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er α antibody  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc er α antibody
    Compression loading induces the expression of USP26 through phosphorylation of <t>estrogen</t> <t>receptor-α</t> at serine 118. Dual-luciferase reporter assays to detect Usp26 promoter activity ( a ) and quantitative analysis of Usp26 mRNA expression ( b ) were conducted in chondrocytes under compression stimulation at levels of 0 and 15 kPa for a duration of 4 h, with or <t>without</t> <t>ER-α</t> knockdown. c The common binding sites of ER-α on the Usp26 gene promoter were further analyzed and screened through three public databases: hTFtarget, Jaspar, and HOCOMOCO. d The binding site mutation significantly impaired the Usp26 promoter activity induced by compression loading in primary human chondrocytes. e ChIP‒qPCR analysis of the binding sites of ER-α to the Usp26 gene promoter in primary human chondrocytes. f Western blot to detect the phosphorylation of serine 118 of ER-α under compression loading in primary human chondrocytes. The phosphorylation-deficient S118A mutation significantly attenuated the compression-induced increases in Usp26 promoter activity ( g ) and mRNA expression ( h ) in primary human chondrocyte. i The S118A mutation significantly restored the decreased protein level of FBP2 caused by compression loading. Immunofluorescence staining to detect phosphorylation of ER-α at S118 in chondrocytes during skeletal growth ( j ), bone fracture healing ( k ), and osteoarthritis ( l ). White and Red scale bars indicated 500 μm. m Schematic of USP26 facilitates endochondral ossification by driving chondrocyte hypertrophy and mineralization. *** P < 0.001. P -values were analyzed by two-way ANOVA in a , b , d , e and one-way ANOVA in g , h
    Er α Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/er α antibody/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    er α antibody - by Bioz Stars, 2026-05
    86/100 stars

    Images

    1) Product Images from "Ubiquitin-specific protease 26 facilitates endochondral ossification by driving chondrocyte hypertrophy and mineralization"

    Article Title: Ubiquitin-specific protease 26 facilitates endochondral ossification by driving chondrocyte hypertrophy and mineralization

    Journal: Bone Research

    doi: 10.1038/s41413-026-00517-5

    Compression loading induces the expression of USP26 through phosphorylation of estrogen receptor-α at serine 118. Dual-luciferase reporter assays to detect Usp26 promoter activity ( a ) and quantitative analysis of Usp26 mRNA expression ( b ) were conducted in chondrocytes under compression stimulation at levels of 0 and 15 kPa for a duration of 4 h, with or without ER-α knockdown. c The common binding sites of ER-α on the Usp26 gene promoter were further analyzed and screened through three public databases: hTFtarget, Jaspar, and HOCOMOCO. d The binding site mutation significantly impaired the Usp26 promoter activity induced by compression loading in primary human chondrocytes. e ChIP‒qPCR analysis of the binding sites of ER-α to the Usp26 gene promoter in primary human chondrocytes. f Western blot to detect the phosphorylation of serine 118 of ER-α under compression loading in primary human chondrocytes. The phosphorylation-deficient S118A mutation significantly attenuated the compression-induced increases in Usp26 promoter activity ( g ) and mRNA expression ( h ) in primary human chondrocyte. i The S118A mutation significantly restored the decreased protein level of FBP2 caused by compression loading. Immunofluorescence staining to detect phosphorylation of ER-α at S118 in chondrocytes during skeletal growth ( j ), bone fracture healing ( k ), and osteoarthritis ( l ). White and Red scale bars indicated 500 μm. m Schematic of USP26 facilitates endochondral ossification by driving chondrocyte hypertrophy and mineralization. *** P < 0.001. P -values were analyzed by two-way ANOVA in a , b , d , e and one-way ANOVA in g , h
    Figure Legend Snippet: Compression loading induces the expression of USP26 through phosphorylation of estrogen receptor-α at serine 118. Dual-luciferase reporter assays to detect Usp26 promoter activity ( a ) and quantitative analysis of Usp26 mRNA expression ( b ) were conducted in chondrocytes under compression stimulation at levels of 0 and 15 kPa for a duration of 4 h, with or without ER-α knockdown. c The common binding sites of ER-α on the Usp26 gene promoter were further analyzed and screened through three public databases: hTFtarget, Jaspar, and HOCOMOCO. d The binding site mutation significantly impaired the Usp26 promoter activity induced by compression loading in primary human chondrocytes. e ChIP‒qPCR analysis of the binding sites of ER-α to the Usp26 gene promoter in primary human chondrocytes. f Western blot to detect the phosphorylation of serine 118 of ER-α under compression loading in primary human chondrocytes. The phosphorylation-deficient S118A mutation significantly attenuated the compression-induced increases in Usp26 promoter activity ( g ) and mRNA expression ( h ) in primary human chondrocyte. i The S118A mutation significantly restored the decreased protein level of FBP2 caused by compression loading. Immunofluorescence staining to detect phosphorylation of ER-α at S118 in chondrocytes during skeletal growth ( j ), bone fracture healing ( k ), and osteoarthritis ( l ). White and Red scale bars indicated 500 μm. m Schematic of USP26 facilitates endochondral ossification by driving chondrocyte hypertrophy and mineralization. *** P < 0.001. P -values were analyzed by two-way ANOVA in a , b , d , e and one-way ANOVA in g , h

    Techniques Used: Expressing, Phospho-proteomics, Luciferase, Activity Assay, Knockdown, Binding Assay, Mutagenesis, Western Blot, Immunofluorescence, Staining



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    Compression loading induces the expression of USP26 through phosphorylation of <t>estrogen</t> <t>receptor-α</t> at serine 118. Dual-luciferase reporter assays to detect Usp26 promoter activity ( a ) and quantitative analysis of Usp26 mRNA expression ( b ) were conducted in chondrocytes under compression stimulation at levels of 0 and 15 kPa for a duration of 4 h, with or <t>without</t> <t>ER-α</t> knockdown. c The common binding sites of ER-α on the Usp26 gene promoter were further analyzed and screened through three public databases: hTFtarget, Jaspar, and HOCOMOCO. d The binding site mutation significantly impaired the Usp26 promoter activity induced by compression loading in primary human chondrocytes. e ChIP‒qPCR analysis of the binding sites of ER-α to the Usp26 gene promoter in primary human chondrocytes. f Western blot to detect the phosphorylation of serine 118 of ER-α under compression loading in primary human chondrocytes. The phosphorylation-deficient S118A mutation significantly attenuated the compression-induced increases in Usp26 promoter activity ( g ) and mRNA expression ( h ) in primary human chondrocyte. i The S118A mutation significantly restored the decreased protein level of FBP2 caused by compression loading. Immunofluorescence staining to detect phosphorylation of ER-α at S118 in chondrocytes during skeletal growth ( j ), bone fracture healing ( k ), and osteoarthritis ( l ). White and Red scale bars indicated 500 μm. m Schematic of USP26 facilitates endochondral ossification by driving chondrocyte hypertrophy and mineralization. *** P < 0.001. P -values were analyzed by two-way ANOVA in a , b , d , e and one-way ANOVA in g , h
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    Image Search Results


    Compression loading induces the expression of USP26 through phosphorylation of estrogen receptor-α at serine 118. Dual-luciferase reporter assays to detect Usp26 promoter activity ( a ) and quantitative analysis of Usp26 mRNA expression ( b ) were conducted in chondrocytes under compression stimulation at levels of 0 and 15 kPa for a duration of 4 h, with or without ER-α knockdown. c The common binding sites of ER-α on the Usp26 gene promoter were further analyzed and screened through three public databases: hTFtarget, Jaspar, and HOCOMOCO. d The binding site mutation significantly impaired the Usp26 promoter activity induced by compression loading in primary human chondrocytes. e ChIP‒qPCR analysis of the binding sites of ER-α to the Usp26 gene promoter in primary human chondrocytes. f Western blot to detect the phosphorylation of serine 118 of ER-α under compression loading in primary human chondrocytes. The phosphorylation-deficient S118A mutation significantly attenuated the compression-induced increases in Usp26 promoter activity ( g ) and mRNA expression ( h ) in primary human chondrocyte. i The S118A mutation significantly restored the decreased protein level of FBP2 caused by compression loading. Immunofluorescence staining to detect phosphorylation of ER-α at S118 in chondrocytes during skeletal growth ( j ), bone fracture healing ( k ), and osteoarthritis ( l ). White and Red scale bars indicated 500 μm. m Schematic of USP26 facilitates endochondral ossification by driving chondrocyte hypertrophy and mineralization. *** P < 0.001. P -values were analyzed by two-way ANOVA in a , b , d , e and one-way ANOVA in g , h

    Journal: Bone Research

    Article Title: Ubiquitin-specific protease 26 facilitates endochondral ossification by driving chondrocyte hypertrophy and mineralization

    doi: 10.1038/s41413-026-00517-5

    Figure Lengend Snippet: Compression loading induces the expression of USP26 through phosphorylation of estrogen receptor-α at serine 118. Dual-luciferase reporter assays to detect Usp26 promoter activity ( a ) and quantitative analysis of Usp26 mRNA expression ( b ) were conducted in chondrocytes under compression stimulation at levels of 0 and 15 kPa for a duration of 4 h, with or without ER-α knockdown. c The common binding sites of ER-α on the Usp26 gene promoter were further analyzed and screened through three public databases: hTFtarget, Jaspar, and HOCOMOCO. d The binding site mutation significantly impaired the Usp26 promoter activity induced by compression loading in primary human chondrocytes. e ChIP‒qPCR analysis of the binding sites of ER-α to the Usp26 gene promoter in primary human chondrocytes. f Western blot to detect the phosphorylation of serine 118 of ER-α under compression loading in primary human chondrocytes. The phosphorylation-deficient S118A mutation significantly attenuated the compression-induced increases in Usp26 promoter activity ( g ) and mRNA expression ( h ) in primary human chondrocyte. i The S118A mutation significantly restored the decreased protein level of FBP2 caused by compression loading. Immunofluorescence staining to detect phosphorylation of ER-α at S118 in chondrocytes during skeletal growth ( j ), bone fracture healing ( k ), and osteoarthritis ( l ). White and Red scale bars indicated 500 μm. m Schematic of USP26 facilitates endochondral ossification by driving chondrocyte hypertrophy and mineralization. *** P < 0.001. P -values were analyzed by two-way ANOVA in a , b , d , e and one-way ANOVA in g , h

    Article Snippet: With 10 μL of ER-α antibody (CST, #13258) or negative control anti-IgG (CST, #2729), fragmented chromatin (200 μg) was incubated overnight to form immune complexes, which were coupled to Protein A beads.

    Techniques: Expressing, Phospho-proteomics, Luciferase, Activity Assay, Knockdown, Binding Assay, Mutagenesis, Western Blot, Immunofluorescence, Staining

    In situ PLA demonstrates close proximity between biotinylated fluoxetine as well as HNK and ERα (red dots) in MCF-7 cells and transfected HEK293T cells (magenta), while no PLA signal was detected in HEK293T cells not expressing ERα. ERα-transfected cells are tagged with GFP and are represented in magenta. Blue represents DAPI staining. Arrows point to the PLA signal.

    Journal: bioRxiv

    Article Title: Antidepressants interact with sex steroid receptors and their intracellular signaling components

    doi: 10.64898/2026.03.17.712321

    Figure Lengend Snippet: In situ PLA demonstrates close proximity between biotinylated fluoxetine as well as HNK and ERα (red dots) in MCF-7 cells and transfected HEK293T cells (magenta), while no PLA signal was detected in HEK293T cells not expressing ERα. ERα-transfected cells are tagged with GFP and are represented in magenta. Blue represents DAPI staining. Arrows point to the PLA signal.

    Article Snippet: A group of HEK293T cells were transfected with a plasmid encoding ERα (pEGFP-C1-ER alpha, Addgene, Plasmid #28230) using Lipofectamine 2000 (Thermo Fisher Scientific).

    Techniques: In Situ, Transfection, Expressing, Staining