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pa1957  (Boster Bio)


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    Structured Review

    Boster Bio pa1957

    Pa1957, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pa1957/Anti-Tight+junction+protein+ZO-2+TJP2+Antibody+Picoband/pmc10809936-25-7-5
    Average 93 stars, based on 2 article reviews
    pa1957 - by Bioz Stars, 2026-09
    93/100 stars

    Images

    1) Product Images from "p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP"

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP

    Journal: Cell reports

    doi: 10.1016/j.celrep.2023.113486


    Figure Legend Snippet:

    Techniques Used:

    KEY RESOURCES TABLE
    Figure Legend Snippet: KEY RESOURCES TABLE

    Techniques Used: Virus, Recombinant, cDNA Synthesis, RNA Sequencing, Knockdown, Plasmid Preparation, shRNA, Software

    Related Articles

    Virus:

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP
    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.


    Recombinant:

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP
    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.


    cDNA Synthesis:

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP
    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.


    RNA Sequencing:

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP
    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.


    Knockdown:

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP
    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.


    Plasmid Preparation:

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP
    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.


    shRNA:

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP
    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.


    Software:

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP
    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.




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    93
    Boster Bio pa1957

    Pa1957, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pa1957/Anti-Tight+junction+protein+ZO-2+TJP2+Antibody+Picoband/pmc10809936-25-7-5
    Average 93 stars, based on 1 article reviews
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    Boster Bio rabbit polyclonal
    (A) Validation of the interaction between p190A and ZO-1/2 detected by mass spectrometry. Confluent cultures of control cells and H661 expressing Myc-tagged p190A cells were lysed in gold lysis buffer and processed for immunoprecipitation (IP) using mouse monoclonal 9E10 anti-Myc epitope antibody immobilized on agarose beads followed by western blotting (WB) to detect p190A, ZO-1, ZO-2, and ERK1/2. (B) Confluent cultures of MDA-MB-231 cells were processed for immunoprecipitation with rabbit <t>polyclonal</t> anti-p190A antibody or without antibody followed by protein A/G Sepharose beads. Next, p190A, RasGAP, ZO-1, ZO-2, and ERK1/2 were detected in immunoprecipitates and lysates by western blotting. (C) ZO-1 and ZO-2 bind p190A in a RasGAP-dependent manner. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A(WT) ± RASA1-KO or p190A(Y2F) were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-1, ZO-2, and ERK1/2. (D) Binding of p190A to RasGAP is independent of ZO-2. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A ± TJP2-KO were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-2, and ERK1/2. (E and F) The U5GuK and ABR domains of ZO-1 are necessary for the interaction with p190A. (E) Cartoon depicting domain structure of zonula occludens proteins ZO-1, ZO-2, and ZO-3. The regions encoded by ZO-1 and ZO-2 sequences targeted by sgRNAs are marked. (F) MDCK II cells depleted of endogenous ZO-1 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-1 deletion mutant missing the ABR, U5GuK, or PDZ1 domains were processed for immunoprecipitation with polyclonal rabbit anti-p190A antibody followed by western blotting to detect GFP, p190A, and ERK1/2. (G) Interaction of ZO-2 with p190A in MDCK cells. MDCK II cells depleted of endogenous ZO-2 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-2 were processed for immunoprecipitation with polyclonal p190A antibody followed by western blotting to detect GFP and p190A. (H) Immunofluorescence to detect p190A (red) in MDCK II cell depleted of ZO-1 or ZO-2 expressing either EGFP alone or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-2 as indicated. Scale bars represent 10 μm. (I) 5× magnification of the boxed areas in (H).
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    (A) Validation of the interaction between p190A and ZO-1/2 detected by mass spectrometry. Confluent cultures of control cells and H661 expressing Myc-tagged p190A cells were lysed in gold lysis buffer and processed for immunoprecipitation (IP) using mouse monoclonal 9E10 anti-Myc epitope antibody immobilized on agarose beads followed by western blotting (WB) to detect p190A, ZO-1, ZO-2, and ERK1/2. (B) Confluent cultures of MDA-MB-231 cells were processed for immunoprecipitation with rabbit <t>polyclonal</t> anti-p190A antibody or without antibody followed by protein A/G Sepharose beads. Next, p190A, RasGAP, ZO-1, ZO-2, and ERK1/2 were detected in immunoprecipitates and lysates by western blotting. (C) ZO-1 and ZO-2 bind p190A in a RasGAP-dependent manner. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A(WT) ± RASA1-KO or p190A(Y2F) were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-1, ZO-2, and ERK1/2. (D) Binding of p190A to RasGAP is independent of ZO-2. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A ± TJP2-KO were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-2, and ERK1/2. (E and F) The U5GuK and ABR domains of ZO-1 are necessary for the interaction with p190A. (E) Cartoon depicting domain structure of zonula occludens proteins ZO-1, ZO-2, and ZO-3. The regions encoded by ZO-1 and ZO-2 sequences targeted by sgRNAs are marked. (F) MDCK II cells depleted of endogenous ZO-1 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-1 deletion mutant missing the ABR, U5GuK, or PDZ1 domains were processed for immunoprecipitation with polyclonal rabbit anti-p190A antibody followed by western blotting to detect GFP, p190A, and ERK1/2. (G) Interaction of ZO-2 with p190A in MDCK cells. MDCK II cells depleted of endogenous ZO-2 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-2 were processed for immunoprecipitation with polyclonal p190A antibody followed by western blotting to detect GFP and p190A. (H) Immunofluorescence to detect p190A (red) in MDCK II cell depleted of ZO-1 or ZO-2 expressing either EGFP alone or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-2 as indicated. Scale bars represent 10 μm. (I) 5× magnification of the boxed areas in (H).
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    (A) Validation of the interaction between p190A and ZO-1/2 detected by mass spectrometry. Confluent cultures of control cells and H661 expressing Myc-tagged p190A cells were lysed in gold lysis buffer and processed for immunoprecipitation (IP) using mouse monoclonal 9E10 anti-Myc epitope antibody immobilized on agarose beads followed by western blotting (WB) to detect p190A, ZO-1, ZO-2, and ERK1/2. (B) Confluent cultures of MDA-MB-231 cells were processed for immunoprecipitation with rabbit <t>polyclonal</t> anti-p190A antibody or without antibody followed by protein A/G Sepharose beads. Next, p190A, RasGAP, ZO-1, ZO-2, and ERK1/2 were detected in immunoprecipitates and lysates by western blotting. (C) ZO-1 and ZO-2 bind p190A in a RasGAP-dependent manner. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A(WT) ± RASA1-KO or p190A(Y2F) were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-1, ZO-2, and ERK1/2. (D) Binding of p190A to RasGAP is independent of ZO-2. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A ± TJP2-KO were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-2, and ERK1/2. (E and F) The U5GuK and ABR domains of ZO-1 are necessary for the interaction with p190A. (E) Cartoon depicting domain structure of zonula occludens proteins ZO-1, ZO-2, and ZO-3. The regions encoded by ZO-1 and ZO-2 sequences targeted by sgRNAs are marked. (F) MDCK II cells depleted of endogenous ZO-1 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-1 deletion mutant missing the ABR, U5GuK, or PDZ1 domains were processed for immunoprecipitation with polyclonal rabbit anti-p190A antibody followed by western blotting to detect GFP, p190A, and ERK1/2. (G) Interaction of ZO-2 with p190A in MDCK cells. MDCK II cells depleted of endogenous ZO-2 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-2 were processed for immunoprecipitation with polyclonal p190A antibody followed by western blotting to detect GFP and p190A. (H) Immunofluorescence to detect p190A (red) in MDCK II cell depleted of ZO-1 or ZO-2 expressing either EGFP alone or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-2 as indicated. Scale bars represent 10 μm. (I) 5× magnification of the boxed areas in (H).
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    (A) Validation of the interaction between p190A and ZO-1/2 detected by mass spectrometry. Confluent cultures of control cells and H661 expressing Myc-tagged p190A cells were lysed in gold lysis buffer and processed for immunoprecipitation (IP) using mouse monoclonal 9E10 anti-Myc epitope antibody immobilized on agarose beads followed by western blotting (WB) to detect p190A, ZO-1, ZO-2, and ERK1/2. (B) Confluent cultures of MDA-MB-231 cells were processed for immunoprecipitation with rabbit <t>polyclonal</t> anti-p190A antibody or without antibody followed by protein A/G Sepharose beads. Next, p190A, RasGAP, ZO-1, ZO-2, and ERK1/2 were detected in immunoprecipitates and lysates by western blotting. (C) ZO-1 and ZO-2 bind p190A in a RasGAP-dependent manner. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A(WT) ± RASA1-KO or p190A(Y2F) were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-1, ZO-2, and ERK1/2. (D) Binding of p190A to RasGAP is independent of ZO-2. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A ± TJP2-KO were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-2, and ERK1/2. (E and F) The U5GuK and ABR domains of ZO-1 are necessary for the interaction with p190A. (E) Cartoon depicting domain structure of zonula occludens proteins ZO-1, ZO-2, and ZO-3. The regions encoded by ZO-1 and ZO-2 sequences targeted by sgRNAs are marked. (F) MDCK II cells depleted of endogenous ZO-1 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-1 deletion mutant missing the ABR, U5GuK, or PDZ1 domains were processed for immunoprecipitation with polyclonal rabbit anti-p190A antibody followed by western blotting to detect GFP, p190A, and ERK1/2. (G) Interaction of ZO-2 with p190A in MDCK cells. MDCK II cells depleted of endogenous ZO-2 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-2 were processed for immunoprecipitation with polyclonal p190A antibody followed by western blotting to detect GFP and p190A. (H) Immunofluorescence to detect p190A (red) in MDCK II cell depleted of ZO-1 or ZO-2 expressing either EGFP alone or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-2 as indicated. Scale bars represent 10 μm. (I) 5× magnification of the boxed areas in (H).
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    (A) Validation of the interaction between p190A and ZO-1/2 detected by mass spectrometry. Confluent cultures of control cells and H661 expressing Myc-tagged p190A cells were lysed in gold lysis buffer and processed for immunoprecipitation (IP) using mouse monoclonal 9E10 anti-Myc epitope antibody immobilized on agarose beads followed by western blotting (WB) to detect p190A, ZO-1, ZO-2, and ERK1/2. (B) Confluent cultures of MDA-MB-231 cells were processed for immunoprecipitation with rabbit <t>polyclonal</t> anti-p190A antibody or without antibody followed by protein A/G Sepharose beads. Next, p190A, RasGAP, ZO-1, ZO-2, and ERK1/2 were detected in immunoprecipitates and lysates by western blotting. (C) ZO-1 and ZO-2 bind p190A in a RasGAP-dependent manner. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A(WT) ± RASA1-KO or p190A(Y2F) were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-1, ZO-2, and ERK1/2. (D) Binding of p190A to RasGAP is independent of ZO-2. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A ± TJP2-KO were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-2, and ERK1/2. (E and F) The U5GuK and ABR domains of ZO-1 are necessary for the interaction with p190A. (E) Cartoon depicting domain structure of zonula occludens proteins ZO-1, ZO-2, and ZO-3. The regions encoded by ZO-1 and ZO-2 sequences targeted by sgRNAs are marked. (F) MDCK II cells depleted of endogenous ZO-1 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-1 deletion mutant missing the ABR, U5GuK, or PDZ1 domains were processed for immunoprecipitation with polyclonal rabbit anti-p190A antibody followed by western blotting to detect GFP, p190A, and ERK1/2. (G) Interaction of ZO-2 with p190A in MDCK cells. MDCK II cells depleted of endogenous ZO-2 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-2 were processed for immunoprecipitation with polyclonal p190A antibody followed by western blotting to detect GFP and p190A. (H) Immunofluorescence to detect p190A (red) in MDCK II cell depleted of ZO-1 or ZO-2 expressing either EGFP alone or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-2 as indicated. Scale bars represent 10 μm. (I) 5× magnification of the boxed areas in (H).
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    Image Search Results


    Journal: Cell reports

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP

    doi: 10.1016/j.celrep.2023.113486

    Figure Lengend Snippet:

    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.

    Techniques:

    KEY RESOURCES TABLE

    Journal: Cell reports

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP

    doi: 10.1016/j.celrep.2023.113486

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.

    Techniques: Virus, Recombinant, cDNA Synthesis, RNA Sequencing, Knockdown, Plasmid Preparation, shRNA, Software

    (A) Validation of the interaction between p190A and ZO-1/2 detected by mass spectrometry. Confluent cultures of control cells and H661 expressing Myc-tagged p190A cells were lysed in gold lysis buffer and processed for immunoprecipitation (IP) using mouse monoclonal 9E10 anti-Myc epitope antibody immobilized on agarose beads followed by western blotting (WB) to detect p190A, ZO-1, ZO-2, and ERK1/2. (B) Confluent cultures of MDA-MB-231 cells were processed for immunoprecipitation with rabbit polyclonal anti-p190A antibody or without antibody followed by protein A/G Sepharose beads. Next, p190A, RasGAP, ZO-1, ZO-2, and ERK1/2 were detected in immunoprecipitates and lysates by western blotting. (C) ZO-1 and ZO-2 bind p190A in a RasGAP-dependent manner. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A(WT) ± RASA1-KO or p190A(Y2F) were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-1, ZO-2, and ERK1/2. (D) Binding of p190A to RasGAP is independent of ZO-2. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A ± TJP2-KO were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-2, and ERK1/2. (E and F) The U5GuK and ABR domains of ZO-1 are necessary for the interaction with p190A. (E) Cartoon depicting domain structure of zonula occludens proteins ZO-1, ZO-2, and ZO-3. The regions encoded by ZO-1 and ZO-2 sequences targeted by sgRNAs are marked. (F) MDCK II cells depleted of endogenous ZO-1 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-1 deletion mutant missing the ABR, U5GuK, or PDZ1 domains were processed for immunoprecipitation with polyclonal rabbit anti-p190A antibody followed by western blotting to detect GFP, p190A, and ERK1/2. (G) Interaction of ZO-2 with p190A in MDCK cells. MDCK II cells depleted of endogenous ZO-2 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-2 were processed for immunoprecipitation with polyclonal p190A antibody followed by western blotting to detect GFP and p190A. (H) Immunofluorescence to detect p190A (red) in MDCK II cell depleted of ZO-1 or ZO-2 expressing either EGFP alone or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-2 as indicated. Scale bars represent 10 μm. (I) 5× magnification of the boxed areas in (H).

    Journal: Cell reports

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP

    doi: 10.1016/j.celrep.2023.113486

    Figure Lengend Snippet: (A) Validation of the interaction between p190A and ZO-1/2 detected by mass spectrometry. Confluent cultures of control cells and H661 expressing Myc-tagged p190A cells were lysed in gold lysis buffer and processed for immunoprecipitation (IP) using mouse monoclonal 9E10 anti-Myc epitope antibody immobilized on agarose beads followed by western blotting (WB) to detect p190A, ZO-1, ZO-2, and ERK1/2. (B) Confluent cultures of MDA-MB-231 cells were processed for immunoprecipitation with rabbit polyclonal anti-p190A antibody or without antibody followed by protein A/G Sepharose beads. Next, p190A, RasGAP, ZO-1, ZO-2, and ERK1/2 were detected in immunoprecipitates and lysates by western blotting. (C) ZO-1 and ZO-2 bind p190A in a RasGAP-dependent manner. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A(WT) ± RASA1-KO or p190A(Y2F) were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-1, ZO-2, and ERK1/2. (D) Binding of p190A to RasGAP is independent of ZO-2. Confluent cultures of control cells or H661 cells expressing Myc-tagged p190A ± TJP2-KO were processed for immunoprecipitation with 9E10 antibody followed by western blotting to detect p190A, RasGAP, ZO-2, and ERK1/2. (E and F) The U5GuK and ABR domains of ZO-1 are necessary for the interaction with p190A. (E) Cartoon depicting domain structure of zonula occludens proteins ZO-1, ZO-2, and ZO-3. The regions encoded by ZO-1 and ZO-2 sequences targeted by sgRNAs are marked. (F) MDCK II cells depleted of endogenous ZO-1 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-1 deletion mutant missing the ABR, U5GuK, or PDZ1 domains were processed for immunoprecipitation with polyclonal rabbit anti-p190A antibody followed by western blotting to detect GFP, p190A, and ERK1/2. (G) Interaction of ZO-2 with p190A in MDCK cells. MDCK II cells depleted of endogenous ZO-2 and expressing exogenous EGFP only or knockdown-resistant EGFP-tagged full-length ZO-2 were processed for immunoprecipitation with polyclonal p190A antibody followed by western blotting to detect GFP and p190A. (H) Immunofluorescence to detect p190A (red) in MDCK II cell depleted of ZO-1 or ZO-2 expressing either EGFP alone or knockdown-resistant EGFP-tagged full-length ZO-1 or ZO-2 as indicated. Scale bars represent 10 μm. (I) 5× magnification of the boxed areas in (H).

    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.

    Techniques: Biomarker Discovery, Mass Spectrometry, Control, Expressing, Lysis, Immunoprecipitation, Western Blot, Binding Assay, Knockdown, Mutagenesis, Immunofluorescence

    Journal: Cell reports

    Article Title: p120 RasGAP and ZO-2 are essential for Hippo signaling and tumor-suppressor function mediated by p190A RhoGAP

    doi: 10.1016/j.celrep.2023.113486

    Figure Lengend Snippet:

    Article Snippet: ZO-2 , rabbit polyclonal , Boster , PA1957.

    Techniques: