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polyclonal antibodies against lc3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc polyclonal antibodies against lc3
    Polyclonal Antibodies Against Lc3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 2550 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal antibodies against lc3/product/Cell Signaling Technology Inc
    Average 99 stars, based on 2550 article reviews
    polyclonal antibodies against lc3 - by Bioz Stars, 2026-03
    99/100 stars

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    Histological sections of Parkin and <t>LC3</t> staining. a1—sham group, 40×, b1—control group, 40×, and c1—treatment group, 40×. Parkin staining: a2—sham group, 40×, b2—control group, 40×, and c2 treatment group—40×, LC3 staining. Parkin- and <t>LC3-positive</t> cells marked with black arrow.
    Antibodies Against Lc3, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Histological sections of Parkin and <t>LC3</t> staining. a1—sham group, 40×, b1—control group, 40×, and c1—treatment group, 40×. Parkin staining: a2—sham group, 40×, b2—control group, 40×, and c2 treatment group—40×, LC3 staining. Parkin- and <t>LC3-positive</t> cells marked with black arrow.
    Polyclonal Antibodies Against Lc3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Histological sections of Parkin and <t>LC3</t> staining. a1—sham group, 40×, b1—control group, 40×, and c1—treatment group, 40×. Parkin staining: a2—sham group, 40×, b2—control group, 40×, and c2 treatment group—40×, LC3 staining. Parkin- and <t>LC3-positive</t> cells marked with black arrow.
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    Fig. 7 CgLRSAM1 mediated the degradation of V. splendidus through the ubiquitination-autophagy-lysosome pathway. CgLRSAM1 recognized the intra cellular bacteria through binding PAMPs, which then functioned as E3 ligase to mediate the ubiquitination of V. splendidus. The ubiquitination on bacteria could be targeted by <t>p62-LC3-mediated</t> autophagy-lysosome pathway, which eventually mediated the degradation of V. splendidus in haemocytes. The destroy of CgLRSAM1 would reduce the ubiquitination of bacteria and co-localization of V. splendidus with CgLC3 and lysosome, leading to the accumula tion of CgLC3II. This figure was drawn by Figdraw
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    Fig. 7 CgLRSAM1 mediated the degradation of V. splendidus through the ubiquitination-autophagy-lysosome pathway. CgLRSAM1 recognized the intra cellular bacteria through binding PAMPs, which then functioned as E3 ligase to mediate the ubiquitination of V. splendidus. The ubiquitination on bacteria could be targeted by <t>p62-LC3-mediated</t> autophagy-lysosome pathway, which eventually mediated the degradation of V. splendidus in haemocytes. The destroy of CgLRSAM1 would reduce the ubiquitination of bacteria and co-localization of V. splendidus with CgLC3 and lysosome, leading to the accumula tion of CgLC3II. This figure was drawn by Figdraw
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    Histological sections of Parkin and LC3 staining. a1—sham group, 40×, b1—control group, 40×, and c1—treatment group, 40×. Parkin staining: a2—sham group, 40×, b2—control group, 40×, and c2 treatment group—40×, LC3 staining. Parkin- and LC3-positive cells marked with black arrow.

    Journal: Revista da Associação Médica Brasileira

    Article Title: Enoxaparin preserves cellular morphology and modulates mitophagy-associated Parkin–LC3 in acute ischemic rat myocardium

    doi: 10.1590/1806-9282.20251136

    Figure Lengend Snippet: Histological sections of Parkin and LC3 staining. a1—sham group, 40×, b1—control group, 40×, and c1—treatment group, 40×. Parkin staining: a2—sham group, 40×, b2—control group, 40×, and c2 treatment group—40×, LC3 staining. Parkin- and LC3-positive cells marked with black arrow.

    Article Snippet: Nonspecific binding was prevented by incubation with a normal serum-blocking solution for 30 min. Next, sections were incubated overnight in a humidified chamber (30–60% humidity) with primary antibodies against LC3 (BiossUSA, LC3 Polyclonal Antibody, Cat. No: BS-4843R) and Parkin (BiossUSA, Parkin Polyclonal Antibody, Cat. No: BS-1865R).

    Techniques: Staining, Control

    Fig. 7 CgLRSAM1 mediated the degradation of V. splendidus through the ubiquitination-autophagy-lysosome pathway. CgLRSAM1 recognized the intra cellular bacteria through binding PAMPs, which then functioned as E3 ligase to mediate the ubiquitination of V. splendidus. The ubiquitination on bacteria could be targeted by p62-LC3-mediated autophagy-lysosome pathway, which eventually mediated the degradation of V. splendidus in haemocytes. The destroy of CgLRSAM1 would reduce the ubiquitination of bacteria and co-localization of V. splendidus with CgLC3 and lysosome, leading to the accumula tion of CgLC3II. This figure was drawn by Figdraw

    Journal: Cell communication and signaling : CCS

    Article Title: LRSAM1 mediated the degradation of intracellular Vibrio through the ubiquitination-autophagy-lysosome pathway in oyster.

    doi: 10.1186/s12964-025-02111-4

    Figure Lengend Snippet: Fig. 7 CgLRSAM1 mediated the degradation of V. splendidus through the ubiquitination-autophagy-lysosome pathway. CgLRSAM1 recognized the intra cellular bacteria through binding PAMPs, which then functioned as E3 ligase to mediate the ubiquitination of V. splendidus. The ubiquitination on bacteria could be targeted by p62-LC3-mediated autophagy-lysosome pathway, which eventually mediated the degradation of V. splendidus in haemocytes. The destroy of CgLRSAM1 would reduce the ubiquitination of bacteria and co-localization of V. splendidus with CgLC3 and lysosome, leading to the accumula tion of CgLC3II. This figure was drawn by Figdraw

    Article Snippet: The polyclonal antibodies against LC3 (Proteintech, USA) and beta-tubulin (Beyotime, China) were demonstrated to be specific in oysters [23], and they were employed in the present study.

    Techniques: Ubiquitin Proteomics, Bacteria, Binding Assay