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anti cd2ap  (Proteintech)


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    Structured Review

    Proteintech anti cd2ap
    Anti Cd2ap, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+cd2ap/Cd2ap+Antibody/bio_rxiv__64898__2026__03__14__711835-411-22-23
    Average 93 stars, based on 22 article reviews
    anti cd2ap - by Bioz Stars, 2026-10
    93/100 stars

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    Related Articles

    other:

    Article Title: Interactome mapping in human excitatory neurons reveals novel risk genes and pathways in Alzheimer’s disease
    Article Snippet: Primary antibodies included anti-SNX9 (Proteintech,15721-1-AP), anti-SNX18 (Proteintech, 21946-1-AP), anti-GFP (Genetex, GTX 628528), anti-AP2A1 (Proteintech, 29887-1-AP), anti-AP2B1 (Proteintech, 15690-1-AP), anti-TOMM40 (Proteintech, 18409-1-AP), and anti-CD2AP (Proteintech, 51046-1-AP).

    Article Title: Interactome mapping in human excitatory neurons reveals novel risk genes and pathways in Alzheimer’s disease
    Article Snippet: Primary antibodies included anti-PICALM (Proteintech, 28554-1-AP), anti-CD2AP (Proteintech, 51046-1-AP), anti-AP2B1 (Proteintech, 15690-1-AP), anti-CLTC (Proteintech, 26523-1-AP), anti-CAPZB (Proteintech, 25043-1-AP), and anti-CAPZA2 (Proteintech, 15948-1-AP).

    Article Title: Microglial CD2AP deficiency exerts protection in an Alzheimer's disease model of amyloidosis.
    Article Snippet: Primary antibodies used were: anti-APP (Millipore, mab348, 1:1000), anti-CD2AP (Proteintech, 51046–1–AP, 1:2000), anti-GAPDH (Abway, ab0038, 1:10000), anti-NeuN (Abcam, ab177487, 1:1000), anti-GFAP (Cell Signaling Technology, 3670S, 1:1000), anti-Iba1 (Wako, 016–20001, 1:1000), anti-βactin (Cell Signaling Technology, 8457S, 1:10000), antiCX3CR1 (Abclonal, a2890, 1:1000), anti-CSF1R (Abcam, ab254357, 1:2000), anti-CD11b (Biolegend, 101202, 1:1000), anti-p-ERK (Cell Signaling Technology, 4370, 1:1000), anti-C1q (Hycult Biotech, HM1096BT, 1:1000), anti-CD93 (Abcam, ab134079), anti-MYC (Cell Signaling Technology, 2276S, 1:2000), anti-HA (Proteintech, 51064–2-AP, 1:2000), and anti-ERK (Cell Signaling Technology, 4695, 1:1000), Secondary antibodies used were: Goat anti-Rabbit IgG (H + L) Secondary Antibody, HRP (Thermo Fisher Scientific, 31460, 1:5000), and Goat antiMouse IgG (H + L) Secondary Antibody, HRP (Thermo Fisher Scientific, 31430, 1:5000).

    Article Title: The Rab GTPase-binding protein EHBP1L1 and its interactors CD2AP/CIN85 negatively regulate the length of primary cilia via actin remodeling
    Article Snippet: The following additional primary antibodies were used: rabbit anti-pericentrin (ATLAS antibodies, #HPA016820); mouse anti-acetylated tubulin and anti-FLAG M2 (Sigma-Aldrich, #T7451 and #F1804); mouse anti-Arl13b (Abcam, #ab136648); rabbit anti-ß-actin, anti-Arl13b, anti-CD2AP, and mouse anti-GAPDH (Proteintech, #20536-1-AP, #17711-1-AP, #51046-1-AP, and #66004-1-Ig); mouse anti-CIN85 and anti-Arp2 (Santa Cruz Biotechnology, #sc-166862 and #sc-166103); rabbit anti-myosin Va (Cell signaling, #3402) and mouse anti-MBP (Developmental Studies Hybridoma Bank).

    Article Title: The Rab GTPase-binding protein EHBP1L1 and its interactors CD2AP/CIN85 negatively regulate the length of primary cilia via actin remodeling.
    Article Snippet: The following additional primary antibodies were used: rabbit anti-pericentrin (ATLAS antibodies, #HPA016820); mouse anti-acetylated tubulin and anti-FLAG M2 (Sigma-Aldrich, #T7451 and #F1804); mouse anti-Arl13b (Abcam, #ab136648); rabbit anti-ß-actin, antiArl13b, anti-CD2AP, and mouse anti-GAPDH (Proteintech, #20536-1-AP, #17711-1-AP, #51046-1-AP, and #66004-1-Ig); mouse anti-CIN85 and anti-Arp2 (Santa Cruz Biotechnology, #sc-166862 and #sc-166103); rabbit anti-myosin Va (Cell signaling, #3402) and mouse anti-MBP (Developmental Studies Hybridoma Bank).

    Article Title: Microglial CD2AP deficiency exerts protection in an Alzheimer’s disease model of amyloidosis
    Article Snippet: Primary antibodies used were: anti-APP (Millipore, mab348, 1:1000), anti-CD2AP (Proteintech, 51046–1–AP, 1:2000), anti-GAPDH (Abway, ab0038, 1:10000), anti-NeuN (Abcam, ab177487, 1:1000), anti-GFAP (Cell Signaling Technology, 3670S, 1:1000), anti-Iba1 (Wako, 016–20001, 1:1000), anti-β-actin (Cell Signaling Technology, 8457S, 1:10000), anti-CX3CR1 (Abclonal, a2890, 1:1000), anti-CSF1R (Abcam, ab254357, 1:2000), anti-CD11b (Biolegend, 101202, 1:1000), anti-p-ERK (Cell Signaling Technology, 4370, 1:1000), anti-C1q (Hycult Biotech, HM1096BT, 1:1000), anti-CD93 (Abcam, ab134079), anti-MYC (Cell Signaling Technology, 2276S, 1:2000), anti-HA (Proteintech, 51064–2-AP, 1:2000), and anti-ERK (Cell Signaling Technology, 4695, 1:1000), Secondary antibodies used were: Goat anti-Rabbit IgG (H + L) Secondary Antibody, HRP (Thermo Fisher Scientific, 31460, 1:5000), and Goat anti-Mouse IgG (H + L) Secondary Antibody, HRP (Thermo Fisher Scientific, 31430, 1:5000).

    Fluorescence:

    Article Title: CD2AP is Co-Expressed with Tropomyosin-Related Kinase A and Ras-Related Protein Rab-5A in Cholinergic Neurons of the Murine Basal Forebrain
    Article Snippet: Finally, slides were washed 5 times for 5 minutes with washing buffer (0.3% Triton X-100 in PBS) before mounting with Fluoroshield Mounting Medium with DAPI (Abcam, Cat# ab104139) using 1.5 thickness coverslips. .. The following primary antibodies were used: Anti-Cd2ap (Proteintech, Cat# 51046-1-AP, RRID:AB_2879436); anti-TrkA (R&D, Cat# AF1056, RRID:AB_2283049); anti-choline acetyltransferase (ChAT; Sigma-Aldrich, Cat# AB144P, RRID:AB_2079751); anti-green fluorescence protein (GFP; Aves Labs, Cat# GFP-1020, RRID:AB_10000240); and anti-Rab5 (Cell Signaling Technology, Cat# 46449, RRID:AB_2799303). ..

    Incubation:

    Article Title: Transforming growth factor-β1-induced podocyte injury is associated with increased microRNA-155 expression, enhanced inflammatory responses and MAPK pathway activation.
    Article Snippet: .. Subsequently, the membranes were incubated with the antibodies, including rabbit anti‐CD2AP (cat. no. 51046‐1‐AP; ProteinTech Group, Inc.) at 1:500 dilution; synaptopodin (cat. no. 21064‐1‐AP; ProteinTech Group, Inc.) at 1:500 dilution; CD2AP (cat. no. 51046‐1‐AP; ProteinTech Group, Inc.) at 1:500 dilution; phosphorylated (p)‐p38 [Thr180/Tyr182 (clone D3F9); cat. no. 4511; Cell Signaling Technology, Inc. (CST)] at 1:1,000 dilution; p38 (cat. no. 9212; CST) at 1:1,000 dilution; p‐Erk [Thr202/Tyr204 (clone D13.14.4E), cat. no. 4370, CST] at 1:2,000 dilution; Erk 1/2 (cat. no. 9102; CST) at 1:1,000 dilu‐ tion, and GAPDH (cat. no. 10494‐1‐AP; ProteinTech Group, Inc.) at 1:5,000 dilution at 4 ̊C overnight. .. After washing, the horseradish peroxidase (HRP)‐conjugated affinity‐purified goat anti‐rabbit IgG (H + L) (cat. no. SA00001‐2; ProteinTech Group, Inc.) was used for hybridization at room temperature for 1 h, followed by autoradiograph.



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    Analysis of proteomics data in the CPTAC database. (A) Comparison of the protein levels between normal (green) and tumour (red) samples. (B) Kaplan–Meier curve for each protein. (C) Pan-cancer analysis for <t>CD2AP</t> (green: normal tissue, red: cancer tissue). (D) Relationship between CD2AP protein level and immune infiltration in pan-cancer.
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    Characterization of a novel lipid-dependent YAP complex. ( A – C ) Western blots illustrating co-immunoprecipitations for Talin, <t>CD2AP,</t> YAP, PDLIM7, and Ezrin. GAPDH was used for assessing loading. ( D ) Western blots illustrating co-IPs for talin, CD2AP, YAP, PDLIM7, and ezrin using OA to disrupt the interactions of the complex. GAPDH was used for assessing loading. ( E ) Immunofluorescent images of YAP with and without OA treatment and different siRNA knockdowns of YAP, CD2AP, talin, and ezrin observing the amount of lipid droplets present in the cell. Red box illustrates zoomed in area. Scale bar 100 μm. ( F ) Immunoblots illustrating the effect of Talin siRNA on pYAP (S127), total YAP, and a housekeeping gene (GAPDH). ( G ) Representative brightfield images of a scratch wound (migration assay) showing effect of siRNA of YAP, talin, CD2AP, and ezrin at 0 and 48 h post-scratch compared to control. Scale bar 300 μm. ( H ) Graph illustrating the rate of wound closure upon siRNA of YAP, Talin, CD2AP, and ezrin in comparison to control. ( I ) Immunofluorescent images showing the effect of siRNA on YAP, talin, CD2AP, and ezrin and observing the amount of nuclear YAP present. Scale bar 20 μm. Experiments were repeated 3–4 times (n = 3/n = 4).
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    Characterization of a novel lipid-dependent YAP complex. ( A – C ) Western blots illustrating co-immunoprecipitations for Talin, <t>CD2AP,</t> YAP, PDLIM7, and Ezrin. GAPDH was used for assessing loading. ( D ) Western blots illustrating co-IPs for talin, CD2AP, YAP, PDLIM7, and ezrin using OA to disrupt the interactions of the complex. GAPDH was used for assessing loading. ( E ) Immunofluorescent images of YAP with and without OA treatment and different siRNA knockdowns of YAP, CD2AP, talin, and ezrin observing the amount of lipid droplets present in the cell. Red box illustrates zoomed in area. Scale bar 100 μm. ( F ) Immunoblots illustrating the effect of Talin siRNA on pYAP (S127), total YAP, and a housekeeping gene (GAPDH). ( G ) Representative brightfield images of a scratch wound (migration assay) showing effect of siRNA of YAP, talin, CD2AP, and ezrin at 0 and 48 h post-scratch compared to control. Scale bar 300 μm. ( H ) Graph illustrating the rate of wound closure upon siRNA of YAP, Talin, CD2AP, and ezrin in comparison to control. ( I ) Immunofluorescent images showing the effect of siRNA on YAP, talin, CD2AP, and ezrin and observing the amount of nuclear YAP present. Scale bar 20 μm. Experiments were repeated 3–4 times (n = 3/n = 4).
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    Characterization of a novel lipid-dependent YAP complex. ( A – C ) Western blots illustrating co-immunoprecipitations for Talin, <t>CD2AP,</t> YAP, PDLIM7, and Ezrin. GAPDH was used for assessing loading. ( D ) Western blots illustrating co-IPs for talin, CD2AP, YAP, PDLIM7, and ezrin using OA to disrupt the interactions of the complex. GAPDH was used for assessing loading. ( E ) Immunofluorescent images of YAP with and without OA treatment and different siRNA knockdowns of YAP, CD2AP, talin, and ezrin observing the amount of lipid droplets present in the cell. Red box illustrates zoomed in area. Scale bar 100 μm. ( F ) Immunoblots illustrating the effect of Talin siRNA on pYAP (S127), total YAP, and a housekeeping gene (GAPDH). ( G ) Representative brightfield images of a scratch wound (migration assay) showing effect of siRNA of YAP, talin, CD2AP, and ezrin at 0 and 48 h post-scratch compared to control. Scale bar 300 μm. ( H ) Graph illustrating the rate of wound closure upon siRNA of YAP, Talin, CD2AP, and ezrin in comparison to control. ( I ) Immunofluorescent images showing the effect of siRNA on YAP, talin, CD2AP, and ezrin and observing the amount of nuclear YAP present. Scale bar 20 μm. Experiments were repeated 3–4 times (n = 3/n = 4).
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    Characterization of a novel lipid-dependent YAP complex. ( A – C ) Western blots illustrating co-immunoprecipitations for Talin, <t>CD2AP,</t> YAP, PDLIM7, and Ezrin. GAPDH was used for assessing loading. ( D ) Western blots illustrating co-IPs for talin, CD2AP, YAP, PDLIM7, and ezrin using OA to disrupt the interactions of the complex. GAPDH was used for assessing loading. ( E ) Immunofluorescent images of YAP with and without OA treatment and different siRNA knockdowns of YAP, CD2AP, talin, and ezrin observing the amount of lipid droplets present in the cell. Red box illustrates zoomed in area. Scale bar 100 μm. ( F ) Immunoblots illustrating the effect of Talin siRNA on pYAP (S127), total YAP, and a housekeeping gene (GAPDH). ( G ) Representative brightfield images of a scratch wound (migration assay) showing effect of siRNA of YAP, talin, CD2AP, and ezrin at 0 and 48 h post-scratch compared to control. Scale bar 300 μm. ( H ) Graph illustrating the rate of wound closure upon siRNA of YAP, Talin, CD2AP, and ezrin in comparison to control. ( I ) Immunofluorescent images showing the effect of siRNA on YAP, talin, CD2AP, and ezrin and observing the amount of nuclear YAP present. Scale bar 20 μm. Experiments were repeated 3–4 times (n = 3/n = 4).
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    Image Search Results


    Analysis of proteomics data in the CPTAC database. (A) Comparison of the protein levels between normal (green) and tumour (red) samples. (B) Kaplan–Meier curve for each protein. (C) Pan-cancer analysis for CD2AP (green: normal tissue, red: cancer tissue). (D) Relationship between CD2AP protein level and immune infiltration in pan-cancer.

    Journal: Frontiers in Immunology

    Article Title: Identification of a ubiquitin-binding domain protein, CD2AP, in predicting the prognosis and treatment of lung adenocarcinoma

    doi: 10.3389/fimmu.2025.1726531

    Figure Lengend Snippet: Analysis of proteomics data in the CPTAC database. (A) Comparison of the protein levels between normal (green) and tumour (red) samples. (B) Kaplan–Meier curve for each protein. (C) Pan-cancer analysis for CD2AP (green: normal tissue, red: cancer tissue). (D) Relationship between CD2AP protein level and immune infiltration in pan-cancer.

    Article Snippet: The sections were then incubated overnight at 4 °C with a primary antibody against CD2AP (Proteintech, Wuhan, China).

    Techniques: Comparison

    TMB and immune cell analysis. (A) The top 20 mutated genes in the CD2AP -low subgroup. (B) The top 20 mutated genes in the CD2AP -high subgroup. In both panels, the genes are ordered from top to bottom by their mutation frequency. The most frequently mutated genes in the entire cohort are TP53 and TTN. (C) The infiltration fraction for each immune cell between the CD2AP -low(blue) and the CD2AP -high(red) subgroups. (D) The relationship between CD2AP copy number variation and the infiltration level of immune cells. *, P <0.05**, P <0.01; ***, P <0.001.

    Journal: Frontiers in Immunology

    Article Title: Identification of a ubiquitin-binding domain protein, CD2AP, in predicting the prognosis and treatment of lung adenocarcinoma

    doi: 10.3389/fimmu.2025.1726531

    Figure Lengend Snippet: TMB and immune cell analysis. (A) The top 20 mutated genes in the CD2AP -low subgroup. (B) The top 20 mutated genes in the CD2AP -high subgroup. In both panels, the genes are ordered from top to bottom by their mutation frequency. The most frequently mutated genes in the entire cohort are TP53 and TTN. (C) The infiltration fraction for each immune cell between the CD2AP -low(blue) and the CD2AP -high(red) subgroups. (D) The relationship between CD2AP copy number variation and the infiltration level of immune cells. *, P <0.05**, P <0.01; ***, P <0.001.

    Article Snippet: The sections were then incubated overnight at 4 °C with a primary antibody against CD2AP (Proteintech, Wuhan, China).

    Techniques: Cell Analysis, Mutagenesis

    Pathway enrichment analysis. (A) GO analysis for the DEGs between the CD2AP -low and CD2AP -high subgroups. (B) KEGG analysis for the DEGs between the CD2AP -low and CD2AP -high subgroups. (C) GSEA analysis for CD2AP -low and CD2AP -high subgroups.

    Journal: Frontiers in Immunology

    Article Title: Identification of a ubiquitin-binding domain protein, CD2AP, in predicting the prognosis and treatment of lung adenocarcinoma

    doi: 10.3389/fimmu.2025.1726531

    Figure Lengend Snippet: Pathway enrichment analysis. (A) GO analysis for the DEGs between the CD2AP -low and CD2AP -high subgroups. (B) KEGG analysis for the DEGs between the CD2AP -low and CD2AP -high subgroups. (C) GSEA analysis for CD2AP -low and CD2AP -high subgroups.

    Article Snippet: The sections were then incubated overnight at 4 °C with a primary antibody against CD2AP (Proteintech, Wuhan, China).

    Techniques:

    Single-cell and IHC analysis. (A) Single-cell analysis for GSE99254 . (B) Healthy lung tissue (Patient ID: 2101) staining with CD2AP. (C) LUAD tissue (Patient ID: 2438) staining with CD2AP.

    Journal: Frontiers in Immunology

    Article Title: Identification of a ubiquitin-binding domain protein, CD2AP, in predicting the prognosis and treatment of lung adenocarcinoma

    doi: 10.3389/fimmu.2025.1726531

    Figure Lengend Snippet: Single-cell and IHC analysis. (A) Single-cell analysis for GSE99254 . (B) Healthy lung tissue (Patient ID: 2101) staining with CD2AP. (C) LUAD tissue (Patient ID: 2438) staining with CD2AP.

    Article Snippet: The sections were then incubated overnight at 4 °C with a primary antibody against CD2AP (Proteintech, Wuhan, China).

    Techniques: Single-cell Analysis, Staining

    Exploration of CD2AP functions. (A) CD2AP gene expression across all cell types; (B) CD2AP gene expression in monocyte subtypes; (C) Expression distribution of CD2AP in cancer cells and monocytes; (D) Cellular interaction network of CD2AP + cancer cells LUAD; (E) Dot plot for the enrichment of ligand-receptor pathways; (F) KEGG pathway enrichment analysis for CD2AP + and CD2AP - monocytes.

    Journal: Frontiers in Immunology

    Article Title: Identification of a ubiquitin-binding domain protein, CD2AP, in predicting the prognosis and treatment of lung adenocarcinoma

    doi: 10.3389/fimmu.2025.1726531

    Figure Lengend Snippet: Exploration of CD2AP functions. (A) CD2AP gene expression across all cell types; (B) CD2AP gene expression in monocyte subtypes; (C) Expression distribution of CD2AP in cancer cells and monocytes; (D) Cellular interaction network of CD2AP + cancer cells LUAD; (E) Dot plot for the enrichment of ligand-receptor pathways; (F) KEGG pathway enrichment analysis for CD2AP + and CD2AP - monocytes.

    Article Snippet: The sections were then incubated overnight at 4 °C with a primary antibody against CD2AP (Proteintech, Wuhan, China).

    Techniques: Gene Expression, Expressing

    Drug sensitivity analysis and molecular docking. (A) Venn plot indicating the potential targeted compounds. (B) The structures of CD2AP. (C) Molecular docking between afatinib and CD2AP. (D) Molecular docking between dasatinib and CD2AP.

    Journal: Frontiers in Immunology

    Article Title: Identification of a ubiquitin-binding domain protein, CD2AP, in predicting the prognosis and treatment of lung adenocarcinoma

    doi: 10.3389/fimmu.2025.1726531

    Figure Lengend Snippet: Drug sensitivity analysis and molecular docking. (A) Venn plot indicating the potential targeted compounds. (B) The structures of CD2AP. (C) Molecular docking between afatinib and CD2AP. (D) Molecular docking between dasatinib and CD2AP.

    Article Snippet: The sections were then incubated overnight at 4 °C with a primary antibody against CD2AP (Proteintech, Wuhan, China).

    Techniques:

    Histological experiments to validate the expression of CD2AP. (A) Validation of CD2AP expression in cancer and adjacent tissues by immunofluorescence (n=3 biologically independent samples); (B) Determine CD2AP protein levels using Western blot analysis; (C) Statistical chart for WB, data are presented as mean ± SD (n=5 biologically independent samples). * P < 0.05; (D) Results of rt-qPCR for 5 controls vs. 5 LUADs, data are presented as mean ± SD (n=5 biologically independent samples). ** P < 0.01.

    Journal: Frontiers in Immunology

    Article Title: Identification of a ubiquitin-binding domain protein, CD2AP, in predicting the prognosis and treatment of lung adenocarcinoma

    doi: 10.3389/fimmu.2025.1726531

    Figure Lengend Snippet: Histological experiments to validate the expression of CD2AP. (A) Validation of CD2AP expression in cancer and adjacent tissues by immunofluorescence (n=3 biologically independent samples); (B) Determine CD2AP protein levels using Western blot analysis; (C) Statistical chart for WB, data are presented as mean ± SD (n=5 biologically independent samples). * P < 0.05; (D) Results of rt-qPCR for 5 controls vs. 5 LUADs, data are presented as mean ± SD (n=5 biologically independent samples). ** P < 0.01.

    Article Snippet: The sections were then incubated overnight at 4 °C with a primary antibody against CD2AP (Proteintech, Wuhan, China).

    Techniques: Expressing, Biomarker Discovery, Immunofluorescence, Western Blot, Quantitative RT-PCR

    Cell experiments to validate the function of CD2AP. (A) WB to show the knockdown efficiency of CD2AP; (B) Statistical chart for WB, data are presented as mean ± SD (n=3 biologically independent samples). ** P < 0.01; (C) Proliferative capacity of A549 cells by CCK-8 assay, data are presented as mean ± SD (n=3 technical replicates per group, representative of three independent experiments); (D) Cell migration capabilities by transwell; (E) Statistical chart for transwell counts, data are presented as mean ± SD (n=3 biologically independent samples). **** P < 0.0001; (F) Cell migration capabilities by wound healing assays; (G) Statistical chart for wound healing assays, data are presented as mean ± SD (n=3 biologically independent samples). ** P < 0.01.

    Journal: Frontiers in Immunology

    Article Title: Identification of a ubiquitin-binding domain protein, CD2AP, in predicting the prognosis and treatment of lung adenocarcinoma

    doi: 10.3389/fimmu.2025.1726531

    Figure Lengend Snippet: Cell experiments to validate the function of CD2AP. (A) WB to show the knockdown efficiency of CD2AP; (B) Statistical chart for WB, data are presented as mean ± SD (n=3 biologically independent samples). ** P < 0.01; (C) Proliferative capacity of A549 cells by CCK-8 assay, data are presented as mean ± SD (n=3 technical replicates per group, representative of three independent experiments); (D) Cell migration capabilities by transwell; (E) Statistical chart for transwell counts, data are presented as mean ± SD (n=3 biologically independent samples). **** P < 0.0001; (F) Cell migration capabilities by wound healing assays; (G) Statistical chart for wound healing assays, data are presented as mean ± SD (n=3 biologically independent samples). ** P < 0.01.

    Article Snippet: The sections were then incubated overnight at 4 °C with a primary antibody against CD2AP (Proteintech, Wuhan, China).

    Techniques: Knockdown, CCK-8 Assay, Migration

    Characterization of a novel lipid-dependent YAP complex. ( A – C ) Western blots illustrating co-immunoprecipitations for Talin, CD2AP, YAP, PDLIM7, and Ezrin. GAPDH was used for assessing loading. ( D ) Western blots illustrating co-IPs for talin, CD2AP, YAP, PDLIM7, and ezrin using OA to disrupt the interactions of the complex. GAPDH was used for assessing loading. ( E ) Immunofluorescent images of YAP with and without OA treatment and different siRNA knockdowns of YAP, CD2AP, talin, and ezrin observing the amount of lipid droplets present in the cell. Red box illustrates zoomed in area. Scale bar 100 μm. ( F ) Immunoblots illustrating the effect of Talin siRNA on pYAP (S127), total YAP, and a housekeeping gene (GAPDH). ( G ) Representative brightfield images of a scratch wound (migration assay) showing effect of siRNA of YAP, talin, CD2AP, and ezrin at 0 and 48 h post-scratch compared to control. Scale bar 300 μm. ( H ) Graph illustrating the rate of wound closure upon siRNA of YAP, Talin, CD2AP, and ezrin in comparison to control. ( I ) Immunofluorescent images showing the effect of siRNA on YAP, talin, CD2AP, and ezrin and observing the amount of nuclear YAP present. Scale bar 20 μm. Experiments were repeated 3–4 times (n = 3/n = 4).

    Journal: Cells

    Article Title: The Regulation of the Hippo Signalling Pathway Effector YAP Through a Novel Lipid-Dependent Extracellular Matrix Complex

    doi: 10.3390/cells14211701

    Figure Lengend Snippet: Characterization of a novel lipid-dependent YAP complex. ( A – C ) Western blots illustrating co-immunoprecipitations for Talin, CD2AP, YAP, PDLIM7, and Ezrin. GAPDH was used for assessing loading. ( D ) Western blots illustrating co-IPs for talin, CD2AP, YAP, PDLIM7, and ezrin using OA to disrupt the interactions of the complex. GAPDH was used for assessing loading. ( E ) Immunofluorescent images of YAP with and without OA treatment and different siRNA knockdowns of YAP, CD2AP, talin, and ezrin observing the amount of lipid droplets present in the cell. Red box illustrates zoomed in area. Scale bar 100 μm. ( F ) Immunoblots illustrating the effect of Talin siRNA on pYAP (S127), total YAP, and a housekeeping gene (GAPDH). ( G ) Representative brightfield images of a scratch wound (migration assay) showing effect of siRNA of YAP, talin, CD2AP, and ezrin at 0 and 48 h post-scratch compared to control. Scale bar 300 μm. ( H ) Graph illustrating the rate of wound closure upon siRNA of YAP, Talin, CD2AP, and ezrin in comparison to control. ( I ) Immunofluorescent images showing the effect of siRNA on YAP, talin, CD2AP, and ezrin and observing the amount of nuclear YAP present. Scale bar 20 μm. Experiments were repeated 3–4 times (n = 3/n = 4).

    Article Snippet: Antibodies used in all experiments were rabbit anti-PDLIM7 (Novus, UK NBP1-84841), rabbit anti-YAP H-125 (Cat.# sc-15407), mouse anti-YAP (63.7) (Cat.# sc-101199) (both Santa Cruz Biotechnology (Distributed by Insight Biotechnology, Welwyn Garden City, UK), rabbit phospho-YAP (Ser127) (CST, UK, Cat no.#4911) CD2AP (B-4), mouse monoclonal (Cat.# sc-25272), mouse anti-Talin T3287-0.2 ml (SLS, UK), mouse ezrin antibody (3C12) (Cat.#sc-58758), and mouse GAPDH antibody (6C5) (Cat.#sc-32233) Santa Cruz Biotechnology (Distributed by Insight Biotechnology, Welwyn Garden City, UK).

    Techniques: Western Blot, Migration, Control, Comparison

    Schematic diagram of signalling dynamics in the ECM/cytoskeleton. This schematic illustrates the key molecular components involved in cell adhesion and mechanotransduction at focal adhesions. Integrin receptors (α and β subunits) span the plasma membrane, linking extracellular fibronectin within the extracellular matrix (ECM) to intracellular adaptor and signalling proteins. Talin, Paxillin, Vinculin, Src, and FAK form a dynamic protein complex that anchors integrins to the actin cytoskeleton, represented by F-actin stress fibres and crosslinking α-Actinin. These interactions facilitate mechanical force transmission and initiate downstream signalling cascades. Cytoplasmic signalling molecules, including the novel complex YAP, PDLM, CD2AP and ezrin, are shown participating in mechanosensitive pathways that regulate cellular responses such as migration, proliferation, and gene expression. The diagram highlights the integrative role of focal adhesions as hubs for biochemical and biomechanical signal transduction.

    Journal: Cells

    Article Title: The Regulation of the Hippo Signalling Pathway Effector YAP Through a Novel Lipid-Dependent Extracellular Matrix Complex

    doi: 10.3390/cells14211701

    Figure Lengend Snippet: Schematic diagram of signalling dynamics in the ECM/cytoskeleton. This schematic illustrates the key molecular components involved in cell adhesion and mechanotransduction at focal adhesions. Integrin receptors (α and β subunits) span the plasma membrane, linking extracellular fibronectin within the extracellular matrix (ECM) to intracellular adaptor and signalling proteins. Talin, Paxillin, Vinculin, Src, and FAK form a dynamic protein complex that anchors integrins to the actin cytoskeleton, represented by F-actin stress fibres and crosslinking α-Actinin. These interactions facilitate mechanical force transmission and initiate downstream signalling cascades. Cytoplasmic signalling molecules, including the novel complex YAP, PDLM, CD2AP and ezrin, are shown participating in mechanosensitive pathways that regulate cellular responses such as migration, proliferation, and gene expression. The diagram highlights the integrative role of focal adhesions as hubs for biochemical and biomechanical signal transduction.

    Article Snippet: Antibodies used in all experiments were rabbit anti-PDLIM7 (Novus, UK NBP1-84841), rabbit anti-YAP H-125 (Cat.# sc-15407), mouse anti-YAP (63.7) (Cat.# sc-101199) (both Santa Cruz Biotechnology (Distributed by Insight Biotechnology, Welwyn Garden City, UK), rabbit phospho-YAP (Ser127) (CST, UK, Cat no.#4911) CD2AP (B-4), mouse monoclonal (Cat.# sc-25272), mouse anti-Talin T3287-0.2 ml (SLS, UK), mouse ezrin antibody (3C12) (Cat.#sc-58758), and mouse GAPDH antibody (6C5) (Cat.#sc-32233) Santa Cruz Biotechnology (Distributed by Insight Biotechnology, Welwyn Garden City, UK).

    Techniques: Clinical Proteomics, Membrane, Transmission Assay, Migration, Gene Expression, Transduction