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sin3a  (Proteintech)


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    Structured Review

    Proteintech sin3a
    In the presence of RNA, binding to certain proteins, such as TBLR1 and <t>Sin3a,</t> is limited, however there are other unknown protein complexes to which MeCP2 interacts through, perhaps, scaffolding RNAs that may bind at the RBD, at some other region of the protein, or both. When RNA is degraded, some large complexes disassociate from MeCP2, as indicated from sucrose density ultracentrifugation, but MeCP2’s total protein interactome increases through interactions at the RBD, such as to TBLR1, as shown by IP data. When UV crosslinking is applied to create a covalent link between RNA bound to MeCP2, RNase treatment does not result in the increased interactome or TBLR1 binding as before, but instead obstructs TBLR1 binding, allowing other proteins, like Sin3a, to bind MeCP2 at a domain outside the RBD.
    Sin3a, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sin3a/product/Proteintech
    Average 93 stars, based on 10 article reviews
    sin3a - by Bioz Stars, 2026-03
    93/100 stars

    Images

    1) Product Images from "MeCP2 NID interaction with RNA: Implications for Rett Syndrome-Relevant Protein Regulation"

    Article Title: MeCP2 NID interaction with RNA: Implications for Rett Syndrome-Relevant Protein Regulation

    Journal: bioRxiv

    doi: 10.1101/2025.11.19.689340

    In the presence of RNA, binding to certain proteins, such as TBLR1 and Sin3a, is limited, however there are other unknown protein complexes to which MeCP2 interacts through, perhaps, scaffolding RNAs that may bind at the RBD, at some other region of the protein, or both. When RNA is degraded, some large complexes disassociate from MeCP2, as indicated from sucrose density ultracentrifugation, but MeCP2’s total protein interactome increases through interactions at the RBD, such as to TBLR1, as shown by IP data. When UV crosslinking is applied to create a covalent link between RNA bound to MeCP2, RNase treatment does not result in the increased interactome or TBLR1 binding as before, but instead obstructs TBLR1 binding, allowing other proteins, like Sin3a, to bind MeCP2 at a domain outside the RBD.
    Figure Legend Snippet: In the presence of RNA, binding to certain proteins, such as TBLR1 and Sin3a, is limited, however there are other unknown protein complexes to which MeCP2 interacts through, perhaps, scaffolding RNAs that may bind at the RBD, at some other region of the protein, or both. When RNA is degraded, some large complexes disassociate from MeCP2, as indicated from sucrose density ultracentrifugation, but MeCP2’s total protein interactome increases through interactions at the RBD, such as to TBLR1, as shown by IP data. When UV crosslinking is applied to create a covalent link between RNA bound to MeCP2, RNase treatment does not result in the increased interactome or TBLR1 binding as before, but instead obstructs TBLR1 binding, allowing other proteins, like Sin3a, to bind MeCP2 at a domain outside the RBD.

    Techniques Used: RNA Binding Assay, Scaffolding, Binding Assay



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    Single-cell data analysis of <t>SIN3A</t> in AR. ( a – d ) UMAP clustering results: ( a ) “pre” on the right signifies the period prior to SLIT treatment, while “post” denotes the period following SLIT treatment; ( b ) illustrates the clustering of various samples before and after de-batching; ( c ) on the right, the four principal cell types identified through annotation are: CD4+ cytotoxic T cells, CD4+ regulatory T cells, CD4+ naïve T cells, and CD4+ helper T cells17; ( d ) depicts SIN3A expression across each immune cell type. ( e ) Differential expression of the SIN3A gene across various immune cell types in allergic rhinitis patients prior to sublingual immunotherapy treatment. ( f ) Differential expression of the SIN3A gene in various immune cell types in allergic rhinitis patients following sublingual immunotherapy treatment.
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    Image Search Results


    In the presence of RNA, binding to certain proteins, such as TBLR1 and Sin3a, is limited, however there are other unknown protein complexes to which MeCP2 interacts through, perhaps, scaffolding RNAs that may bind at the RBD, at some other region of the protein, or both. When RNA is degraded, some large complexes disassociate from MeCP2, as indicated from sucrose density ultracentrifugation, but MeCP2’s total protein interactome increases through interactions at the RBD, such as to TBLR1, as shown by IP data. When UV crosslinking is applied to create a covalent link between RNA bound to MeCP2, RNase treatment does not result in the increased interactome or TBLR1 binding as before, but instead obstructs TBLR1 binding, allowing other proteins, like Sin3a, to bind MeCP2 at a domain outside the RBD.

    Journal: bioRxiv

    Article Title: MeCP2 NID interaction with RNA: Implications for Rett Syndrome-Relevant Protein Regulation

    doi: 10.1101/2025.11.19.689340

    Figure Lengend Snippet: In the presence of RNA, binding to certain proteins, such as TBLR1 and Sin3a, is limited, however there are other unknown protein complexes to which MeCP2 interacts through, perhaps, scaffolding RNAs that may bind at the RBD, at some other region of the protein, or both. When RNA is degraded, some large complexes disassociate from MeCP2, as indicated from sucrose density ultracentrifugation, but MeCP2’s total protein interactome increases through interactions at the RBD, such as to TBLR1, as shown by IP data. When UV crosslinking is applied to create a covalent link between RNA bound to MeCP2, RNase treatment does not result in the increased interactome or TBLR1 binding as before, but instead obstructs TBLR1 binding, allowing other proteins, like Sin3a, to bind MeCP2 at a domain outside the RBD.

    Article Snippet: Primary antibodies used were: MeCP2 (M9317, Sigma®, St. Louis, MO, USA), H4 (rabbit serum produced in-house), Sin3a (ProteinTech 14638-1-AP), TBLR1 (Bethyl, A300-408A), HDAC1 (Santa Cruz Biotechnology, sc-81598).

    Techniques: RNA Binding Assay, Scaffolding, Binding Assay

    Single-cell data analysis of SIN3A in AR. ( a – d ) UMAP clustering results: ( a ) “pre” on the right signifies the period prior to SLIT treatment, while “post” denotes the period following SLIT treatment; ( b ) illustrates the clustering of various samples before and after de-batching; ( c ) on the right, the four principal cell types identified through annotation are: CD4+ cytotoxic T cells, CD4+ regulatory T cells, CD4+ naïve T cells, and CD4+ helper T cells17; ( d ) depicts SIN3A expression across each immune cell type. ( e ) Differential expression of the SIN3A gene across various immune cell types in allergic rhinitis patients prior to sublingual immunotherapy treatment. ( f ) Differential expression of the SIN3A gene in various immune cell types in allergic rhinitis patients following sublingual immunotherapy treatment.

    Journal: Journal of Inflammation Research

    Article Title: Identification of SIN3A as a Promising Epigenetic Target Against Allergic Rhinitis

    doi: 10.2147/JIR.S535690

    Figure Lengend Snippet: Single-cell data analysis of SIN3A in AR. ( a – d ) UMAP clustering results: ( a ) “pre” on the right signifies the period prior to SLIT treatment, while “post” denotes the period following SLIT treatment; ( b ) illustrates the clustering of various samples before and after de-batching; ( c ) on the right, the four principal cell types identified through annotation are: CD4+ cytotoxic T cells, CD4+ regulatory T cells, CD4+ naïve T cells, and CD4+ helper T cells17; ( d ) depicts SIN3A expression across each immune cell type. ( e ) Differential expression of the SIN3A gene across various immune cell types in allergic rhinitis patients prior to sublingual immunotherapy treatment. ( f ) Differential expression of the SIN3A gene in various immune cell types in allergic rhinitis patients following sublingual immunotherapy treatment.

    Article Snippet: The Anti- SIN3A antibody was acquired from Proteintech (USA).

    Techniques: Expressing, Quantitative Proteomics

    Correlation of SIN3A with common immune checkpoints and human leukocyte antigens. ( A ) Correlation of SIN3A with common immune checkpoints; ( B ) Correlation of SIN3A with common immune checkpoints.

    Journal: Journal of Inflammation Research

    Article Title: Identification of SIN3A as a Promising Epigenetic Target Against Allergic Rhinitis

    doi: 10.2147/JIR.S535690

    Figure Lengend Snippet: Correlation of SIN3A with common immune checkpoints and human leukocyte antigens. ( A ) Correlation of SIN3A with common immune checkpoints; ( B ) Correlation of SIN3A with common immune checkpoints.

    Article Snippet: The Anti- SIN3A antibody was acquired from Proteintech (USA).

    Techniques:

    SIN3A is differentially expressed in AR patients.( a and b ) Relative protein expression of SIN3A in AR and controls. ( c ) SIN3A expression in nasal mucosa (immunofluorescence detection 20×; 40×). ( d ) Relative mRNA expression of SIN3A in AR and control. “***” indicates p<0.001.

    Journal: Journal of Inflammation Research

    Article Title: Identification of SIN3A as a Promising Epigenetic Target Against Allergic Rhinitis

    doi: 10.2147/JIR.S535690

    Figure Lengend Snippet: SIN3A is differentially expressed in AR patients.( a and b ) Relative protein expression of SIN3A in AR and controls. ( c ) SIN3A expression in nasal mucosa (immunofluorescence detection 20×; 40×). ( d ) Relative mRNA expression of SIN3A in AR and control. “***” indicates p<0.001.

    Article Snippet: The Anti- SIN3A antibody was acquired from Proteintech (USA).

    Techniques: Expressing, Immunofluorescence, Control

    Functional verification of SIN3A in in vitro cell experiments. ( a and b ) Relative expression levels of IL-25, IL-33 and TSLP proteins in HDM-sensitized nasal mucosal epithelial cells. ( c-f ) Representative flow cytometry plots of IL-17A and Foxp3 expression in naive CD4+T cells co-cultured with nasal mucosal epithelial cells from different treatment groups. Experimental groups were as follows: control group (untreated HNEpCs), HDM group (HDM-sensitized HNEpCs), HDM + si- SIN3A group (HDM-sensitized and SIN3A knockdown HNEpCs), HDM + OE- SIN3A group (HDM-sensitized and SIN3A overexpressed HNEpCs). ( d ) Quantitative analysis of Th17 cell proportions in each group; ( f ) Quantitative analysis of Treg cell proportions in each group.

    Journal: Journal of Inflammation Research

    Article Title: Identification of SIN3A as a Promising Epigenetic Target Against Allergic Rhinitis

    doi: 10.2147/JIR.S535690

    Figure Lengend Snippet: Functional verification of SIN3A in in vitro cell experiments. ( a and b ) Relative expression levels of IL-25, IL-33 and TSLP proteins in HDM-sensitized nasal mucosal epithelial cells. ( c-f ) Representative flow cytometry plots of IL-17A and Foxp3 expression in naive CD4+T cells co-cultured with nasal mucosal epithelial cells from different treatment groups. Experimental groups were as follows: control group (untreated HNEpCs), HDM group (HDM-sensitized HNEpCs), HDM + si- SIN3A group (HDM-sensitized and SIN3A knockdown HNEpCs), HDM + OE- SIN3A group (HDM-sensitized and SIN3A overexpressed HNEpCs). ( d ) Quantitative analysis of Th17 cell proportions in each group; ( f ) Quantitative analysis of Treg cell proportions in each group.

    Article Snippet: The Anti- SIN3A antibody was acquired from Proteintech (USA).

    Techniques: Functional Assay, In Vitro, Expressing, Flow Cytometry, Cell Culture, Control, Knockdown