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β 2 ar  (Bioss)


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  • 93

    Structured Review

    Bioss β 2 ar
    β 2 Ar, supplied by Bioss, used in various techniques. Bioz Stars score: 93/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+%CE%B2+2+antibody/ADRB2+Polyclonal+Antibody/pmc12971017-68-59-70
    Average 93 stars, based on 24 article reviews
    β 2 ar - by Bioz Stars, 2026-09
    93/100 stars

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    Related Articles

    Hybridization:

    Article Title: Norepinephrine protects against cochlear outer hair cell damage and noise-induced hearing loss via α 2A -adrenergic receptor
    Article Snippet: After electrophoresis, protein samples were transferred into a polyvinylidene fluoride membrane (IPVH00010, Millipore, Burlington, MA, USA) and blocked for 1 h with 5% dry milk in tris buffered saline (TBS) and 0.1% tween-20 (TBST). .. The blots were cut prior to hybridisation with antibodies during blotting, the membranes were incubated with specific primary antibodies: anti-α 1A -specific polyclonal antibody (1:1000, 19777-1-AP, Proteintech), anti-α 1B antibody (1:1000, DF8798, Affinity), anti-α 1D antibody (0.2 μg/ml, ab166925, Abcam), anti-α 2A polyclonal antibody (1:1000, 14266-1-AP, Proteintech), anti-α 2B antibody (1:1000, A8535, ABclonal), anti-α 2C antibody (1:1000, DF3108, Affinity), anti-β 1 antibody (1:1000, bs-0498R, Bioss), anti-β 2 antibody (1:1000, DF3512, Affinity), anti-β 3 antibody (1:1000, bs-1063R, Bioss) and anti-GAPDH polyclonal antibody (1:10000, 10494-1-AP, Proteintech) overnight at 4 °C. .. Then, the membranes were washed in TBST and incubated with secondary antibodies (1:5000 dilution, CWBIO, China) for 1 h followed by chemiluminescent detection (Merck Millipore).

    Incubation:

    Article Title: Norepinephrine protects against cochlear outer hair cell damage and noise-induced hearing loss via α 2A -adrenergic receptor
    Article Snippet: After electrophoresis, protein samples were transferred into a polyvinylidene fluoride membrane (IPVH00010, Millipore, Burlington, MA, USA) and blocked for 1 h with 5% dry milk in tris buffered saline (TBS) and 0.1% tween-20 (TBST). .. The blots were cut prior to hybridisation with antibodies during blotting, the membranes were incubated with specific primary antibodies: anti-α 1A -specific polyclonal antibody (1:1000, 19777-1-AP, Proteintech), anti-α 1B antibody (1:1000, DF8798, Affinity), anti-α 1D antibody (0.2 μg/ml, ab166925, Abcam), anti-α 2A polyclonal antibody (1:1000, 14266-1-AP, Proteintech), anti-α 2B antibody (1:1000, A8535, ABclonal), anti-α 2C antibody (1:1000, DF3108, Affinity), anti-β 1 antibody (1:1000, bs-0498R, Bioss), anti-β 2 antibody (1:1000, DF3512, Affinity), anti-β 3 antibody (1:1000, bs-1063R, Bioss) and anti-GAPDH polyclonal antibody (1:10000, 10494-1-AP, Proteintech) overnight at 4 °C. .. Then, the membranes were washed in TBST and incubated with secondary antibodies (1:5000 dilution, CWBIO, China) for 1 h followed by chemiluminescent detection (Merck Millipore).



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    Mechanism of ECM biosynthesis disorders and <t>abnormal</t> <t>Wnt/β-Catenin</t> signaling pathway transduction in TD models. (A) mRNA levels of ECM biosynthesis factors and canonical Wnt/β-Catenin signaling pathway components. (B) mRNA levels of Cant1. (C) Quantitative analysis of GAG content. (D) Protein blots. (E) Protein levels of ACAN, Col2α1, β-Catenin, and Cant1. (F) Immunofluorescence digital images of CON tibia and TD tibia. (G and H) Relative fluorescence intensity of Cant1 and β-Catenin in ROI of CON tibia and TD tibia.
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    Mechanism of ECM biosynthesis disorders and <t>abnormal</t> <t>Wnt/β-Catenin</t> signaling pathway transduction in TD models. (A) mRNA levels of ECM biosynthesis factors and canonical Wnt/β-Catenin signaling pathway components. (B) mRNA levels of Cant1. (C) Quantitative analysis of GAG content. (D) Protein blots. (E) Protein levels of ACAN, Col2α1, β-Catenin, and Cant1. (F) Immunofluorescence digital images of CON tibia and TD tibia. (G and H) Relative fluorescence intensity of Cant1 and β-Catenin in ROI of CON tibia and TD tibia.
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    Mechanism of ECM biosynthesis disorders and <t>abnormal</t> <t>Wnt/β-Catenin</t> signaling pathway transduction in TD models. (A) mRNA levels of ECM biosynthesis factors and canonical Wnt/β-Catenin signaling pathway components. (B) mRNA levels of Cant1. (C) Quantitative analysis of GAG content. (D) Protein blots. (E) Protein levels of ACAN, Col2α1, β-Catenin, and Cant1. (F) Immunofluorescence digital images of CON tibia and TD tibia. (G and H) Relative fluorescence intensity of Cant1 and β-Catenin in ROI of CON tibia and TD tibia.
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    Image Search Results


    Mechanism of ECM biosynthesis disorders and abnormal Wnt/β-Catenin signaling pathway transduction in TD models. (A) mRNA levels of ECM biosynthesis factors and canonical Wnt/β-Catenin signaling pathway components. (B) mRNA levels of Cant1. (C) Quantitative analysis of GAG content. (D) Protein blots. (E) Protein levels of ACAN, Col2α1, β-Catenin, and Cant1. (F) Immunofluorescence digital images of CON tibia and TD tibia. (G and H) Relative fluorescence intensity of Cant1 and β-Catenin in ROI of CON tibia and TD tibia.

    Journal: Research

    Article Title: Dysregulation of the Cant1/β-Catenin/TCF4–CHSY1 Axis Underpins Impaired ECM Biosynthesis in Skeletal Disorders

    doi: 10.34133/research.1227

    Figure Lengend Snippet: Mechanism of ECM biosynthesis disorders and abnormal Wnt/β-Catenin signaling pathway transduction in TD models. (A) mRNA levels of ECM biosynthesis factors and canonical Wnt/β-Catenin signaling pathway components. (B) mRNA levels of Cant1. (C) Quantitative analysis of GAG content. (D) Protein blots. (E) Protein levels of ACAN, Col2α1, β-Catenin, and Cant1. (F) Immunofluorescence digital images of CON tibia and TD tibia. (G and H) Relative fluorescence intensity of Cant1 and β-Catenin in ROI of CON tibia and TD tibia.

    Article Snippet: Protein bands were blocked in tris–borate–sodium Tween-20 (TBST) with 5% skim milk and then incubated with primary antibodies against Cant1 (no. A6341, ABclonal, China), β-Catenin (no. 66379-1-Ig, Proteintech, China), phospho-β-Catenin (no. AP1076, ABclonal, China), Col2α1 (no. A1520, ABclonal, China), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (no. 60004-1-1g, Proteintech, China), and ACAN (no. A12045, ABclonal, China).

    Techniques: Transduction, Immunofluorescence, Fluorescence

    Regulation of Cant1 on ECM biosynthesis and canonical Wnt/β-Catenin signaling pathway activity in chondrocytes. (A) Illustration of Cant1 inhibition/overexpression and canonical Wnt/β-Catenin signaling pathway activation/inhibition in chondrocytes. (B) mRNA levels of Cant1. (C) mRNA levels of ECM biosynthesis factors. (D) mRNA levels of Wnt/β-Catenin signaling pathway components. (E) Protein blots. (F) Protein levels of ACAN, Col2α1, Cant1, and β-Catenin. (G) Quantitative analysis of GAG content. (H) Wnt/β-Catenin transcriptional activity (TOP/FOPFLASH ratio). (I and J) Relative β-Catenin fluorescence intensity in CON and TD chondrocytes.

    Journal: Research

    Article Title: Dysregulation of the Cant1/β-Catenin/TCF4–CHSY1 Axis Underpins Impaired ECM Biosynthesis in Skeletal Disorders

    doi: 10.34133/research.1227

    Figure Lengend Snippet: Regulation of Cant1 on ECM biosynthesis and canonical Wnt/β-Catenin signaling pathway activity in chondrocytes. (A) Illustration of Cant1 inhibition/overexpression and canonical Wnt/β-Catenin signaling pathway activation/inhibition in chondrocytes. (B) mRNA levels of Cant1. (C) mRNA levels of ECM biosynthesis factors. (D) mRNA levels of Wnt/β-Catenin signaling pathway components. (E) Protein blots. (F) Protein levels of ACAN, Col2α1, Cant1, and β-Catenin. (G) Quantitative analysis of GAG content. (H) Wnt/β-Catenin transcriptional activity (TOP/FOPFLASH ratio). (I and J) Relative β-Catenin fluorescence intensity in CON and TD chondrocytes.

    Article Snippet: Protein bands were blocked in tris–borate–sodium Tween-20 (TBST) with 5% skim milk and then incubated with primary antibodies against Cant1 (no. A6341, ABclonal, China), β-Catenin (no. 66379-1-Ig, Proteintech, China), phospho-β-Catenin (no. AP1076, ABclonal, China), Col2α1 (no. A1520, ABclonal, China), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (no. 60004-1-1g, Proteintech, China), and ACAN (no. A12045, ABclonal, China).

    Techniques: Activity Assay, Inhibition, Over Expression, Activation Assay, Fluorescence

    The inhibition of the canonical Wnt/β-Catenin signaling pathway down-regulates ECM biosynthesis promoted by Cant1 overexpression. (A) Illustration of the cell model for Cant1 overexpression combined with activation or inhibition of the canonical Wnt/β-Catenin signaling pathway. (B) Quantitative analysis of GAG content. (C) mRNA levels of ECM biosynthesis factors. (D) mRNA levels of Cant1. (E) Protein blots. (F) Protein levels of ACAN, Col2α1, Cant1, and β-Catenin. (G) Wnt/β-Catenin transcriptional activity (TOP/FOPFLASH ratio).

    Journal: Research

    Article Title: Dysregulation of the Cant1/β-Catenin/TCF4–CHSY1 Axis Underpins Impaired ECM Biosynthesis in Skeletal Disorders

    doi: 10.34133/research.1227

    Figure Lengend Snippet: The inhibition of the canonical Wnt/β-Catenin signaling pathway down-regulates ECM biosynthesis promoted by Cant1 overexpression. (A) Illustration of the cell model for Cant1 overexpression combined with activation or inhibition of the canonical Wnt/β-Catenin signaling pathway. (B) Quantitative analysis of GAG content. (C) mRNA levels of ECM biosynthesis factors. (D) mRNA levels of Cant1. (E) Protein blots. (F) Protein levels of ACAN, Col2α1, Cant1, and β-Catenin. (G) Wnt/β-Catenin transcriptional activity (TOP/FOPFLASH ratio).

    Article Snippet: Protein bands were blocked in tris–borate–sodium Tween-20 (TBST) with 5% skim milk and then incubated with primary antibodies against Cant1 (no. A6341, ABclonal, China), β-Catenin (no. 66379-1-Ig, Proteintech, China), phospho-β-Catenin (no. AP1076, ABclonal, China), Col2α1 (no. A1520, ABclonal, China), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (no. 60004-1-1g, Proteintech, China), and ACAN (no. A12045, ABclonal, China).

    Techniques: Inhibition, Over Expression, Activation Assay, Activity Assay

    Analysis of the interaction between Cant1 and β-Catenin. (A) Digital immunofluorescence images of CON tibia and TD tibia. (B) Plot profile of Cant1 and β-Catenin fluorescence intensity in ROI of RZ, PZ, and HZ. (C) Colocalization analysis of Cant1 and β-Catenin fluorescence intensity in ROI of RZ, PZ, and HZ. (D) Digital immunofluorescence images of chondrocytes. (E) Plot profile of Cant1 and β-Catenin fluorescence intensity in ROI of chondrocytes. (F) Colocalization analysis of Cant1 and β-Catenin fluorescence intensity in ROI of chondrocytes. (G) Illustration of cell model construction for Co-IP assay. (H) Co-IP of Cant1 and β-Catenin proteins in chondrocytes. (I) Protein levels of Cant1 and β-Catenin.

    Journal: Research

    Article Title: Dysregulation of the Cant1/β-Catenin/TCF4–CHSY1 Axis Underpins Impaired ECM Biosynthesis in Skeletal Disorders

    doi: 10.34133/research.1227

    Figure Lengend Snippet: Analysis of the interaction between Cant1 and β-Catenin. (A) Digital immunofluorescence images of CON tibia and TD tibia. (B) Plot profile of Cant1 and β-Catenin fluorescence intensity in ROI of RZ, PZ, and HZ. (C) Colocalization analysis of Cant1 and β-Catenin fluorescence intensity in ROI of RZ, PZ, and HZ. (D) Digital immunofluorescence images of chondrocytes. (E) Plot profile of Cant1 and β-Catenin fluorescence intensity in ROI of chondrocytes. (F) Colocalization analysis of Cant1 and β-Catenin fluorescence intensity in ROI of chondrocytes. (G) Illustration of cell model construction for Co-IP assay. (H) Co-IP of Cant1 and β-Catenin proteins in chondrocytes. (I) Protein levels of Cant1 and β-Catenin.

    Article Snippet: Protein bands were blocked in tris–borate–sodium Tween-20 (TBST) with 5% skim milk and then incubated with primary antibodies against Cant1 (no. A6341, ABclonal, China), β-Catenin (no. 66379-1-Ig, Proteintech, China), phospho-β-Catenin (no. AP1076, ABclonal, China), Col2α1 (no. A1520, ABclonal, China), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (no. 60004-1-1g, Proteintech, China), and ACAN (no. A12045, ABclonal, China).

    Techniques: Immunofluorescence, Fluorescence, Co-Immunoprecipitation Assay

    Canonical Wnt/β-Catenin signaling pathway transcription factor TCF4 transcriptionally activates CHSY1 expression in chondrocytes. (A and B) Correlation analysis of ECM biosynthesis factors with key factor expression levels. (C) Illustration of the CHSY1 promoter luciferase reporter constructs used in the study. (D) Luciferase activity of the full-length and truncated CHSY1 promoter. (E and F) Luciferase activity of the CHSY1 promoter in cells transfected with a basic plasmid or a TCF4 overexpression plasmid. (G) Potential TCF4-binding sites in the CHSY1 promoter sequence. (H) Luciferase activity of the CHSY1 promoter (WT, MUT1, MUT2, and MUT3) in cells.

    Journal: Research

    Article Title: Dysregulation of the Cant1/β-Catenin/TCF4–CHSY1 Axis Underpins Impaired ECM Biosynthesis in Skeletal Disorders

    doi: 10.34133/research.1227

    Figure Lengend Snippet: Canonical Wnt/β-Catenin signaling pathway transcription factor TCF4 transcriptionally activates CHSY1 expression in chondrocytes. (A and B) Correlation analysis of ECM biosynthesis factors with key factor expression levels. (C) Illustration of the CHSY1 promoter luciferase reporter constructs used in the study. (D) Luciferase activity of the full-length and truncated CHSY1 promoter. (E and F) Luciferase activity of the CHSY1 promoter in cells transfected with a basic plasmid or a TCF4 overexpression plasmid. (G) Potential TCF4-binding sites in the CHSY1 promoter sequence. (H) Luciferase activity of the CHSY1 promoter (WT, MUT1, MUT2, and MUT3) in cells.

    Article Snippet: Protein bands were blocked in tris–borate–sodium Tween-20 (TBST) with 5% skim milk and then incubated with primary antibodies against Cant1 (no. A6341, ABclonal, China), β-Catenin (no. 66379-1-Ig, Proteintech, China), phospho-β-Catenin (no. AP1076, ABclonal, China), Col2α1 (no. A1520, ABclonal, China), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (no. 60004-1-1g, Proteintech, China), and ACAN (no. A12045, ABclonal, China).

    Techniques: Expressing, Luciferase, Construct, Activity Assay, Transfection, Plasmid Preparation, Over Expression, Binding Assay, Sequencing