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heat shock protein 60 (hsp60) sc1052 antibody  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology heat shock protein 60 (hsp60) sc1052 antibody
    Heat Shock Protein 60 (Hsp60) Sc1052 Antibody, supplied by Santa Cruz Biotechnology, 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/result/heat shock protein 60 (hsp60) sc1052 antibody/product/Santa Cruz Biotechnology
    Average 90 stars, based on 1 article reviews
    heat shock protein 60 (hsp60) sc1052 antibody - by Bioz Stars, 2026-02
    90/100 stars

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    Santa Cruz Biotechnology mouse anti heat shock protein 60 hsp60
    FIGURE 6 Mitochondrial BER. (a) Representative immunoblots of target proteins in mitochondrial extracts from cortex and hippocampus. Proteins probed for are shown on the left. APE1, apurinic/apyrimidinic endonuclease 1; <t>HSP60,</t> heat shock protein 60. (b) Representative gel from in vitro AP endonuclease activity assay with mitochondrial extracts from hippocampus. S, substrate; P, product; AP, oligonucleotide with AP site; C, control oligonucleotide without a lesion. (c–f) All values are normalized to HSP60 (mitochondrial loading control) and set relative to the sedentary group mean. Bars represent means ± SD. Differences were evaluated by Student’s unpaired t-test (c) or Mann–Whitney U-test (d–f). (c) n = 10 and 8 for sedentary and running group, respectively. (d) n = 10 and 7 for sedentary and running group, respectively. (e) n = 9 and 8 for sedentary and running group, respectively. (f) n = 7 and 9 for sedentary and running group, respectively. One outlier was excluded from the analysis in the sedentary group for (e, f). Other discrepancies in sample size are due to technical issues in assays or insufficient yield from mitochondrial purification. BER, base excision repair.
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    Proteintech heat shock protein 60
    FIGURE 6 Mitochondrial BER. (a) Representative immunoblots of target proteins in mitochondrial extracts from cortex and hippocampus. Proteins probed for are shown on the left. APE1, apurinic/apyrimidinic endonuclease 1; <t>HSP60,</t> heat shock protein 60. (b) Representative gel from in vitro AP endonuclease activity assay with mitochondrial extracts from hippocampus. S, substrate; P, product; AP, oligonucleotide with AP site; C, control oligonucleotide without a lesion. (c–f) All values are normalized to HSP60 (mitochondrial loading control) and set relative to the sedentary group mean. Bars represent means ± SD. Differences were evaluated by Student’s unpaired t-test (c) or Mann–Whitney U-test (d–f). (c) n = 10 and 8 for sedentary and running group, respectively. (d) n = 10 and 7 for sedentary and running group, respectively. (e) n = 9 and 8 for sedentary and running group, respectively. (f) n = 7 and 9 for sedentary and running group, respectively. One outlier was excluded from the analysis in the sedentary group for (e, f). Other discrepancies in sample size are due to technical issues in assays or insufficient yield from mitochondrial purification. BER, base excision repair.
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    Proteintech heat shock protein 60 (hsp60)
    FIGURE 6 Mitochondrial BER. (a) Representative immunoblots of target proteins in mitochondrial extracts from cortex and hippocampus. Proteins probed for are shown on the left. APE1, apurinic/apyrimidinic endonuclease 1; <t>HSP60,</t> heat shock protein 60. (b) Representative gel from in vitro AP endonuclease activity assay with mitochondrial extracts from hippocampus. S, substrate; P, product; AP, oligonucleotide with AP site; C, control oligonucleotide without a lesion. (c–f) All values are normalized to HSP60 (mitochondrial loading control) and set relative to the sedentary group mean. Bars represent means ± SD. Differences were evaluated by Student’s unpaired t-test (c) or Mann–Whitney U-test (d–f). (c) n = 10 and 8 for sedentary and running group, respectively. (d) n = 10 and 7 for sedentary and running group, respectively. (e) n = 9 and 8 for sedentary and running group, respectively. (f) n = 7 and 9 for sedentary and running group, respectively. One outlier was excluded from the analysis in the sedentary group for (e, f). Other discrepancies in sample size are due to technical issues in assays or insufficient yield from mitochondrial purification. BER, base excision repair.
    Heat Shock Protein 60 (Hsp60), supplied by Proteintech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology heat shock protein 60 (hsp60)
    ( A ) Representative immunofluorescence images of <t>Hsp60</t> tissue distribution in skeletal muscle of mice fed a standard diet (12 Ctrl), ethanol (12 EtOH), and ethanol plus L. fermentum LF31 (12 EtOH + P) for 12 weeks. Scale, 25 µm bar. ( B ) Enhanced magnification of the images shown in ( A ). ( C ) ELISA assays of Hsp60 on whole murine model hindlimb muscle lysates after 8 and 12 weeks of treatment. The analysis was conducted on six mice in each group. Data are presented as the mean ± SD.
    Heat Shock Protein 60 (Hsp60), supplied by Santa Cruz Biotechnology, 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/result/heat shock protein 60 (hsp60)/product/Santa Cruz Biotechnology
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    Image Search Results


    FIGURE 6 Mitochondrial BER. (a) Representative immunoblots of target proteins in mitochondrial extracts from cortex and hippocampus. Proteins probed for are shown on the left. APE1, apurinic/apyrimidinic endonuclease 1; HSP60, heat shock protein 60. (b) Representative gel from in vitro AP endonuclease activity assay with mitochondrial extracts from hippocampus. S, substrate; P, product; AP, oligonucleotide with AP site; C, control oligonucleotide without a lesion. (c–f) All values are normalized to HSP60 (mitochondrial loading control) and set relative to the sedentary group mean. Bars represent means ± SD. Differences were evaluated by Student’s unpaired t-test (c) or Mann–Whitney U-test (d–f). (c) n = 10 and 8 for sedentary and running group, respectively. (d) n = 10 and 7 for sedentary and running group, respectively. (e) n = 9 and 8 for sedentary and running group, respectively. (f) n = 7 and 9 for sedentary and running group, respectively. One outlier was excluded from the analysis in the sedentary group for (e, f). Other discrepancies in sample size are due to technical issues in assays or insufficient yield from mitochondrial purification. BER, base excision repair.

    Journal: Experimental Physiology

    Article Title: Effect of prolonged voluntary wheel running on oxidative stress and defence mechanisms in cortex and hippocampus of healthy female rats

    doi: 10.1113/ep092815

    Figure Lengend Snippet: FIGURE 6 Mitochondrial BER. (a) Representative immunoblots of target proteins in mitochondrial extracts from cortex and hippocampus. Proteins probed for are shown on the left. APE1, apurinic/apyrimidinic endonuclease 1; HSP60, heat shock protein 60. (b) Representative gel from in vitro AP endonuclease activity assay with mitochondrial extracts from hippocampus. S, substrate; P, product; AP, oligonucleotide with AP site; C, control oligonucleotide without a lesion. (c–f) All values are normalized to HSP60 (mitochondrial loading control) and set relative to the sedentary group mean. Bars represent means ± SD. Differences were evaluated by Student’s unpaired t-test (c) or Mann–Whitney U-test (d–f). (c) n = 10 and 8 for sedentary and running group, respectively. (d) n = 10 and 7 for sedentary and running group, respectively. (e) n = 9 and 8 for sedentary and running group, respectively. (f) n = 7 and 9 for sedentary and running group, respectively. One outlier was excluded from the analysis in the sedentary group for (e, f). Other discrepancies in sample size are due to technical issues in assays or insufficient yield from mitochondrial purification. BER, base excision repair.

    Article Snippet: anti-8-oxoguanine DNA glycosylase 1 (OGG1) (Novus Biologicals, cat. no. NB100-106, 1:500, RRID: AB_10104097), mouse anti-superoxide dismutase 1 (SOD1) (Santa Cruz Biotechnology, Dallas, TX, USA, cat. no. sc-101523, 1:500, RRID: AB_2191632), mouse anti-superoxide dismutase 2 (SOD2) (Santa Cruz Biotechnology, cat. no. sc-137254, 1:200, RRID: AB_2191808), mouse anti-catalase (CAT) (Santa Cruz Biotechnology, cat. no. sc-271803, 1:500, RRID: AB_10708550), mouse anti-heat shock protein 60 (HSP60) (Santa Cruz Biotechnology, cat. no. sc-271215, 1:1000, RRID: AB_10607973), and mouse antiβ-actin (Sigma-Aldrich, St Louis, MO, USA, cat. no. A2228, 1:10,000, RRID: 476697).

    Techniques: Western Blot, In Vitro, Activity Assay, Control, MANN-WHITNEY, Purification

    ( A ) Representative immunofluorescence images of Hsp60 tissue distribution in skeletal muscle of mice fed a standard diet (12 Ctrl), ethanol (12 EtOH), and ethanol plus L. fermentum LF31 (12 EtOH + P) for 12 weeks. Scale, 25 µm bar. ( B ) Enhanced magnification of the images shown in ( A ). ( C ) ELISA assays of Hsp60 on whole murine model hindlimb muscle lysates after 8 and 12 weeks of treatment. The analysis was conducted on six mice in each group. Data are presented as the mean ± SD.

    Journal: Nutrients

    Article Title: Lactobacillus fermentum LF31 Supplementation Reversed Atrophy Fibers in a Model of Myopathy Through the Modulation of IL-6, TNF-α, and Hsp60 Levels Enhancing Muscle Regeneration

    doi: 10.3390/nu17091550

    Figure Lengend Snippet: ( A ) Representative immunofluorescence images of Hsp60 tissue distribution in skeletal muscle of mice fed a standard diet (12 Ctrl), ethanol (12 EtOH), and ethanol plus L. fermentum LF31 (12 EtOH + P) for 12 weeks. Scale, 25 µm bar. ( B ) Enhanced magnification of the images shown in ( A ). ( C ) ELISA assays of Hsp60 on whole murine model hindlimb muscle lysates after 8 and 12 weeks of treatment. The analysis was conducted on six mice in each group. Data are presented as the mean ± SD.

    Article Snippet: Heat Shock Protein 60 (Hsp60) , Sc-1722 Goat Polyclonal Santa Cruz, CA, USA , - , 1:50 , -.

    Techniques: Immunofluorescence, Enzyme-linked Immunosorbent Assay

    Working hypothesis. ( A ) Chronic alcohol consumption leads to an increase in circulating reactive oxygen species (ROS) and, locally, to an increase in the mitochondrial protein Hsp60. Hsp60, in the presence of oxidative stress, could translocate from the mitochondria to the cytoplasm via a voltage-dependent anion channel located on the mitochondrial membrane and interact directly with IκB. The dissociation of IκB from NF-κB would induce the phosphorylation of NF-κB (pNF-κB) and its translocation to the nuclear level, where it could induce the expression of inflammatory cytokines, including TNF-α, IL-6, and IL-10, as well as the reduction of the expression of markers responsible for mechanisms of muscle regeneration and differentiation, such as Pax7 and MyoD. These events would be responsible for the atrophy of muscle fibers found in animals treated with alcohol for 8 and 12 weeks. ( B ) The potential effects of L. fermentum may involve modulation of the NF-κB signaling pathway . The probiotic L. fermentum , through the production of the antioxidant glutathione, could induce the reduction of local Hsp60 levels as a protective mechanism against oxidative stress. In this way, Hsp60 would not be exported from the mitochondria to the cytoplasm and would not interact with IκB. NF-κB would therefore remain associated with IκB in an inactive complex and could not activate the expression of inflammatory cytokines. Consequently, the negative effects of alcohol-induced damage, such as the reduction of markers of muscle regeneration and differentiation (Pax7 and MyoD) at the muscle level, may be enhanced. These phenomena would contribute to counteract the atrophy of skeletal muscle fibers induced by chronic EtOH consumption, suggesting a possible protective role of the probiotic L. fermentum .

    Journal: Nutrients

    Article Title: Lactobacillus fermentum LF31 Supplementation Reversed Atrophy Fibers in a Model of Myopathy Through the Modulation of IL-6, TNF-α, and Hsp60 Levels Enhancing Muscle Regeneration

    doi: 10.3390/nu17091550

    Figure Lengend Snippet: Working hypothesis. ( A ) Chronic alcohol consumption leads to an increase in circulating reactive oxygen species (ROS) and, locally, to an increase in the mitochondrial protein Hsp60. Hsp60, in the presence of oxidative stress, could translocate from the mitochondria to the cytoplasm via a voltage-dependent anion channel located on the mitochondrial membrane and interact directly with IκB. The dissociation of IκB from NF-κB would induce the phosphorylation of NF-κB (pNF-κB) and its translocation to the nuclear level, where it could induce the expression of inflammatory cytokines, including TNF-α, IL-6, and IL-10, as well as the reduction of the expression of markers responsible for mechanisms of muscle regeneration and differentiation, such as Pax7 and MyoD. These events would be responsible for the atrophy of muscle fibers found in animals treated with alcohol for 8 and 12 weeks. ( B ) The potential effects of L. fermentum may involve modulation of the NF-κB signaling pathway . The probiotic L. fermentum , through the production of the antioxidant glutathione, could induce the reduction of local Hsp60 levels as a protective mechanism against oxidative stress. In this way, Hsp60 would not be exported from the mitochondria to the cytoplasm and would not interact with IκB. NF-κB would therefore remain associated with IκB in an inactive complex and could not activate the expression of inflammatory cytokines. Consequently, the negative effects of alcohol-induced damage, such as the reduction of markers of muscle regeneration and differentiation (Pax7 and MyoD) at the muscle level, may be enhanced. These phenomena would contribute to counteract the atrophy of skeletal muscle fibers induced by chronic EtOH consumption, suggesting a possible protective role of the probiotic L. fermentum .

    Article Snippet: Heat Shock Protein 60 (Hsp60) , Sc-1722 Goat Polyclonal Santa Cruz, CA, USA , - , 1:50 , -.

    Techniques: Membrane, Phospho-proteomics, Translocation Assay, Expressing