (A) L. donovani or (B) L. amazonensis metacyclic promastigotes and at the indicated times points, the distribution of CLIMP-63 (red) was assessed by confocal immunofluorescence microscopy. DNA is in blue. White arrowheads denote internalized parasites. 5X-enlarged insets of representative localization of CLIMP-63 are shown. Controls for the specificity of the anti-CLIMP-63 antibody were performed using BMM pretreated with siRNA to CLIMP-63 and infected for 6 h with either L. donovani or L. amazonensis metacyclic promastigotes. Results are representative of at least three independent experiments. (C) Lysates of uninfected BMM (NI) and of BMM infected with either L. donovani or L. amazonensis metacyclic promastigotes were prepared at the indicated time points in lysis buffer containing 10 mM 1,10-phenanthroline. Levels and integrity of CLIMP-63 were assessed by Western blot analysis. <t>β-actin</t> was used a loading control. Immunoblots shown are representative of at least three independent experiments.
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    BMM were infected or not (NI) with either (A) L. donovani or (B) L. amazonensis metacyclic promastigotes and at the indicated times points, the distribution of CLIMP-63 (red) was assessed by confocal immunofluorescence microscopy. DNA is in blue. White arrowheads denote internalized parasites. 5X-enlarged insets of representative localization of CLIMP-63 are shown. Controls for the specificity of the anti-CLIMP-63 antibody were performed using BMM pretreated with siRNA to CLIMP-63 and infected for 6 h with either L. donovani or L. amazonensis metacyclic promastigotes. Results are representative of at least three independent experiments. (C) Lysates of uninfected BMM (NI) and of BMM infected with either L. donovani or L. amazonensis metacyclic promastigotes were prepared at the indicated time points in lysis buffer containing 10 mM 1,10-phenanthroline. Levels and integrity of CLIMP-63 were assessed by Western blot analysis. <t>β-actin</t> was used a loading control. Immunoblots shown are representative of at least three independent experiments.
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    Image Search Results


    Signaling pathways of Garrya flavescens extract under LPS treatment in microglia. ( A ) Western blot analysis of BV-2 cells pre-treated with vehicle or GF, followed by LPS treatment at 10, 30 and 60 min. Antibodies against phosphorylated ERK, p38, AKT and β-Actin were used. ( B – D ) Quantitative analysis of the band intensities: p-ERK/β-Actin ( B ), p-p38/β-Actin ( C ), and p-AKT/β-Actin ( D ). * p < 0.05; ** p < 0.01; Student’s t -test. N = 3 independent cultures. Bars indicate mean ± SD. Abbreviations: GF, Garrya flavescens ; LPS, lipopolysaccharide; CGA, chlorogenic acid; ERK, extracellular signal-regulated kinase; p38, p38 mitogen-activated protein kinase; AKT, protein kinase B; β-actin, beta-actin.

    Journal: Plants

    Article Title: Anti-Inflammatory Properties of Garrya flavescens : Phytochemical Profiling and Mitigation of LPS-Induced Neuroinflammation via ERK Signaling and Mitochondrial Modulation

    doi: 10.3390/plants15091319

    Figure Lengend Snippet: Signaling pathways of Garrya flavescens extract under LPS treatment in microglia. ( A ) Western blot analysis of BV-2 cells pre-treated with vehicle or GF, followed by LPS treatment at 10, 30 and 60 min. Antibodies against phosphorylated ERK, p38, AKT and β-Actin were used. ( B – D ) Quantitative analysis of the band intensities: p-ERK/β-Actin ( B ), p-p38/β-Actin ( C ), and p-AKT/β-Actin ( D ). * p < 0.05; ** p < 0.01; Student’s t -test. N = 3 independent cultures. Bars indicate mean ± SD. Abbreviations: GF, Garrya flavescens ; LPS, lipopolysaccharide; CGA, chlorogenic acid; ERK, extracellular signal-regulated kinase; p38, p38 mitogen-activated protein kinase; AKT, protein kinase B; β-actin, beta-actin.

    Article Snippet: Rabbit anti-β-actin antibody (bs-0061R) was obtained from Bioss (Beijing, China).

    Techniques: Protein-Protein interactions, Western Blot

    Effects of magnesium extracts on lymphangiogenesis-related gene and protein expression in LECs. ( A ) Relative Vegfa mRNA expression levels in LECs treated with Control, Mg (1:10), Mg (1:100), and Mg (1:1000), as determined by qRT-PCR. ( B ) Relative Vegfc mRNA expression levels in LECs under the same treatment conditions. ( C ) Representative Western blot images showing VEGFA and VEGFC protein expression in LECs after treatment with different concentrations of magnesium extracts, with GAPDH used as the internal loading control. ( D ) Additional Western blot analysis showing VEGFR3 protein expression under the same treatment conditions, with β-actin used as the internal loading control. Data in ( A , B ) are presented as the mean ± SD ( n = 3). Statistical analysis for ( A , B ) was performed using one-way ANOVA followed by Tukey’s multiple-comparisons test. Statistical significance is indicated as * p < 0.05, ** p < 0.01; ns, not significant.

    Journal: Biomedicines

    Article Title: Ionic Extracts of Magnesium Powders Promote In Vitro Lymphangiogenesis

    doi: 10.3390/biomedicines14040913

    Figure Lengend Snippet: Effects of magnesium extracts on lymphangiogenesis-related gene and protein expression in LECs. ( A ) Relative Vegfa mRNA expression levels in LECs treated with Control, Mg (1:10), Mg (1:100), and Mg (1:1000), as determined by qRT-PCR. ( B ) Relative Vegfc mRNA expression levels in LECs under the same treatment conditions. ( C ) Representative Western blot images showing VEGFA and VEGFC protein expression in LECs after treatment with different concentrations of magnesium extracts, with GAPDH used as the internal loading control. ( D ) Additional Western blot analysis showing VEGFR3 protein expression under the same treatment conditions, with β-actin used as the internal loading control. Data in ( A , B ) are presented as the mean ± SD ( n = 3). Statistical analysis for ( A , B ) was performed using one-way ANOVA followed by Tukey’s multiple-comparisons test. Statistical significance is indicated as * p < 0.05, ** p < 0.01; ns, not significant.

    Article Snippet: The primary antibodies used in this study included anti-VEGFA rabbit polyclonal antibody (ZEN-BIOSCIENCE Co., Ltd., Chengdu, China), anti-VEGFC rabbit polyclonal antibody (ZEN-BIOSCIENCE Co., Ltd., Chengdu, China), anti-VEGFR3 rabbit polyclonal antibody (Affinity Biosciences, Shanghai, China), anti-GAPDH rabbit polyclonal antibody (Affinity Biosciences, Shanghai, China), and anti-β-actin rabbit polyclonal antibody (Affinity Biosciences, Shanghai, China).

    Techniques: Expressing, Control, Quantitative RT-PCR, Western Blot

    BMM were infected or not (NI) with either (A) L. donovani or (B) L. amazonensis metacyclic promastigotes and at the indicated times points, the distribution of CLIMP-63 (red) was assessed by confocal immunofluorescence microscopy. DNA is in blue. White arrowheads denote internalized parasites. 5X-enlarged insets of representative localization of CLIMP-63 are shown. Controls for the specificity of the anti-CLIMP-63 antibody were performed using BMM pretreated with siRNA to CLIMP-63 and infected for 6 h with either L. donovani or L. amazonensis metacyclic promastigotes. Results are representative of at least three independent experiments. (C) Lysates of uninfected BMM (NI) and of BMM infected with either L. donovani or L. amazonensis metacyclic promastigotes were prepared at the indicated time points in lysis buffer containing 10 mM 1,10-phenanthroline. Levels and integrity of CLIMP-63 were assessed by Western blot analysis. β-actin was used a loading control. Immunoblots shown are representative of at least three independent experiments.

    Journal: bioRxiv

    Article Title: Leishmania exploits the macrophage endoplasmic reticulum-shaping protein CLIMP-63 to modulate mitochondrial biogenesis and bioenergetics

    doi: 10.64898/2026.03.19.712868

    Figure Lengend Snippet: BMM were infected or not (NI) with either (A) L. donovani or (B) L. amazonensis metacyclic promastigotes and at the indicated times points, the distribution of CLIMP-63 (red) was assessed by confocal immunofluorescence microscopy. DNA is in blue. White arrowheads denote internalized parasites. 5X-enlarged insets of representative localization of CLIMP-63 are shown. Controls for the specificity of the anti-CLIMP-63 antibody were performed using BMM pretreated with siRNA to CLIMP-63 and infected for 6 h with either L. donovani or L. amazonensis metacyclic promastigotes. Results are representative of at least three independent experiments. (C) Lysates of uninfected BMM (NI) and of BMM infected with either L. donovani or L. amazonensis metacyclic promastigotes were prepared at the indicated time points in lysis buffer containing 10 mM 1,10-phenanthroline. Levels and integrity of CLIMP-63 were assessed by Western blot analysis. β-actin was used a loading control. Immunoblots shown are representative of at least three independent experiments.

    Article Snippet: The mouse anti-CLIMP-63 monoclonal antibody (sc-393544) was from Santa Cruz Biotechnology, the rabbit anti-RTN4 polyclonal antibody (ab186735) and the rat anti-BrdU (ab6326) were from Abcam, the rabbit polyclonal antibody RTN4 (10950-1-AP) was from Proteintech, the mouse anti-phosphoglycan (Galβ1,4Manα1-PO4) CA7AE monoclonal antibody ( ) was from Cedarlane, the rabbit anti-β-actin polyclonal antibody was from Cell Signalling, the rabbit anti-Tom20 polyclonal antibody (EPR15581-54) was from Abcam, and the rat anti-LAMP-1 monoclonal antibody 1D4B developed by J.T.

    Techniques: Infection, Immunofluorescence, Microscopy, Lysis, Western Blot, Control