mouse monoclonal igg antibody to hsp60  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc mouse monoclonal igg antibody to hsp60
    BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and <t>Hsp60</t> were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.
    Mouse Monoclonal Igg Antibody To Hsp60, supplied by Cell Signaling Technology Inc, 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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    Images

    1) Product Images from "Pro-apoptotic activity of α-bisabolol in preclinical models of primary human acute leukemia cells"

    Article Title: Pro-apoptotic activity of α-bisabolol in preclinical models of primary human acute leukemia cells

    Journal: Journal of Translational Medicine

    doi: 10.1186/1479-5876-9-45

    BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and Hsp60 were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.
    Figure Legend Snippet: BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and Hsp60 were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.

    Techniques Used: Concentration Assay, Positive Control, Translocation Assay, Incubation, Modification

    mouse monoclonal igg antibody to hsp60  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc mouse monoclonal igg antibody to hsp60
    BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and <t>Hsp60</t> were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.
    Mouse Monoclonal Igg Antibody To Hsp60, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse monoclonal igg antibody to hsp60/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
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    mouse monoclonal igg antibody to hsp60 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Pro-apoptotic activity of α-bisabolol in preclinical models of primary human acute leukemia cells"

    Article Title: Pro-apoptotic activity of α-bisabolol in preclinical models of primary human acute leukemia cells

    Journal: Journal of Translational Medicine

    doi: 10.1186/1479-5876-9-45

    BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and Hsp60 were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.
    Figure Legend Snippet: BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and Hsp60 were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.

    Techniques Used: Concentration Assay, Positive Control, Translocation Assay, Incubation, Modification

    hsp60  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc hsp60
    Hsp60, supplied by Cell Signaling Technology Inc, 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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    hsp60 d6f1 xp rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc hsp60 d6f1 xp rabbit mab
    Hsp60 D6f1 Xp Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hsp60 d6f1 xp rabbit mab/product/Cell Signaling Technology Inc
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    hsp60  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc hsp60
    SHED-CM suppresses SOD1 G85R -induced ER stress and increases HSP70 levels. (A) : N2a cells expressing mCherry-SOD1G85R were treated with SHED-CM (30%, 50%, and 70%) for 24 h. Subsequently, immunoblot analysis of Bip and Chop was conducted in relation to ER stress. (B and C) : Densitometric quantification of Bip and Chop. ### p < 0.001 vs. WT; *** p < 0.001, ** p < 0.01, and * p < 0.05 vs. G85R. (D) : Immunoblot analysis of <t>HSP60,</t> HSP70, and HSP90. (E–G) : Densitometric quantification of HSP60, HSP70, and HSP90. Results are presented as means ± SEM of three independent experiments based on the fluorescence intensity of the “mock” (mock = 1). *** p < 0.001, ** p < 0.01, and * p < 0.05 vs. G85R. n.s.: not significant. (H–J) : N2a cells expressing mCherry-SOD1 G85R were treated with SHED-CM (30%, 50%, and 70%) for 24 h, HSP-related gene mRNA expression of HSP60, HSP70, and HSP90 ( Hspd1, Hspa1, and Hsp90aa1 , respectively) were analyzed using the SYBR Green-based RT-qPCR assay. The expression levels of mRNAs were normalized to the expression level of β-actin mRNA. Results are presented as means ± SEM of three independent experiments based on the fluorescence intensity of the “mock” (mock = 1). n.s.: not significant.
    Hsp60, supplied by Cell Signaling Technology Inc, 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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    1) Product Images from "Stem Cells From Human Exfoliated Deciduous Teeth-Conditioned Medium (SHED-CM) is a Promising Treatment for Amyotrophic Lateral Sclerosis"

    Article Title: Stem Cells From Human Exfoliated Deciduous Teeth-Conditioned Medium (SHED-CM) is a Promising Treatment for Amyotrophic Lateral Sclerosis

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2022.805379

    SHED-CM suppresses SOD1 G85R -induced ER stress and increases HSP70 levels. (A) : N2a cells expressing mCherry-SOD1G85R were treated with SHED-CM (30%, 50%, and 70%) for 24 h. Subsequently, immunoblot analysis of Bip and Chop was conducted in relation to ER stress. (B and C) : Densitometric quantification of Bip and Chop. ### p < 0.001 vs. WT; *** p < 0.001, ** p < 0.01, and * p < 0.05 vs. G85R. (D) : Immunoblot analysis of HSP60, HSP70, and HSP90. (E–G) : Densitometric quantification of HSP60, HSP70, and HSP90. Results are presented as means ± SEM of three independent experiments based on the fluorescence intensity of the “mock” (mock = 1). *** p < 0.001, ** p < 0.01, and * p < 0.05 vs. G85R. n.s.: not significant. (H–J) : N2a cells expressing mCherry-SOD1 G85R were treated with SHED-CM (30%, 50%, and 70%) for 24 h, HSP-related gene mRNA expression of HSP60, HSP70, and HSP90 ( Hspd1, Hspa1, and Hsp90aa1 , respectively) were analyzed using the SYBR Green-based RT-qPCR assay. The expression levels of mRNAs were normalized to the expression level of β-actin mRNA. Results are presented as means ± SEM of three independent experiments based on the fluorescence intensity of the “mock” (mock = 1). n.s.: not significant.
    Figure Legend Snippet: SHED-CM suppresses SOD1 G85R -induced ER stress and increases HSP70 levels. (A) : N2a cells expressing mCherry-SOD1G85R were treated with SHED-CM (30%, 50%, and 70%) for 24 h. Subsequently, immunoblot analysis of Bip and Chop was conducted in relation to ER stress. (B and C) : Densitometric quantification of Bip and Chop. ### p < 0.001 vs. WT; *** p < 0.001, ** p < 0.01, and * p < 0.05 vs. G85R. (D) : Immunoblot analysis of HSP60, HSP70, and HSP90. (E–G) : Densitometric quantification of HSP60, HSP70, and HSP90. Results are presented as means ± SEM of three independent experiments based on the fluorescence intensity of the “mock” (mock = 1). *** p < 0.001, ** p < 0.01, and * p < 0.05 vs. G85R. n.s.: not significant. (H–J) : N2a cells expressing mCherry-SOD1 G85R were treated with SHED-CM (30%, 50%, and 70%) for 24 h, HSP-related gene mRNA expression of HSP60, HSP70, and HSP90 ( Hspd1, Hspa1, and Hsp90aa1 , respectively) were analyzed using the SYBR Green-based RT-qPCR assay. The expression levels of mRNAs were normalized to the expression level of β-actin mRNA. Results are presented as means ± SEM of three independent experiments based on the fluorescence intensity of the “mock” (mock = 1). n.s.: not significant.

    Techniques Used: Expressing, Western Blot, Fluorescence, SYBR Green Assay, Quantitative RT-PCR

    hsp60 rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc hsp60 rabbit mab
    CD4+CD45RA+ T cells from RA patients and controls were activated for 72 h and stained for the mitochondrial marker <t>HSP60.</t> Nuclei were marked with DAPI.
    Hsp60 Rabbit Mab, supplied by Cell Signaling Technology Inc, 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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    1) Product Images from "Succinyl-CoA Ligase Deficiency in Pro-inflammatory and Tissue-Invasive T Cells"

    Article Title: Succinyl-CoA Ligase Deficiency in Pro-inflammatory and Tissue-Invasive T Cells

    Journal: Cell metabolism

    doi: 10.1016/j.cmet.2020.10.025

    CD4+CD45RA+ T cells from RA patients and controls were activated for 72 h and stained for the mitochondrial marker HSP60. Nuclei were marked with DAPI.
    Figure Legend Snippet: CD4+CD45RA+ T cells from RA patients and controls were activated for 72 h and stained for the mitochondrial marker HSP60. Nuclei were marked with DAPI.

    Techniques Used: Staining, Marker

    KEY RESOURCES TABLE
    Figure Legend Snippet: KEY RESOURCES TABLE

    Techniques Used: Recombinant, Activation Assay, SYBR Green Assay, Cell Isolation, Citrate Assay, Activity Assay, Staining, Plasmid Preparation, Software

    rabbit monoclonal anti hsp60  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal anti hsp60
    Rabbit Monoclonal Anti Hsp60, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit monoclonal anti hsp60/product/Cell Signaling Technology Inc
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    anti hsp60  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti hsp60
    Anti Hsp60, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti hsp60/product/Cell Signaling Technology Inc
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    rabbit anti hsp60  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti hsp60
    (A) Western blot analysis of TFAM protein levels in liver whole cell lysates of CAG-TFAM (+/CAG) mice. Litter mates were used as controls (Con). Actin was used as a loading control. A representative image is shown (n = 2 independent experiments). (B) TFAM protein levels in control and CAG-TFAM animals were quantified by densitometry and are expressed as folds of control (means ± SEM, n = 4–5 biological replicates; P < 0.05: *, two-way ANOVA with Sidak’s test for multiple comparisons). (C) Quantification of steady-state mtDNA levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA levels were quantified by qPCR using specific probes against COX1 and 18S. Data are expressed as means ± SEM (n = 6–7 biological replicates). (D) Southern blot analysis of PstI-digested mtDNA derived from heart and skeletal muscle of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA was quantified by radiolabeling with a specific probe against COX1, nuclear DNA was probed with 18S. A representative image is shown (n = 3 independent experiments). (E) Analysis of steady-state mitochondrial transcript levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con) by qRT-PCR. Data are expressed as means ± SEM (n = 5 biological replicates). (F) De novo RNA synthesis in skeletal muscle and liver mitochondria isolated from CAG-TFAM (+/CAG) mice and control litter mates. Mitochondria were pulse labelled for 1 h. Mitochondrial <t>HSP60</t> was used as a loading control. A representative image is shown (n = 2–3 independent experiments). (G) Representative images of fixed liver tissue from control (Con) and CAG-TFAM animals at 16 d of age analysed by transmission electron microscopy. For each genotype, six biological replicates were analysed. Scale bars, 20 (upper panels), 5 (middle), 2 μm (lower panels). (H) Measurement of triglyceride content. Approximately 100 mg of liver tissue was homogenized and triglycerides were quantified using the triglycerides quantification kit (Sigma-Aldrich). Data are expressed as means ± SEM (n = 5 biological replicates; P < 0.001:***, unpaired t test). Source data are available for this figure.
    Rabbit Anti Hsp60, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti hsp60/product/Cell Signaling Technology Inc
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    1) Product Images from "High levels of TFAM repress mammalian mitochondrial DNA transcription in vivo"

    Article Title: High levels of TFAM repress mammalian mitochondrial DNA transcription in vivo

    Journal: Life Science Alliance

    doi: 10.26508/lsa.202101034

    (A) Western blot analysis of TFAM protein levels in liver whole cell lysates of CAG-TFAM (+/CAG) mice. Litter mates were used as controls (Con). Actin was used as a loading control. A representative image is shown (n = 2 independent experiments). (B) TFAM protein levels in control and CAG-TFAM animals were quantified by densitometry and are expressed as folds of control (means ± SEM, n = 4–5 biological replicates; P < 0.05: *, two-way ANOVA with Sidak’s test for multiple comparisons). (C) Quantification of steady-state mtDNA levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA levels were quantified by qPCR using specific probes against COX1 and 18S. Data are expressed as means ± SEM (n = 6–7 biological replicates). (D) Southern blot analysis of PstI-digested mtDNA derived from heart and skeletal muscle of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA was quantified by radiolabeling with a specific probe against COX1, nuclear DNA was probed with 18S. A representative image is shown (n = 3 independent experiments). (E) Analysis of steady-state mitochondrial transcript levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con) by qRT-PCR. Data are expressed as means ± SEM (n = 5 biological replicates). (F) De novo RNA synthesis in skeletal muscle and liver mitochondria isolated from CAG-TFAM (+/CAG) mice and control litter mates. Mitochondria were pulse labelled for 1 h. Mitochondrial HSP60 was used as a loading control. A representative image is shown (n = 2–3 independent experiments). (G) Representative images of fixed liver tissue from control (Con) and CAG-TFAM animals at 16 d of age analysed by transmission electron microscopy. For each genotype, six biological replicates were analysed. Scale bars, 20 (upper panels), 5 (middle), 2 μm (lower panels). (H) Measurement of triglyceride content. Approximately 100 mg of liver tissue was homogenized and triglycerides were quantified using the triglycerides quantification kit (Sigma-Aldrich). Data are expressed as means ± SEM (n = 5 biological replicates; P < 0.001:***, unpaired t test). Source data are available for this figure.
    Figure Legend Snippet: (A) Western blot analysis of TFAM protein levels in liver whole cell lysates of CAG-TFAM (+/CAG) mice. Litter mates were used as controls (Con). Actin was used as a loading control. A representative image is shown (n = 2 independent experiments). (B) TFAM protein levels in control and CAG-TFAM animals were quantified by densitometry and are expressed as folds of control (means ± SEM, n = 4–5 biological replicates; P < 0.05: *, two-way ANOVA with Sidak’s test for multiple comparisons). (C) Quantification of steady-state mtDNA levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA levels were quantified by qPCR using specific probes against COX1 and 18S. Data are expressed as means ± SEM (n = 6–7 biological replicates). (D) Southern blot analysis of PstI-digested mtDNA derived from heart and skeletal muscle of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA was quantified by radiolabeling with a specific probe against COX1, nuclear DNA was probed with 18S. A representative image is shown (n = 3 independent experiments). (E) Analysis of steady-state mitochondrial transcript levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con) by qRT-PCR. Data are expressed as means ± SEM (n = 5 biological replicates). (F) De novo RNA synthesis in skeletal muscle and liver mitochondria isolated from CAG-TFAM (+/CAG) mice and control litter mates. Mitochondria were pulse labelled for 1 h. Mitochondrial HSP60 was used as a loading control. A representative image is shown (n = 2–3 independent experiments). (G) Representative images of fixed liver tissue from control (Con) and CAG-TFAM animals at 16 d of age analysed by transmission electron microscopy. For each genotype, six biological replicates were analysed. Scale bars, 20 (upper panels), 5 (middle), 2 μm (lower panels). (H) Measurement of triglyceride content. Approximately 100 mg of liver tissue was homogenized and triglycerides were quantified using the triglycerides quantification kit (Sigma-Aldrich). Data are expressed as means ± SEM (n = 5 biological replicates; P < 0.001:***, unpaired t test). Source data are available for this figure.

    Techniques Used: Western Blot, Southern Blot, Derivative Assay, Radioactivity, Quantitative RT-PCR, Isolation, Transmission Assay, Electron Microscopy

    rabbit monoclonal anti hsp60 d6f1 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal anti hsp60 d6f1 antibody
    ( A ) Sub-mitochondrial localizations of new mitochondrial kinases. Transfected HeLa cells were stained and imaged by 3D structured illumination microscopy (3D-SIM). ( B ) MOK2 is imported into mitochondria. Transfected HeLa cells were fixed and permeabilized with digitonin or Triton X-100 before staining. ( C ) MOK is not a mitochondrial membrane protein. Mitochondria purified from transfected HeLa cells were incubated in indicated buffers, and then centrifuged. Supernatants (S) and pellets (P) were analyzed by western blotting. Equal loading was achieved by normalizing to the same number of cells. ( D ) MOK is an IMS protein. COS-7 cells transfected with MOK2-GFP were imaged by Hessian SIM. MitoTracker Red marked inner membrane (IMM) and co-transfected <t>HSP60-mCherry</t> marked matrix. ( E ) MOK2 has better mitochondrial localization than MOK1. HeLa cells were transfected with full-length (FL) or kinase domain (KD) of MOK1 and MOK2. Cells with mitochondrial MOK were quantified. Data is represented as mean ± SD; n = 3 independent experiments, two-tailed Student’s t test; n = 100 cells were analyzed in each experiment. ( F ) Mitochondrial localization of MOK mutants. Transfected HeLa cells were stained with anti-Myc and anti-TOM20 antibodies. ( G ) TOM20-TIM23 complex is required for mitochondrial importing of MOK. HeLa cells expressing specific shRNAs were transfected with MOK2-Myc and stained . Figure 6—source data 1. Uncropped western blot for . Figure 6—source data 2. Raw data for and .
    Rabbit Monoclonal Anti Hsp60 D6f1 Antibody, supplied by Cell Signaling Technology Inc, 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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    Images

    1) Product Images from "A subcellular map of the human kinome"

    Article Title: A subcellular map of the human kinome

    Journal: eLife

    doi: 10.7554/eLife.64943

    ( A ) Sub-mitochondrial localizations of new mitochondrial kinases. Transfected HeLa cells were stained and imaged by 3D structured illumination microscopy (3D-SIM). ( B ) MOK2 is imported into mitochondria. Transfected HeLa cells were fixed and permeabilized with digitonin or Triton X-100 before staining. ( C ) MOK is not a mitochondrial membrane protein. Mitochondria purified from transfected HeLa cells were incubated in indicated buffers, and then centrifuged. Supernatants (S) and pellets (P) were analyzed by western blotting. Equal loading was achieved by normalizing to the same number of cells. ( D ) MOK is an IMS protein. COS-7 cells transfected with MOK2-GFP were imaged by Hessian SIM. MitoTracker Red marked inner membrane (IMM) and co-transfected HSP60-mCherry marked matrix. ( E ) MOK2 has better mitochondrial localization than MOK1. HeLa cells were transfected with full-length (FL) or kinase domain (KD) of MOK1 and MOK2. Cells with mitochondrial MOK were quantified. Data is represented as mean ± SD; n = 3 independent experiments, two-tailed Student’s t test; n = 100 cells were analyzed in each experiment. ( F ) Mitochondrial localization of MOK mutants. Transfected HeLa cells were stained with anti-Myc and anti-TOM20 antibodies. ( G ) TOM20-TIM23 complex is required for mitochondrial importing of MOK. HeLa cells expressing specific shRNAs were transfected with MOK2-Myc and stained . Figure 6—source data 1. Uncropped western blot for . Figure 6—source data 2. Raw data for and .
    Figure Legend Snippet: ( A ) Sub-mitochondrial localizations of new mitochondrial kinases. Transfected HeLa cells were stained and imaged by 3D structured illumination microscopy (3D-SIM). ( B ) MOK2 is imported into mitochondria. Transfected HeLa cells were fixed and permeabilized with digitonin or Triton X-100 before staining. ( C ) MOK is not a mitochondrial membrane protein. Mitochondria purified from transfected HeLa cells were incubated in indicated buffers, and then centrifuged. Supernatants (S) and pellets (P) were analyzed by western blotting. Equal loading was achieved by normalizing to the same number of cells. ( D ) MOK is an IMS protein. COS-7 cells transfected with MOK2-GFP were imaged by Hessian SIM. MitoTracker Red marked inner membrane (IMM) and co-transfected HSP60-mCherry marked matrix. ( E ) MOK2 has better mitochondrial localization than MOK1. HeLa cells were transfected with full-length (FL) or kinase domain (KD) of MOK1 and MOK2. Cells with mitochondrial MOK were quantified. Data is represented as mean ± SD; n = 3 independent experiments, two-tailed Student’s t test; n = 100 cells were analyzed in each experiment. ( F ) Mitochondrial localization of MOK mutants. Transfected HeLa cells were stained with anti-Myc and anti-TOM20 antibodies. ( G ) TOM20-TIM23 complex is required for mitochondrial importing of MOK. HeLa cells expressing specific shRNAs were transfected with MOK2-Myc and stained . Figure 6—source data 1. Uncropped western blot for . Figure 6—source data 2. Raw data for and .

    Techniques Used: Transfection, Staining, Microscopy, Purification, Incubation, Western Blot, Two Tailed Test, Expressing


    Figure Legend Snippet:

    Techniques Used: Transfection, Construct, Sequencing, shRNA, Protease Inhibitor, Software

    rabbit anti hsp60  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc rabbit anti hsp60
    ( A ) BJ STING KO cells stably expressing WT cGAS or the indicated mutants were analyzed for endogenous cGAMP levels (upper). Cell lysates were analyzed by immunoblotting for the indicated proteins (lower). ( B ) THP-1 STING KO cells stably expressing empty vector (EV) and indicated cGAS proteins: endogenous cGAMP levels and schematic of constructs (upper). Red lines, cryptic mitochondrial localization sequence (MLS). Immunoblotting showing expression of cGAS proteins depicted in the middle diagrams (lower). ( C ) Confocal microscopy images showing distinct subcellular distribution of cGAS and C-Flag cGAS-ΔN in THP-1 STING KO or BJ-5ta STING KO cells in relation to mitochondria (mitotracker). Values shown on the bottom are the numbers of cells displaying mitochondrial cGAS relative to total numbers of cells examined. (D) Alignment of the MLS of cGAS from different species. Red, positively charged residues; green, hydrophobic residues. ( E ) The split GFP-cGAS proteins were fused at the N-termini with the signal peptide from <t>Hsp60,</t> which targets the proteins to the mitochondrial matrix. Confocal microscopy shows GFP distribution in HEK293T cells stably expressing these proteins. Size bars in (C and E) = 10 μm.
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    Images

    1) Product Images from "Phosphorylation and Chromatin Tethering Prevent cGAS activation During Mitosis"

    Article Title: Phosphorylation and Chromatin Tethering Prevent cGAS activation During Mitosis

    Journal: Science (New York, N.Y.)

    doi: 10.1126/science.abc5386

    ( A ) BJ STING KO cells stably expressing WT cGAS or the indicated mutants were analyzed for endogenous cGAMP levels (upper). Cell lysates were analyzed by immunoblotting for the indicated proteins (lower). ( B ) THP-1 STING KO cells stably expressing empty vector (EV) and indicated cGAS proteins: endogenous cGAMP levels and schematic of constructs (upper). Red lines, cryptic mitochondrial localization sequence (MLS). Immunoblotting showing expression of cGAS proteins depicted in the middle diagrams (lower). ( C ) Confocal microscopy images showing distinct subcellular distribution of cGAS and C-Flag cGAS-ΔN in THP-1 STING KO or BJ-5ta STING KO cells in relation to mitochondria (mitotracker). Values shown on the bottom are the numbers of cells displaying mitochondrial cGAS relative to total numbers of cells examined. (D) Alignment of the MLS of cGAS from different species. Red, positively charged residues; green, hydrophobic residues. ( E ) The split GFP-cGAS proteins were fused at the N-termini with the signal peptide from Hsp60, which targets the proteins to the mitochondrial matrix. Confocal microscopy shows GFP distribution in HEK293T cells stably expressing these proteins. Size bars in (C and E) = 10 μm.
    Figure Legend Snippet: ( A ) BJ STING KO cells stably expressing WT cGAS or the indicated mutants were analyzed for endogenous cGAMP levels (upper). Cell lysates were analyzed by immunoblotting for the indicated proteins (lower). ( B ) THP-1 STING KO cells stably expressing empty vector (EV) and indicated cGAS proteins: endogenous cGAMP levels and schematic of constructs (upper). Red lines, cryptic mitochondrial localization sequence (MLS). Immunoblotting showing expression of cGAS proteins depicted in the middle diagrams (lower). ( C ) Confocal microscopy images showing distinct subcellular distribution of cGAS and C-Flag cGAS-ΔN in THP-1 STING KO or BJ-5ta STING KO cells in relation to mitochondria (mitotracker). Values shown on the bottom are the numbers of cells displaying mitochondrial cGAS relative to total numbers of cells examined. (D) Alignment of the MLS of cGAS from different species. Red, positively charged residues; green, hydrophobic residues. ( E ) The split GFP-cGAS proteins were fused at the N-termini with the signal peptide from Hsp60, which targets the proteins to the mitochondrial matrix. Confocal microscopy shows GFP distribution in HEK293T cells stably expressing these proteins. Size bars in (C and E) = 10 μm.

    Techniques Used: Stable Transfection, Expressing, Western Blot, Plasmid Preparation, Construct, Sequencing, Confocal Microscopy


    Figure Legend Snippet:

    Techniques Used:

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    Cell Signaling Technology Inc mouse monoclonal igg antibody to hsp60
    BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and <t>Hsp60</t> were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.
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    Cell Signaling Technology Inc hsp60
    BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and <t>Hsp60</t> were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.
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    Cell Signaling Technology Inc hsp60 d6f1 xp rabbit mab
    BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and <t>Hsp60</t> were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.
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    Cell Signaling Technology Inc hsp60 rabbit mab
    CD4+CD45RA+ T cells from RA patients and controls were activated for 72 h and stained for the mitochondrial marker <t>HSP60.</t> Nuclei were marked with DAPI.
    Hsp60 Rabbit Mab, supplied by Cell Signaling Technology Inc, 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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    Cell Signaling Technology Inc rabbit monoclonal anti hsp60
    CD4+CD45RA+ T cells from RA patients and controls were activated for 72 h and stained for the mitochondrial marker <t>HSP60.</t> Nuclei were marked with DAPI.
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    Cell Signaling Technology Inc anti hsp60
    CD4+CD45RA+ T cells from RA patients and controls were activated for 72 h and stained for the mitochondrial marker <t>HSP60.</t> Nuclei were marked with DAPI.
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    (A) Western blot analysis of TFAM protein levels in liver whole cell lysates of CAG-TFAM (+/CAG) mice. Litter mates were used as controls (Con). Actin was used as a loading control. A representative image is shown (n = 2 independent experiments). (B) TFAM protein levels in control and CAG-TFAM animals were quantified by densitometry and are expressed as folds of control (means ± SEM, n = 4–5 biological replicates; P < 0.05: *, two-way ANOVA with Sidak’s test for multiple comparisons). (C) Quantification of steady-state mtDNA levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA levels were quantified by qPCR using specific probes against COX1 and 18S. Data are expressed as means ± SEM (n = 6–7 biological replicates). (D) Southern blot analysis of PstI-digested mtDNA derived from heart and skeletal muscle of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA was quantified by radiolabeling with a specific probe against COX1, nuclear DNA was probed with 18S. A representative image is shown (n = 3 independent experiments). (E) Analysis of steady-state mitochondrial transcript levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con) by qRT-PCR. Data are expressed as means ± SEM (n = 5 biological replicates). (F) De novo RNA synthesis in skeletal muscle and liver mitochondria isolated from CAG-TFAM (+/CAG) mice and control litter mates. Mitochondria were pulse labelled for 1 h. Mitochondrial <t>HSP60</t> was used as a loading control. A representative image is shown (n = 2–3 independent experiments). (G) Representative images of fixed liver tissue from control (Con) and CAG-TFAM animals at 16 d of age analysed by transmission electron microscopy. For each genotype, six biological replicates were analysed. Scale bars, 20 (upper panels), 5 (middle), 2 μm (lower panels). (H) Measurement of triglyceride content. Approximately 100 mg of liver tissue was homogenized and triglycerides were quantified using the triglycerides quantification kit (Sigma-Aldrich). Data are expressed as means ± SEM (n = 5 biological replicates; P < 0.001:***, unpaired t test). Source data are available for this figure.
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    Cell Signaling Technology Inc rabbit monoclonal anti hsp60 d6f1 antibody
    ( A ) Sub-mitochondrial localizations of new mitochondrial kinases. Transfected HeLa cells were stained and imaged by 3D structured illumination microscopy (3D-SIM). ( B ) MOK2 is imported into mitochondria. Transfected HeLa cells were fixed and permeabilized with digitonin or Triton X-100 before staining. ( C ) MOK is not a mitochondrial membrane protein. Mitochondria purified from transfected HeLa cells were incubated in indicated buffers, and then centrifuged. Supernatants (S) and pellets (P) were analyzed by western blotting. Equal loading was achieved by normalizing to the same number of cells. ( D ) MOK is an IMS protein. COS-7 cells transfected with MOK2-GFP were imaged by Hessian SIM. MitoTracker Red marked inner membrane (IMM) and co-transfected <t>HSP60-mCherry</t> marked matrix. ( E ) MOK2 has better mitochondrial localization than MOK1. HeLa cells were transfected with full-length (FL) or kinase domain (KD) of MOK1 and MOK2. Cells with mitochondrial MOK were quantified. Data is represented as mean ± SD; n = 3 independent experiments, two-tailed Student’s t test; n = 100 cells were analyzed in each experiment. ( F ) Mitochondrial localization of MOK mutants. Transfected HeLa cells were stained with anti-Myc and anti-TOM20 antibodies. ( G ) TOM20-TIM23 complex is required for mitochondrial importing of MOK. HeLa cells expressing specific shRNAs were transfected with MOK2-Myc and stained . Figure 6—source data 1. Uncropped western blot for . Figure 6—source data 2. Raw data for and .
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    Image Search Results


    BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and Hsp60 were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.

    Journal: Journal of Translational Medicine

    Article Title: Pro-apoptotic activity of α-bisabolol in preclinical models of primary human acute leukemia cells

    doi: 10.1186/1479-5876-9-45

    Figure Lengend Snippet: BID and NADH-supported state 3 respiration in normal PBMCs and leukemic blasts treated with α-bisabolol . (A) 24-hour α-bisabolol did not induced the cleavage of BID (full length 22 kDa, cleaved 15 kDa) at any concentration. Etoposide-treated Jurkat cells were used as a positive control for tBID. (B) No BID translocation was detected in mitochondrial fraction at different times and solubilized doses of α-bisabolol. α-tubulin and Hsp60 were used as markers for the cytosol and mitochondria fractions, respectively. A representative case is shown. (C) Permeabilized leukemic cells and healthy lymphocytes were incubated for 10 minutes in respiration buffer at 30°C in the presence or in the absence of 3 μM α-bisabolol. In treated leukemic cells, the G/M oxygen consumption was clearly lower than in untreated leukemic controls ( p < 0.05). The S/G3P oxygen consumption was not modified by treatment, and the mitochondrial respiration was not stimulated by FCCP addition. This is in line with a direct effect of α-bisabolol on mitochondrial integrity. Healthy lymphocyte respiration was not affected by treatment. G/M: glutamate plus malate; S/G3P: succinate plus glycerol-3-phosphate; FCCP: carbonylcyanide-4-(trifluoromethoxy)-phenyl-hydrazone. Means ± SD of 6 leukemias and 6 normal donors are depicted.

    Article Snippet: Then, the membrane with the cytosolic and mitochondrial fractions were probed with a rabbit polyclonal IgG antibody to α-tubulin (Cell Signaling Technology) and with a mouse monoclonal IgG antibody to Hsp60 (Abcam, Cambridge, UK), respectively.

    Techniques: Concentration Assay, Positive Control, Translocation Assay, Incubation, Modification

    CD4+CD45RA+ T cells from RA patients and controls were activated for 72 h and stained for the mitochondrial marker HSP60. Nuclei were marked with DAPI.

    Journal: Cell metabolism

    Article Title: Succinyl-CoA Ligase Deficiency in Pro-inflammatory and Tissue-Invasive T Cells

    doi: 10.1016/j.cmet.2020.10.025

    Figure Lengend Snippet: CD4+CD45RA+ T cells from RA patients and controls were activated for 72 h and stained for the mitochondrial marker HSP60. Nuclei were marked with DAPI.

    Article Snippet: The following primary antibodies were used: Acetyl-alpha Tubulin (Lys40) mouse mAb (1:100, Thermo Fisher Scientific), α-tubulin rabbit mAb (1:100, Cell signaling technology), GM-130 rabbit mAb (1:100, Cell signaling technology), Pericentrin rabbit pAb (1:100, Abcam), Hsp60 rabbit mAb (1:100, Cell signaling technology).

    Techniques: Staining, Marker

    KEY RESOURCES TABLE

    Journal: Cell metabolism

    Article Title: Succinyl-CoA Ligase Deficiency in Pro-inflammatory and Tissue-Invasive T Cells

    doi: 10.1016/j.cmet.2020.10.025

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: The following primary antibodies were used: Acetyl-alpha Tubulin (Lys40) mouse mAb (1:100, Thermo Fisher Scientific), α-tubulin rabbit mAb (1:100, Cell signaling technology), GM-130 rabbit mAb (1:100, Cell signaling technology), Pericentrin rabbit pAb (1:100, Abcam), Hsp60 rabbit mAb (1:100, Cell signaling technology).

    Techniques: Recombinant, Activation Assay, SYBR Green Assay, Cell Isolation, Citrate Assay, Activity Assay, Staining, Plasmid Preparation, Software

    (A) Western blot analysis of TFAM protein levels in liver whole cell lysates of CAG-TFAM (+/CAG) mice. Litter mates were used as controls (Con). Actin was used as a loading control. A representative image is shown (n = 2 independent experiments). (B) TFAM protein levels in control and CAG-TFAM animals were quantified by densitometry and are expressed as folds of control (means ± SEM, n = 4–5 biological replicates; P < 0.05: *, two-way ANOVA with Sidak’s test for multiple comparisons). (C) Quantification of steady-state mtDNA levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA levels were quantified by qPCR using specific probes against COX1 and 18S. Data are expressed as means ± SEM (n = 6–7 biological replicates). (D) Southern blot analysis of PstI-digested mtDNA derived from heart and skeletal muscle of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA was quantified by radiolabeling with a specific probe against COX1, nuclear DNA was probed with 18S. A representative image is shown (n = 3 independent experiments). (E) Analysis of steady-state mitochondrial transcript levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con) by qRT-PCR. Data are expressed as means ± SEM (n = 5 biological replicates). (F) De novo RNA synthesis in skeletal muscle and liver mitochondria isolated from CAG-TFAM (+/CAG) mice and control litter mates. Mitochondria were pulse labelled for 1 h. Mitochondrial HSP60 was used as a loading control. A representative image is shown (n = 2–3 independent experiments). (G) Representative images of fixed liver tissue from control (Con) and CAG-TFAM animals at 16 d of age analysed by transmission electron microscopy. For each genotype, six biological replicates were analysed. Scale bars, 20 (upper panels), 5 (middle), 2 μm (lower panels). (H) Measurement of triglyceride content. Approximately 100 mg of liver tissue was homogenized and triglycerides were quantified using the triglycerides quantification kit (Sigma-Aldrich). Data are expressed as means ± SEM (n = 5 biological replicates; P < 0.001:***, unpaired t test). Source data are available for this figure.

    Journal: Life Science Alliance

    Article Title: High levels of TFAM repress mammalian mitochondrial DNA transcription in vivo

    doi: 10.26508/lsa.202101034

    Figure Lengend Snippet: (A) Western blot analysis of TFAM protein levels in liver whole cell lysates of CAG-TFAM (+/CAG) mice. Litter mates were used as controls (Con). Actin was used as a loading control. A representative image is shown (n = 2 independent experiments). (B) TFAM protein levels in control and CAG-TFAM animals were quantified by densitometry and are expressed as folds of control (means ± SEM, n = 4–5 biological replicates; P < 0.05: *, two-way ANOVA with Sidak’s test for multiple comparisons). (C) Quantification of steady-state mtDNA levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA levels were quantified by qPCR using specific probes against COX1 and 18S. Data are expressed as means ± SEM (n = 6–7 biological replicates). (D) Southern blot analysis of PstI-digested mtDNA derived from heart and skeletal muscle of CAG-TFAM (+/CAG) animals and control litter mates (Con). mtDNA was quantified by radiolabeling with a specific probe against COX1, nuclear DNA was probed with 18S. A representative image is shown (n = 3 independent experiments). (E) Analysis of steady-state mitochondrial transcript levels in liver tissue of CAG-TFAM (+/CAG) animals and control litter mates (Con) by qRT-PCR. Data are expressed as means ± SEM (n = 5 biological replicates). (F) De novo RNA synthesis in skeletal muscle and liver mitochondria isolated from CAG-TFAM (+/CAG) mice and control litter mates. Mitochondria were pulse labelled for 1 h. Mitochondrial HSP60 was used as a loading control. A representative image is shown (n = 2–3 independent experiments). (G) Representative images of fixed liver tissue from control (Con) and CAG-TFAM animals at 16 d of age analysed by transmission electron microscopy. For each genotype, six biological replicates were analysed. Scale bars, 20 (upper panels), 5 (middle), 2 μm (lower panels). (H) Measurement of triglyceride content. Approximately 100 mg of liver tissue was homogenized and triglycerides were quantified using the triglycerides quantification kit (Sigma-Aldrich). Data are expressed as means ± SEM (n = 5 biological replicates; P < 0.001:***, unpaired t test). Source data are available for this figure.

    Article Snippet: The following antibodies were used: rabbit polyclonal anti-TFAM (Abcam), mouse monoclonal anti-actin (Abcam), Total OXPHOS Rodent Western Blotting antibody cocktail (Abcam), mouse monoclonal anti-tubulin (Sigma-Aldrich), rabbit anti-Tubulin (Cell Signaling), rabbit anti-vinculin (Abcam), mouse monoclonal anti-UQCRFS1/RISP (Abcam), mouse monoclonal anti-COX5a (Invitrogen/ThermoFisher Scientific), mouse monoclonal anti-VDAC (Millipore), rabbit polyclonal anti-ACOT2 (Proteintech), mouse monoclonal anti-cytochrome C (Abcam), rabbit anti-HSP60 (Cell Signaling), sheep anti-mouse IgG (GE Healthcare), and donkey anti-rabbit (GE Healthcare).

    Techniques: Western Blot, Southern Blot, Derivative Assay, Radioactivity, Quantitative RT-PCR, Isolation, Transmission Assay, Electron Microscopy

    ( A ) Sub-mitochondrial localizations of new mitochondrial kinases. Transfected HeLa cells were stained and imaged by 3D structured illumination microscopy (3D-SIM). ( B ) MOK2 is imported into mitochondria. Transfected HeLa cells were fixed and permeabilized with digitonin or Triton X-100 before staining. ( C ) MOK is not a mitochondrial membrane protein. Mitochondria purified from transfected HeLa cells were incubated in indicated buffers, and then centrifuged. Supernatants (S) and pellets (P) were analyzed by western blotting. Equal loading was achieved by normalizing to the same number of cells. ( D ) MOK is an IMS protein. COS-7 cells transfected with MOK2-GFP were imaged by Hessian SIM. MitoTracker Red marked inner membrane (IMM) and co-transfected HSP60-mCherry marked matrix. ( E ) MOK2 has better mitochondrial localization than MOK1. HeLa cells were transfected with full-length (FL) or kinase domain (KD) of MOK1 and MOK2. Cells with mitochondrial MOK were quantified. Data is represented as mean ± SD; n = 3 independent experiments, two-tailed Student’s t test; n = 100 cells were analyzed in each experiment. ( F ) Mitochondrial localization of MOK mutants. Transfected HeLa cells were stained with anti-Myc and anti-TOM20 antibodies. ( G ) TOM20-TIM23 complex is required for mitochondrial importing of MOK. HeLa cells expressing specific shRNAs were transfected with MOK2-Myc and stained . Figure 6—source data 1. Uncropped western blot for . Figure 6—source data 2. Raw data for and .

    Journal: eLife

    Article Title: A subcellular map of the human kinome

    doi: 10.7554/eLife.64943

    Figure Lengend Snippet: ( A ) Sub-mitochondrial localizations of new mitochondrial kinases. Transfected HeLa cells were stained and imaged by 3D structured illumination microscopy (3D-SIM). ( B ) MOK2 is imported into mitochondria. Transfected HeLa cells were fixed and permeabilized with digitonin or Triton X-100 before staining. ( C ) MOK is not a mitochondrial membrane protein. Mitochondria purified from transfected HeLa cells were incubated in indicated buffers, and then centrifuged. Supernatants (S) and pellets (P) were analyzed by western blotting. Equal loading was achieved by normalizing to the same number of cells. ( D ) MOK is an IMS protein. COS-7 cells transfected with MOK2-GFP were imaged by Hessian SIM. MitoTracker Red marked inner membrane (IMM) and co-transfected HSP60-mCherry marked matrix. ( E ) MOK2 has better mitochondrial localization than MOK1. HeLa cells were transfected with full-length (FL) or kinase domain (KD) of MOK1 and MOK2. Cells with mitochondrial MOK were quantified. Data is represented as mean ± SD; n = 3 independent experiments, two-tailed Student’s t test; n = 100 cells were analyzed in each experiment. ( F ) Mitochondrial localization of MOK mutants. Transfected HeLa cells were stained with anti-Myc and anti-TOM20 antibodies. ( G ) TOM20-TIM23 complex is required for mitochondrial importing of MOK. HeLa cells expressing specific shRNAs were transfected with MOK2-Myc and stained . Figure 6—source data 1. Uncropped western blot for . Figure 6—source data 2. Raw data for and .

    Article Snippet: Antibody , Rabbit monoclonal anti-HSP60 (D6F1) antibody , Cell Signaling Technology , Cat# 46611, RRID: AB_2799305 , WB (1:1000), IF (1:500).

    Techniques: Transfection, Staining, Microscopy, Purification, Incubation, Western Blot, Two Tailed Test, Expressing

    Journal: eLife

    Article Title: A subcellular map of the human kinome

    doi: 10.7554/eLife.64943

    Figure Lengend Snippet:

    Article Snippet: Antibody , Rabbit monoclonal anti-HSP60 (D6F1) antibody , Cell Signaling Technology , Cat# 46611, RRID: AB_2799305 , WB (1:1000), IF (1:500).

    Techniques: Transfection, Construct, Sequencing, shRNA, Protease Inhibitor, Software