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rabbit polyclonal fkrp  (R&D Systems)


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    R&D Systems rabbit polyclonal fkrp
    Rabbit Polyclonal Fkrp, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+hsp60+antibody/Human%2FMouse%2FRat+HSP60+Antibody/pm37919902-230-0-6
    Average 93 stars, based on 11 article reviews
    rabbit polyclonal fkrp - by Bioz Stars, 2026-10
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    Article Title: Differential Subcellular Distribution and Translocation of Seven 14-3-3 Isoforms in Response to EGF and During the Cell Cycle
    Article Snippet: Rabbit polyclonal anti-HSP60 antibody was purchased from R&D Systems (Minneapolis, MN, USA).

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    Article Title: Differential Subcellular Distribution and Translocation of Seven 14-3-3 Isoforms in Response to EGF and During the Cell Cycle
    Article Snippet: Rabbit polyclonal anti-HSP60 antibody was purchased from R&D Systems (Minneapolis, MN, USA).



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    (A) HSF1-/- cells exhibit reduced expression of heat shock inducible Hsps. WT and HSF1-/- MEF cells were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Hsp90, Grp78, Hsc/Hsp70, <t>Hsp60,</t> Hsp40, and Hsp27 were detected by Western blot analysis with their specific antibodies. (B, C) Hsp70 participates in UPS-dependent Arc/Arg3.1 degradation. HSF1-/- MEF cells overexpressing Flag-Hsp70 were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Flag-Hsp70 and Arc/Arg3.1 were detected by Western blot analysis using their specific antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (C). (D) Hsp70 interacts with Arc/Arg3.1. HEK293T cells were transfected with GFP-Hsp70 and Flag empty vector or Flag-Arc, and the cell lysates were immunoprecipitated using an anti-Flag antibody. The immune complex was analyzed by Western analysis using anti-GFP and anti-Flag antibodies. (E) Arc/Arg3.1 primarly binds to Hsc/Hsp70. Following transfection of HEK293T cells with either Flag empty vector or Flag-Arc, the whole cell lysates were immunoprecipitated using an anti-Flag antibody. Western analysis using anti-Hsc/Hsp70, anti-Hsp40, and anti-Hsp27 antibodies was used to examine the immunological complex. * was an antibody’s light chain. (F, G) CHIP induces Arc/Arg3.1 degradation by interacting with Hsp70. HEK293T cells overexpressing Flag-Arc, GFP-Hsp70, and His-ubiquitin were co-transfected with HA-CHIP WT or mutants. Cells were analyzed by Western blot with anti-Flag, anti-HA, and anti-GFP antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (G). Data are presented as the mean ± S.D. of triplicated experiments (t-test; # < 0.01, **P < 0.001, *** < 0.0001). (H) Arc/Arg3.1 proteins are stabilized by CHIP knockdown. After being depleted of either control or CHIP, MEF cells were exposed to heat shock at 45°C for 15 min and then allowed to recover at 37°C for 9 h.
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    polyclonal rabbit anti hsp60 antibody  (Novus Biologicals)
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    (A) HSF1-/- cells exhibit reduced expression of heat shock inducible Hsps. WT and HSF1-/- MEF cells were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Hsp90, Grp78, Hsc/Hsp70, <t>Hsp60,</t> Hsp40, and Hsp27 were detected by Western blot analysis with their specific antibodies. (B, C) Hsp70 participates in UPS-dependent Arc/Arg3.1 degradation. HSF1-/- MEF cells overexpressing Flag-Hsp70 were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Flag-Hsp70 and Arc/Arg3.1 were detected by Western blot analysis using their specific antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (C). (D) Hsp70 interacts with Arc/Arg3.1. HEK293T cells were transfected with GFP-Hsp70 and Flag empty vector or Flag-Arc, and the cell lysates were immunoprecipitated using an anti-Flag antibody. The immune complex was analyzed by Western analysis using anti-GFP and anti-Flag antibodies. (E) Arc/Arg3.1 primarly binds to Hsc/Hsp70. Following transfection of HEK293T cells with either Flag empty vector or Flag-Arc, the whole cell lysates were immunoprecipitated using an anti-Flag antibody. Western analysis using anti-Hsc/Hsp70, anti-Hsp40, and anti-Hsp27 antibodies was used to examine the immunological complex. * was an antibody’s light chain. (F, G) CHIP induces Arc/Arg3.1 degradation by interacting with Hsp70. HEK293T cells overexpressing Flag-Arc, GFP-Hsp70, and His-ubiquitin were co-transfected with HA-CHIP WT or mutants. Cells were analyzed by Western blot with anti-Flag, anti-HA, and anti-GFP antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (G). Data are presented as the mean ± S.D. of triplicated experiments (t-test; # < 0.01, **P < 0.001, *** < 0.0001). (H) Arc/Arg3.1 proteins are stabilized by CHIP knockdown. After being depleted of either control or CHIP, MEF cells were exposed to heat shock at 45°C for 15 min and then allowed to recover at 37°C for 9 h.
    Polyclonal Rabbit Anti Hsp60 Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit polyclonal antibody against hsp60  (Cell Signaling Technology Inc)
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    (A) HSF1-/- cells exhibit reduced expression of heat shock inducible Hsps. WT and HSF1-/- MEF cells were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Hsp90, Grp78, Hsc/Hsp70, <t>Hsp60,</t> Hsp40, and Hsp27 were detected by Western blot analysis with their specific antibodies. (B, C) Hsp70 participates in UPS-dependent Arc/Arg3.1 degradation. HSF1-/- MEF cells overexpressing Flag-Hsp70 were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Flag-Hsp70 and Arc/Arg3.1 were detected by Western blot analysis using their specific antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (C). (D) Hsp70 interacts with Arc/Arg3.1. HEK293T cells were transfected with GFP-Hsp70 and Flag empty vector or Flag-Arc, and the cell lysates were immunoprecipitated using an anti-Flag antibody. The immune complex was analyzed by Western analysis using anti-GFP and anti-Flag antibodies. (E) Arc/Arg3.1 primarly binds to Hsc/Hsp70. Following transfection of HEK293T cells with either Flag empty vector or Flag-Arc, the whole cell lysates were immunoprecipitated using an anti-Flag antibody. Western analysis using anti-Hsc/Hsp70, anti-Hsp40, and anti-Hsp27 antibodies was used to examine the immunological complex. * was an antibody’s light chain. (F, G) CHIP induces Arc/Arg3.1 degradation by interacting with Hsp70. HEK293T cells overexpressing Flag-Arc, GFP-Hsp70, and His-ubiquitin were co-transfected with HA-CHIP WT or mutants. Cells were analyzed by Western blot with anti-Flag, anti-HA, and anti-GFP antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (G). Data are presented as the mean ± S.D. of triplicated experiments (t-test; # < 0.01, **P < 0.001, *** < 0.0001). (H) Arc/Arg3.1 proteins are stabilized by CHIP knockdown. After being depleted of either control or CHIP, MEF cells were exposed to heat shock at 45°C for 15 min and then allowed to recover at 37°C for 9 h.
    Rabbit Polyclonal Antibody Against Hsp60, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (A) HSF1-/- cells exhibit reduced expression of heat shock inducible Hsps. WT and HSF1-/- MEF cells were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Hsp90, Grp78, Hsc/Hsp70, <t>Hsp60,</t> Hsp40, and Hsp27 were detected by Western blot analysis with their specific antibodies. (B, C) Hsp70 participates in UPS-dependent Arc/Arg3.1 degradation. HSF1-/- MEF cells overexpressing Flag-Hsp70 were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Flag-Hsp70 and Arc/Arg3.1 were detected by Western blot analysis using their specific antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (C). (D) Hsp70 interacts with Arc/Arg3.1. HEK293T cells were transfected with GFP-Hsp70 and Flag empty vector or Flag-Arc, and the cell lysates were immunoprecipitated using an anti-Flag antibody. The immune complex was analyzed by Western analysis using anti-GFP and anti-Flag antibodies. (E) Arc/Arg3.1 primarly binds to Hsc/Hsp70. Following transfection of HEK293T cells with either Flag empty vector or Flag-Arc, the whole cell lysates were immunoprecipitated using an anti-Flag antibody. Western analysis using anti-Hsc/Hsp70, anti-Hsp40, and anti-Hsp27 antibodies was used to examine the immunological complex. * was an antibody’s light chain. (F, G) CHIP induces Arc/Arg3.1 degradation by interacting with Hsp70. HEK293T cells overexpressing Flag-Arc, GFP-Hsp70, and His-ubiquitin were co-transfected with HA-CHIP WT or mutants. Cells were analyzed by Western blot with anti-Flag, anti-HA, and anti-GFP antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (G). Data are presented as the mean ± S.D. of triplicated experiments (t-test; # < 0.01, **P < 0.001, *** < 0.0001). (H) Arc/Arg3.1 proteins are stabilized by CHIP knockdown. After being depleted of either control or CHIP, MEF cells were exposed to heat shock at 45°C for 15 min and then allowed to recover at 37°C for 9 h.
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    (A) HSF1-/- cells exhibit reduced expression of heat shock inducible Hsps. WT and HSF1-/- MEF cells were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Hsp90, Grp78, Hsc/Hsp70, <t>Hsp60,</t> Hsp40, and Hsp27 were detected by Western blot analysis with their specific antibodies. (B, C) Hsp70 participates in UPS-dependent Arc/Arg3.1 degradation. HSF1-/- MEF cells overexpressing Flag-Hsp70 were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Flag-Hsp70 and Arc/Arg3.1 were detected by Western blot analysis using their specific antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (C). (D) Hsp70 interacts with Arc/Arg3.1. HEK293T cells were transfected with GFP-Hsp70 and Flag empty vector or Flag-Arc, and the cell lysates were immunoprecipitated using an anti-Flag antibody. The immune complex was analyzed by Western analysis using anti-GFP and anti-Flag antibodies. (E) Arc/Arg3.1 primarly binds to Hsc/Hsp70. Following transfection of HEK293T cells with either Flag empty vector or Flag-Arc, the whole cell lysates were immunoprecipitated using an anti-Flag antibody. Western analysis using anti-Hsc/Hsp70, anti-Hsp40, and anti-Hsp27 antibodies was used to examine the immunological complex. * was an antibody’s light chain. (F, G) CHIP induces Arc/Arg3.1 degradation by interacting with Hsp70. HEK293T cells overexpressing Flag-Arc, GFP-Hsp70, and His-ubiquitin were co-transfected with HA-CHIP WT or mutants. Cells were analyzed by Western blot with anti-Flag, anti-HA, and anti-GFP antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (G). Data are presented as the mean ± S.D. of triplicated experiments (t-test; # < 0.01, **P < 0.001, *** < 0.0001). (H) Arc/Arg3.1 proteins are stabilized by CHIP knockdown. After being depleted of either control or CHIP, MEF cells were exposed to heat shock at 45°C for 15 min and then allowed to recover at 37°C for 9 h.
    3724s Goat Anti Hsp60 Santa Cruz Sc 1052 Donkey Anti Mouse Igg Polyclonal Antibody, 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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    rabbit polyclonal anti hsp60  (Proteintech)
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    (A) HSF1-/- cells exhibit reduced expression of heat shock inducible Hsps. WT and HSF1-/- MEF cells were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Hsp90, Grp78, Hsc/Hsp70, <t>Hsp60,</t> Hsp40, and Hsp27 were detected by Western blot analysis with their specific antibodies. (B, C) Hsp70 participates in UPS-dependent Arc/Arg3.1 degradation. HSF1-/- MEF cells overexpressing Flag-Hsp70 were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Flag-Hsp70 and Arc/Arg3.1 were detected by Western blot analysis using their specific antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (C). (D) Hsp70 interacts with Arc/Arg3.1. HEK293T cells were transfected with GFP-Hsp70 and Flag empty vector or Flag-Arc, and the cell lysates were immunoprecipitated using an anti-Flag antibody. The immune complex was analyzed by Western analysis using anti-GFP and anti-Flag antibodies. (E) Arc/Arg3.1 primarly binds to Hsc/Hsp70. Following transfection of HEK293T cells with either Flag empty vector or Flag-Arc, the whole cell lysates were immunoprecipitated using an anti-Flag antibody. Western analysis using anti-Hsc/Hsp70, anti-Hsp40, and anti-Hsp27 antibodies was used to examine the immunological complex. * was an antibody’s light chain. (F, G) CHIP induces Arc/Arg3.1 degradation by interacting with Hsp70. HEK293T cells overexpressing Flag-Arc, GFP-Hsp70, and His-ubiquitin were co-transfected with HA-CHIP WT or mutants. Cells were analyzed by Western blot with anti-Flag, anti-HA, and anti-GFP antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (G). Data are presented as the mean ± S.D. of triplicated experiments (t-test; # < 0.01, **P < 0.001, *** < 0.0001). (H) Arc/Arg3.1 proteins are stabilized by CHIP knockdown. After being depleted of either control or CHIP, MEF cells were exposed to heat shock at 45°C for 15 min and then allowed to recover at 37°C for 9 h.
    Rabbit Polyclonal Anti Hsp60, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit polyclonal fkrp  (R&D Systems)
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    (A) HSF1-/- cells exhibit reduced expression of heat shock inducible Hsps. WT and HSF1-/- MEF cells were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Hsp90, Grp78, Hsc/Hsp70, <t>Hsp60,</t> Hsp40, and Hsp27 were detected by Western blot analysis with their specific antibodies. (B, C) Hsp70 participates in UPS-dependent Arc/Arg3.1 degradation. HSF1-/- MEF cells overexpressing Flag-Hsp70 were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Flag-Hsp70 and Arc/Arg3.1 were detected by Western blot analysis using their specific antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (C). (D) Hsp70 interacts with Arc/Arg3.1. HEK293T cells were transfected with GFP-Hsp70 and Flag empty vector or Flag-Arc, and the cell lysates were immunoprecipitated using an anti-Flag antibody. The immune complex was analyzed by Western analysis using anti-GFP and anti-Flag antibodies. (E) Arc/Arg3.1 primarly binds to Hsc/Hsp70. Following transfection of HEK293T cells with either Flag empty vector or Flag-Arc, the whole cell lysates were immunoprecipitated using an anti-Flag antibody. Western analysis using anti-Hsc/Hsp70, anti-Hsp40, and anti-Hsp27 antibodies was used to examine the immunological complex. * was an antibody’s light chain. (F, G) CHIP induces Arc/Arg3.1 degradation by interacting with Hsp70. HEK293T cells overexpressing Flag-Arc, GFP-Hsp70, and His-ubiquitin were co-transfected with HA-CHIP WT or mutants. Cells were analyzed by Western blot with anti-Flag, anti-HA, and anti-GFP antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (G). Data are presented as the mean ± S.D. of triplicated experiments (t-test; # < 0.01, **P < 0.001, *** < 0.0001). (H) Arc/Arg3.1 proteins are stabilized by CHIP knockdown. After being depleted of either control or CHIP, MEF cells were exposed to heat shock at 45°C for 15 min and then allowed to recover at 37°C for 9 h.
    Rabbit Polyclonal Fkrp, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit polyclonal anti hsp60 antibody  (ABclonal Biotechnology)
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    Figure 3. PrP106–126 triggers PINK1/Parkin-dependent mitophagy. (A) Cortical neurons were treated with PrP106–126 for the indicated periods, and then, the protein levels of PINK1 and Parkin were analyzed by Western blotting. (B) Proteins of cytoplasm and mitochondria in PrP106–126-treated neurons and control neurons were extracted, respectively, and the protein levels of PINK1, Parkin, and LC3B-II were analyzed using Western blotting; <t>HSP60</t> (the mitochondrial matrix protein) served as loading control. (C) The colocalization between mitochondria (labeled with mito-DesRed, red) and Parkin (green) in cortical neurons was observed using immunofluorescence imaging (nuclei, blue).
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    hsp60 rabbit polyclonal d307  (Cell Signaling Technology Inc)
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    Figure 3. PrP106–126 triggers PINK1/Parkin-dependent mitophagy. (A) Cortical neurons were treated with PrP106–126 for the indicated periods, and then, the protein levels of PINK1 and Parkin were analyzed by Western blotting. (B) Proteins of cytoplasm and mitochondria in PrP106–126-treated neurons and control neurons were extracted, respectively, and the protein levels of PINK1, Parkin, and LC3B-II were analyzed using Western blotting; <t>HSP60</t> (the mitochondrial matrix protein) served as loading control. (C) The colocalization between mitochondria (labeled with mito-DesRed, red) and Parkin (green) in cortical neurons was observed using immunofluorescence imaging (nuclei, blue).
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    (A) HSF1-/- cells exhibit reduced expression of heat shock inducible Hsps. WT and HSF1-/- MEF cells were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Hsp90, Grp78, Hsc/Hsp70, Hsp60, Hsp40, and Hsp27 were detected by Western blot analysis with their specific antibodies. (B, C) Hsp70 participates in UPS-dependent Arc/Arg3.1 degradation. HSF1-/- MEF cells overexpressing Flag-Hsp70 were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Flag-Hsp70 and Arc/Arg3.1 were detected by Western blot analysis using their specific antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (C). (D) Hsp70 interacts with Arc/Arg3.1. HEK293T cells were transfected with GFP-Hsp70 and Flag empty vector or Flag-Arc, and the cell lysates were immunoprecipitated using an anti-Flag antibody. The immune complex was analyzed by Western analysis using anti-GFP and anti-Flag antibodies. (E) Arc/Arg3.1 primarly binds to Hsc/Hsp70. Following transfection of HEK293T cells with either Flag empty vector or Flag-Arc, the whole cell lysates were immunoprecipitated using an anti-Flag antibody. Western analysis using anti-Hsc/Hsp70, anti-Hsp40, and anti-Hsp27 antibodies was used to examine the immunological complex. * was an antibody’s light chain. (F, G) CHIP induces Arc/Arg3.1 degradation by interacting with Hsp70. HEK293T cells overexpressing Flag-Arc, GFP-Hsp70, and His-ubiquitin were co-transfected with HA-CHIP WT or mutants. Cells were analyzed by Western blot with anti-Flag, anti-HA, and anti-GFP antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (G). Data are presented as the mean ± S.D. of triplicated experiments (t-test; # < 0.01, **P < 0.001, *** < 0.0001). (H) Arc/Arg3.1 proteins are stabilized by CHIP knockdown. After being depleted of either control or CHIP, MEF cells were exposed to heat shock at 45°C for 15 min and then allowed to recover at 37°C for 9 h.

    Journal: bioRxiv

    Article Title: Disulfide Crosslinking Induces Rapid Degradation of Arc/Arg3.1 via Hsp70-Mediated Ubiquitin Ligase Pathway

    doi: 10.1101/2025.07.20.665809

    Figure Lengend Snippet: (A) HSF1-/- cells exhibit reduced expression of heat shock inducible Hsps. WT and HSF1-/- MEF cells were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Hsp90, Grp78, Hsc/Hsp70, Hsp60, Hsp40, and Hsp27 were detected by Western blot analysis with their specific antibodies. (B, C) Hsp70 participates in UPS-dependent Arc/Arg3.1 degradation. HSF1-/- MEF cells overexpressing Flag-Hsp70 were exposed to heat shock at 45 °C for 15 min and allowed to recover at 37 °C for the indicated times. Flag-Hsp70 and Arc/Arg3.1 were detected by Western blot analysis using their specific antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (C). (D) Hsp70 interacts with Arc/Arg3.1. HEK293T cells were transfected with GFP-Hsp70 and Flag empty vector or Flag-Arc, and the cell lysates were immunoprecipitated using an anti-Flag antibody. The immune complex was analyzed by Western analysis using anti-GFP and anti-Flag antibodies. (E) Arc/Arg3.1 primarly binds to Hsc/Hsp70. Following transfection of HEK293T cells with either Flag empty vector or Flag-Arc, the whole cell lysates were immunoprecipitated using an anti-Flag antibody. Western analysis using anti-Hsc/Hsp70, anti-Hsp40, and anti-Hsp27 antibodies was used to examine the immunological complex. * was an antibody’s light chain. (F, G) CHIP induces Arc/Arg3.1 degradation by interacting with Hsp70. HEK293T cells overexpressing Flag-Arc, GFP-Hsp70, and His-ubiquitin were co-transfected with HA-CHIP WT or mutants. Cells were analyzed by Western blot with anti-Flag, anti-HA, and anti-GFP antibodies. Representative Western results were selected from triplicated experiments. Quantified results of triplicated Western images are shown in (G). Data are presented as the mean ± S.D. of triplicated experiments (t-test; # < 0.01, **P < 0.001, *** < 0.0001). (H) Arc/Arg3.1 proteins are stabilized by CHIP knockdown. After being depleted of either control or CHIP, MEF cells were exposed to heat shock at 45°C for 15 min and then allowed to recover at 37°C for 9 h.

    Article Snippet: Mouse monoclonal Arc antibody (E-7) (sc-55475), mouse monoclonal Arc antibody (C-7) (sc-17839), mouse monoclonal anti-β-Actin (C4) (sc-47778), mouse monoclonal HSP27 antibody (sc-13132), and mouse monoclonal α-tubulin antibody (sc-8035) were purchased from Santa Cruz: Rabbit polyclonal GAPDH antibody (LF-PA0018) and mouse monoclonal HA antibody (LF7H5) (LF-MA0048) from Ab Frontier: Mouse monoclonal Hsc/Hsp70 antibody (ADI-SPA-820) and mouse monoclonal HSF1 antibody (ADI-SPA-901) from Enzo: Mouse monoclonal FLAG antibody (F3165) from Sigma Aldrich: Mouse monoclonal GFP antibody (A-11120) from Invitrogen: Streptavidin-HRP (3999), rabbit monoclonal BiP antibody (C50B12) (3177), and rabbit polyclonal Hsp40 antibody (4868) from Cell signaling: Mouse monoclonal Hsp90 antibody (ab13492), rabbit polyclonal Hsp60 antibody (ab13492), and rabbit polyclonal Hsp60 antibody (ab46798) from Abcam: Goat mouse IgG-HRP conjugate antibody (170–5047) and goat rabbit IgG-HRP conjugate antibody (170–6515) from Bio-Rad.

    Techniques: Expressing, Western Blot, Transfection, Plasmid Preparation, Immunoprecipitation, Ubiquitin Proteomics, Knockdown, Control

    Figure 3. PrP106–126 triggers PINK1/Parkin-dependent mitophagy. (A) Cortical neurons were treated with PrP106–126 for the indicated periods, and then, the protein levels of PINK1 and Parkin were analyzed by Western blotting. (B) Proteins of cytoplasm and mitochondria in PrP106–126-treated neurons and control neurons were extracted, respectively, and the protein levels of PINK1, Parkin, and LC3B-II were analyzed using Western blotting; HSP60 (the mitochondrial matrix protein) served as loading control. (C) The colocalization between mitochondria (labeled with mito-DesRed, red) and Parkin (green) in cortical neurons was observed using immunofluorescence imaging (nuclei, blue).

    Journal: International journal of molecular sciences

    Article Title: PHB2 Alleviates Neurotoxicity of Prion Peptide PrP 106-126 via PINK1/Parkin-Dependent Mitophagy.

    doi: 10.3390/ijms242115919

    Figure Lengend Snippet: Figure 3. PrP106–126 triggers PINK1/Parkin-dependent mitophagy. (A) Cortical neurons were treated with PrP106–126 for the indicated periods, and then, the protein levels of PINK1 and Parkin were analyzed by Western blotting. (B) Proteins of cytoplasm and mitochondria in PrP106–126-treated neurons and control neurons were extracted, respectively, and the protein levels of PINK1, Parkin, and LC3B-II were analyzed using Western blotting; HSP60 (the mitochondrial matrix protein) served as loading control. (C) The colocalization between mitochondria (labeled with mito-DesRed, red) and Parkin (green) in cortical neurons was observed using immunofluorescence imaging (nuclei, blue).

    Article Snippet: Rabbit polyclonal anti-HSP60 antibody (A0969), rabbit polyclonal anti-PINK1 antibody (A7131), and mouse monoclonal anti-TOMM20 antibody (A19403) were obtained from ABclonal Technology (Wuhan, China).

    Techniques: Western Blot, Control, Labeling, Imaging

    Figure 5. PHB2 is required for PINK1/Parkin-mediated mitophagy in PrP106–126-treated neu- rons. (A) Western blotting of PINK1 and Parkin proteins in mitochondria of PHB2-overexpression and PHB2-knockdown neurons with the PrP106–126 treatments (HSP60 served as loading control). (B) The colocalization between mitochondria (labeled with HSP60, red) and Parkin (green) in PHB2- knockdown and PHB2-overexpression neurons under the PrP106–126 treatment was observed using immunofluorescence imaging (nuclei, blue).

    Journal: International journal of molecular sciences

    Article Title: PHB2 Alleviates Neurotoxicity of Prion Peptide PrP 106-126 via PINK1/Parkin-Dependent Mitophagy.

    doi: 10.3390/ijms242115919

    Figure Lengend Snippet: Figure 5. PHB2 is required for PINK1/Parkin-mediated mitophagy in PrP106–126-treated neu- rons. (A) Western blotting of PINK1 and Parkin proteins in mitochondria of PHB2-overexpression and PHB2-knockdown neurons with the PrP106–126 treatments (HSP60 served as loading control). (B) The colocalization between mitochondria (labeled with HSP60, red) and Parkin (green) in PHB2- knockdown and PHB2-overexpression neurons under the PrP106–126 treatment was observed using immunofluorescence imaging (nuclei, blue).

    Article Snippet: Rabbit polyclonal anti-HSP60 antibody (A0969), rabbit polyclonal anti-PINK1 antibody (A7131), and mouse monoclonal anti-TOMM20 antibody (A19403) were obtained from ABclonal Technology (Wuhan, China).

    Techniques: Western Blot, Over Expression, Knockdown, Control, Labeling, Imaging