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duolink pla blocking solution  (Millipore)


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    Structured Review

    Millipore duolink pla blocking solution
    Duolink Pla Blocking Solution, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pla+blocking+solution/duolink+pla/pm37480622-106-6-10
    Average 90 stars, based on 1 article reviews
    duolink pla blocking solution - by Bioz Stars, 2026-11
    90/100 stars

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    Related Articles

    Proximity Ligation Assay:

    Article Title: The AP-1 adaptor complex is essential for intracellular trafficking of the ORF2 capsid protein and assembly of Hepatitis E virus
    Article Snippet: .. We used the Duolink PLA technology (Sigma) that uses a pair of primary antibodies and secondary antibodies labeled with oligonucleotides which when in close proximity (within 40 nm) undertake rolling circle amplification to generate specific fluorescent spot signals after the addition of labeled probes that can be visualized by microscopy [ ]. ..

    Article Title: Lipoylation inhibition enhances radiation control of lung cancer by suppressing homologous recombination DNA damage repair.
    Article Snippet: .. An in situ PLA was conducted using Duolink PLA reagents (MilliporeSigma) in accordance with the manufacturer’s instructions. ..

    Article Title: Palmitoylated importin α regulates mitotic spindle orientation through interaction with NuMA.
    Article Snippet: .. Proximity ligation assay (PLA) was performed using DuoLink PLA (Millipore Sigma) following the recommended protocol. .. PLA analysis of importin α and NuMA interaction was performed in mitotically arrested HCT 116 cells using mouse anti-importin α (Proteintech) and rabbit anti-NuMA (Novus Biologicals).

    Labeling:

    Article Title: The AP-1 adaptor complex is essential for intracellular trafficking of the ORF2 capsid protein and assembly of Hepatitis E virus
    Article Snippet: .. We used the Duolink PLA technology (Sigma) that uses a pair of primary antibodies and secondary antibodies labeled with oligonucleotides which when in close proximity (within 40 nm) undertake rolling circle amplification to generate specific fluorescent spot signals after the addition of labeled probes that can be visualized by microscopy [ ]. ..

    Amplification:

    Article Title: The AP-1 adaptor complex is essential for intracellular trafficking of the ORF2 capsid protein and assembly of Hepatitis E virus
    Article Snippet: .. We used the Duolink PLA technology (Sigma) that uses a pair of primary antibodies and secondary antibodies labeled with oligonucleotides which when in close proximity (within 40 nm) undertake rolling circle amplification to generate specific fluorescent spot signals after the addition of labeled probes that can be visualized by microscopy [ ]. ..

    Microscopy:

    Article Title: The AP-1 adaptor complex is essential for intracellular trafficking of the ORF2 capsid protein and assembly of Hepatitis E virus
    Article Snippet: .. We used the Duolink PLA technology (Sigma) that uses a pair of primary antibodies and secondary antibodies labeled with oligonucleotides which when in close proximity (within 40 nm) undertake rolling circle amplification to generate specific fluorescent spot signals after the addition of labeled probes that can be visualized by microscopy [ ]. ..

    other:

    Article Title: Fibromodulin selectively accelerates myofibroblast apoptosis in cutaneous wounds by enhancing interleukin 1β signaling.
    Article Snippet: Direct IL1β-IL1R1 and IL1R1-IL1RAP interactions were visualized by Duolink® in situ PLA assay (MilliporeSigma), respectively, according to the manufacturer’s instructions.

    Article Title: MDC1 mediates Pellino recruitment to sites of DNA double-strand breaks
    Article Snippet: All the following steps were performed using the Duolink® PLA Reagents (Sigma-Aldrich, DUO92001, DUO92005, DUO92008, DUO82049) and according to the manufacturer’s protocol.

    Article Title: Gain-of-function human UNC93B1 variants cause systemic lupus erythematosus and chilblain lupus
    Article Snippet: Cells were then washed, fixed with cold 100% methanol for 3 min at room temperature, and incubated with permeabilization buffer (PBS 0.2% BSA, 0.2% Triton-X100) and primary antibodies (mouse anti-TLR8 antibody, # DDX0480P clone 303F1.14; Novus Biologicals; rabbit anti-V5 antibody, #13202; Cell Signaling).

    Article Title: Foxg1 regulates translation of neocortical neuronal genes, including the main NMDA receptor subunit gene, Grin1
    Article Snippet: PLA assays were performed according to manufacturer’s instructions (DuolinkTM PLA Technology, Sigma).

    Article Title: BioID-based intact cell interactome of the Kv1.3 potassium channel identifies a Kv1.3-STAT3-p53 cellular signaling pathway
    Article Snippet: To perform PLA, cells were washed twice with Buffer A (DUO82046, Sigma-Aldrich) for 5 min each at room temperature and then incubated for 1 hour at 37°C with secondary antibodies conjugated with complementary oligonucleotides [anti-rabbit PLUS (DUO82002, Sigma-Aldrich) and anti-mouse MINUS (DUO82004, Sigma-Aldrich)], diluted 1:5 in the Duolink Antibody Diluent (DUO82008, Sigma-Aldrich).

    In Situ:

    Article Title: Lipoylation inhibition enhances radiation control of lung cancer by suppressing homologous recombination DNA damage repair.
    Article Snippet: .. An in situ PLA was conducted using Duolink PLA reagents (MilliporeSigma) in accordance with the manufacturer’s instructions. ..



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    Loss of BTG3 leads to reduced mobility of XPC at damage sites. ( A – C ) Colocalization of BTG3 and XPC at damage sites after UV. <t>PLA</t> was conducted <t>with</t> <t>HaCaT</t> cells using anti-BTG3 and anti-XPC (A). Mean fluorescence intensity and PLA foci number were quantified and shown in panels (B) and (C), respectively, with n ≧ 100. Data were analyzed using unpaired two-tailed t -test and presented as mean ± SEM Scale bar, 10 μm. ( D ) Co-immunoprecipitation of endogenous BTG3 and XPC from HaCaT cells. ( E, F ) Retention of XPC at localized UV damage in BTG3 KO cells. Localized UVC-irradiation (100 J/m 2 ) was performed with 5 μM isopore membrane filter and XPC loading at localized UV damage sites was assessed using confocal microscopy (E). Scale bar, 10 μm. Percent cells with XPC-positive foci were counted and presented as mean ± SEM in panel (F). Data were analyzed using unpaired two-tailed t -test. n ≧ 50. ( G, H ) Mobility of XPC was reduced in BTG3 KO cells. The mobility of XPC-GFP in mock-treated or global UV-irradiated (20 J/m 2 ) parental and BTG3 KO HEK293T cells was assessed using FRAP. Fluorescence recovery was monitored over 120 s and normalized to prebleach intensity ( n = 36 from 3 independent experiments) (G). Data were analyzed using unpaired two-tailed t -tests and shown as mean ± SEM in panel (H).
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    Loss of BTG3 leads to reduced mobility of XPC at damage sites. ( A – C ) Colocalization of BTG3 and XPC at damage sites after UV. <t>PLA</t> was conducted <t>with</t> <t>HaCaT</t> cells using anti-BTG3 and anti-XPC (A). Mean fluorescence intensity and PLA foci number were quantified and shown in panels (B) and (C), respectively, with n ≧ 100. Data were analyzed using unpaired two-tailed t -test and presented as mean ± SEM Scale bar, 10 μm. ( D ) Co-immunoprecipitation of endogenous BTG3 and XPC from HaCaT cells. ( E, F ) Retention of XPC at localized UV damage in BTG3 KO cells. Localized UVC-irradiation (100 J/m 2 ) was performed with 5 μM isopore membrane filter and XPC loading at localized UV damage sites was assessed using confocal microscopy (E). Scale bar, 10 μm. Percent cells with XPC-positive foci were counted and presented as mean ± SEM in panel (F). Data were analyzed using unpaired two-tailed t -test. n ≧ 50. ( G, H ) Mobility of XPC was reduced in BTG3 KO cells. The mobility of XPC-GFP in mock-treated or global UV-irradiated (20 J/m 2 ) parental and BTG3 KO HEK293T cells was assessed using FRAP. Fluorescence recovery was monitored over 120 s and normalized to prebleach intensity ( n = 36 from 3 independent experiments) (G). Data were analyzed using unpaired two-tailed t -tests and shown as mean ± SEM in panel (H).
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    Loss of BTG3 leads to reduced mobility of XPC at damage sites. ( A – C ) Colocalization of BTG3 and XPC at damage sites after UV. <t>PLA</t> was conducted <t>with</t> <t>HaCaT</t> cells using anti-BTG3 and anti-XPC (A). Mean fluorescence intensity and PLA foci number were quantified and shown in panels (B) and (C), respectively, with n ≧ 100. Data were analyzed using unpaired two-tailed t -test and presented as mean ± SEM Scale bar, 10 μm. ( D ) Co-immunoprecipitation of endogenous BTG3 and XPC from HaCaT cells. ( E, F ) Retention of XPC at localized UV damage in BTG3 KO cells. Localized UVC-irradiation (100 J/m 2 ) was performed with 5 μM isopore membrane filter and XPC loading at localized UV damage sites was assessed using confocal microscopy (E). Scale bar, 10 μm. Percent cells with XPC-positive foci were counted and presented as mean ± SEM in panel (F). Data were analyzed using unpaired two-tailed t -test. n ≧ 50. ( G, H ) Mobility of XPC was reduced in BTG3 KO cells. The mobility of XPC-GFP in mock-treated or global UV-irradiated (20 J/m 2 ) parental and BTG3 KO HEK293T cells was assessed using FRAP. Fluorescence recovery was monitored over 120 s and normalized to prebleach intensity ( n = 36 from 3 independent experiments) (G). Data were analyzed using unpaired two-tailed t -tests and shown as mean ± SEM in panel (H).
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    Loss of BTG3 leads to reduced mobility of XPC at damage sites. ( A – C ) Colocalization of BTG3 and XPC at damage sites after UV. <t>PLA</t> was conducted <t>with</t> <t>HaCaT</t> cells using anti-BTG3 and anti-XPC (A). Mean fluorescence intensity and PLA foci number were quantified and shown in panels (B) and (C), respectively, with n ≧ 100. Data were analyzed using unpaired two-tailed t -test and presented as mean ± SEM Scale bar, 10 μm. ( D ) Co-immunoprecipitation of endogenous BTG3 and XPC from HaCaT cells. ( E, F ) Retention of XPC at localized UV damage in BTG3 KO cells. Localized UVC-irradiation (100 J/m 2 ) was performed with 5 μM isopore membrane filter and XPC loading at localized UV damage sites was assessed using confocal microscopy (E). Scale bar, 10 μm. Percent cells with XPC-positive foci were counted and presented as mean ± SEM in panel (F). Data were analyzed using unpaired two-tailed t -test. n ≧ 50. ( G, H ) Mobility of XPC was reduced in BTG3 KO cells. The mobility of XPC-GFP in mock-treated or global UV-irradiated (20 J/m 2 ) parental and BTG3 KO HEK293T cells was assessed using FRAP. Fluorescence recovery was monitored over 120 s and normalized to prebleach intensity ( n = 36 from 3 independent experiments) (G). Data were analyzed using unpaired two-tailed t -tests and shown as mean ± SEM in panel (H).
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    Millipore blocking solution supplied pla kit
    Loss of BTG3 leads to reduced mobility of XPC at damage sites. ( A – C ) Colocalization of BTG3 and XPC at damage sites after UV. <t>PLA</t> was conducted <t>with</t> <t>HaCaT</t> cells using anti-BTG3 and anti-XPC (A). Mean fluorescence intensity and PLA foci number were quantified and shown in panels (B) and (C), respectively, with n ≧ 100. Data were analyzed using unpaired two-tailed t -test and presented as mean ± SEM Scale bar, 10 μm. ( D ) Co-immunoprecipitation of endogenous BTG3 and XPC from HaCaT cells. ( E, F ) Retention of XPC at localized UV damage in BTG3 KO cells. Localized UVC-irradiation (100 J/m 2 ) was performed with 5 μM isopore membrane filter and XPC loading at localized UV damage sites was assessed using confocal microscopy (E). Scale bar, 10 μm. Percent cells with XPC-positive foci were counted and presented as mean ± SEM in panel (F). Data were analyzed using unpaired two-tailed t -test. n ≧ 50. ( G, H ) Mobility of XPC was reduced in BTG3 KO cells. The mobility of XPC-GFP in mock-treated or global UV-irradiated (20 J/m 2 ) parental and BTG3 KO HEK293T cells was assessed using FRAP. Fluorescence recovery was monitored over 120 s and normalized to prebleach intensity ( n = 36 from 3 independent experiments) (G). Data were analyzed using unpaired two-tailed t -tests and shown as mean ± SEM in panel (H).
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    Image Search Results


    Loss of BTG3 leads to reduced mobility of XPC at damage sites. ( A – C ) Colocalization of BTG3 and XPC at damage sites after UV. PLA was conducted with HaCaT cells using anti-BTG3 and anti-XPC (A). Mean fluorescence intensity and PLA foci number were quantified and shown in panels (B) and (C), respectively, with n ≧ 100. Data were analyzed using unpaired two-tailed t -test and presented as mean ± SEM Scale bar, 10 μm. ( D ) Co-immunoprecipitation of endogenous BTG3 and XPC from HaCaT cells. ( E, F ) Retention of XPC at localized UV damage in BTG3 KO cells. Localized UVC-irradiation (100 J/m 2 ) was performed with 5 μM isopore membrane filter and XPC loading at localized UV damage sites was assessed using confocal microscopy (E). Scale bar, 10 μm. Percent cells with XPC-positive foci were counted and presented as mean ± SEM in panel (F). Data were analyzed using unpaired two-tailed t -test. n ≧ 50. ( G, H ) Mobility of XPC was reduced in BTG3 KO cells. The mobility of XPC-GFP in mock-treated or global UV-irradiated (20 J/m 2 ) parental and BTG3 KO HEK293T cells was assessed using FRAP. Fluorescence recovery was monitored over 120 s and normalized to prebleach intensity ( n = 36 from 3 independent experiments) (G). Data were analyzed using unpaired two-tailed t -tests and shown as mean ± SEM in panel (H).

    Journal: Nucleic Acids Research

    Article Title: BTG3-dependent VCP/p97 nuclear translocation is required for efficient repair of UV-induced DNA lesions

    doi: 10.1093/nar/gkaf626

    Figure Lengend Snippet: Loss of BTG3 leads to reduced mobility of XPC at damage sites. ( A – C ) Colocalization of BTG3 and XPC at damage sites after UV. PLA was conducted with HaCaT cells using anti-BTG3 and anti-XPC (A). Mean fluorescence intensity and PLA foci number were quantified and shown in panels (B) and (C), respectively, with n ≧ 100. Data were analyzed using unpaired two-tailed t -test and presented as mean ± SEM Scale bar, 10 μm. ( D ) Co-immunoprecipitation of endogenous BTG3 and XPC from HaCaT cells. ( E, F ) Retention of XPC at localized UV damage in BTG3 KO cells. Localized UVC-irradiation (100 J/m 2 ) was performed with 5 μM isopore membrane filter and XPC loading at localized UV damage sites was assessed using confocal microscopy (E). Scale bar, 10 μm. Percent cells with XPC-positive foci were counted and presented as mean ± SEM in panel (F). Data were analyzed using unpaired two-tailed t -test. n ≧ 50. ( G, H ) Mobility of XPC was reduced in BTG3 KO cells. The mobility of XPC-GFP in mock-treated or global UV-irradiated (20 J/m 2 ) parental and BTG3 KO HEK293T cells was assessed using FRAP. Fluorescence recovery was monitored over 120 s and normalized to prebleach intensity ( n = 36 from 3 independent experiments) (G). Data were analyzed using unpaired two-tailed t -tests and shown as mean ± SEM in panel (H).

    Article Snippet: After incubation with PLA blocking solution, HaCaT cells were incubated with anti-XPC (Santa Cruz, 1:200 dilution) and anti-BTG3 (Lab raised, 1:100 dilution) antibodies overnight at 4°C with gentle rocking.

    Techniques: Fluorescence, Two Tailed Test, Immunoprecipitation, Irradiation, Membrane, Confocal Microscopy