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polyclonal antibodies against lc3  (Proteintech)


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    Proteintech polyclonal antibodies against lc3
    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
    Polyclonal Antibodies Against Lc3, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1725 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal antibodies against lc3/product/Proteintech
    Average 96 stars, based on 1725 article reviews
    polyclonal antibodies against lc3 - by Bioz Stars, 2026-03
    96/100 stars

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    1) Product Images from "LRSAM1 mediated the degradation of intracellular Vibrio through the ubiquitination-autophagy-lysosome pathway in oyster."

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

    Journal: Cell communication and signaling : CCS

    doi: 10.1186/s12964-025-02111-4

    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
    Figure Legend 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

    Techniques Used: Ubiquitin Proteomics, Bacteria, Binding Assay



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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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    Image Search Results


    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