hsp70 inhibitors  (Millipore)


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    Name:
    KNK437
    Description:

    Catalog Number:
    sml0964
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    Structured Review

    Millipore hsp70 inhibitors
    <t>HSP70</t> plays a role in mediating thermally-enhanced TNF-α production in macrophages. A , Peritoneal macrophages were isolated from LPS-challenged mice after 2 hour heat treatment. Cells were recovered overnight and re-stimulated (1×10 6 /well) in vitro with LPS and IFN-γ at 37°C for 4 hours, then HSP70 mRNA level was measured by quantitative real-time PCR. The results are presented relative to GAPDH and baseline expression in unstimulated cells from RT-mice. B , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 2, 6 or 24 hours to examine HSP70 secretion by ELISA. C , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 6 hours with or without HSP70 inhibitors: KNK437 (20, 10 µM) or Pifithrin-µ (5, 1 µM) to detect TNF-α production by ELISA. Cells from each treatment condition were pooled from 2–4 mice and measured in triplicate. Data are mean ± SD. Data are representative of two independent experiments. * In comparison of cells with and without HSP70 inhibitors from WBH-mice. ** In comparison of cells with and without HSP70 inhibitors from RT-mice. *, ** p

    https://www.bioz.com/result/hsp70 inhibitors/product/Millipore
    Average 94 stars, based on 15 article reviews
    Price from $9.99 to $1999.99
    hsp70 inhibitors - by Bioz Stars, 2020-10
    94/100 stars

    Images

    1) Product Images from "Elevation in Body Temperature to Fever Range Enhances and Prolongs Subsequent Responsiveness of Macrophages to Endotoxin Challenge"

    Article Title: Elevation in Body Temperature to Fever Range Enhances and Prolongs Subsequent Responsiveness of Macrophages to Endotoxin Challenge

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0030077

    HSP70 plays a role in mediating thermally-enhanced TNF-α production in macrophages. A , Peritoneal macrophages were isolated from LPS-challenged mice after 2 hour heat treatment. Cells were recovered overnight and re-stimulated (1×10 6 /well) in vitro with LPS and IFN-γ at 37°C for 4 hours, then HSP70 mRNA level was measured by quantitative real-time PCR. The results are presented relative to GAPDH and baseline expression in unstimulated cells from RT-mice. B , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 2, 6 or 24 hours to examine HSP70 secretion by ELISA. C , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 6 hours with or without HSP70 inhibitors: KNK437 (20, 10 µM) or Pifithrin-µ (5, 1 µM) to detect TNF-α production by ELISA. Cells from each treatment condition were pooled from 2–4 mice and measured in triplicate. Data are mean ± SD. Data are representative of two independent experiments. * In comparison of cells with and without HSP70 inhibitors from WBH-mice. ** In comparison of cells with and without HSP70 inhibitors from RT-mice. *, ** p
    Figure Legend Snippet: HSP70 plays a role in mediating thermally-enhanced TNF-α production in macrophages. A , Peritoneal macrophages were isolated from LPS-challenged mice after 2 hour heat treatment. Cells were recovered overnight and re-stimulated (1×10 6 /well) in vitro with LPS and IFN-γ at 37°C for 4 hours, then HSP70 mRNA level was measured by quantitative real-time PCR. The results are presented relative to GAPDH and baseline expression in unstimulated cells from RT-mice. B , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 2, 6 or 24 hours to examine HSP70 secretion by ELISA. C , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 6 hours with or without HSP70 inhibitors: KNK437 (20, 10 µM) or Pifithrin-µ (5, 1 µM) to detect TNF-α production by ELISA. Cells from each treatment condition were pooled from 2–4 mice and measured in triplicate. Data are mean ± SD. Data are representative of two independent experiments. * In comparison of cells with and without HSP70 inhibitors from WBH-mice. ** In comparison of cells with and without HSP70 inhibitors from RT-mice. *, ** p

    Techniques Used: Isolation, Mouse Assay, In Vitro, Real-time Polymerase Chain Reaction, Expressing, Enzyme-linked Immunosorbent Assay

    2) Product Images from "Defining Immunological Impact and Therapeutic Benefit of Mild Heating in a Murine Model of Arthritis"

    Article Title: Defining Immunological Impact and Therapeutic Benefit of Mild Heating in a Murine Model of Arthritis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0120327

    Multiple targets are affected by heat treatment. (A), Serum TNF-α concentration from CIA mice was determined by ELISA. Error bars show SEM (n = 7). (B-C), TNF-α and IL-10 concentrations were detected in the tissue homogenates from naïve and CIA mice paws by ELISA (day 53). Error bars show SEM. Data are representative of two experiments. (D-E), tissue homogenates were prepared from naïve and CIA mice paws and expression of phosphorylated IKKα /β, NF-κB p65, p50, HSP70 and HIF-1α were detected by Western blotting. Each lane represents different mice. The graph shows the ratio of the band intensity of proteins normalized to β-actin. * p
    Figure Legend Snippet: Multiple targets are affected by heat treatment. (A), Serum TNF-α concentration from CIA mice was determined by ELISA. Error bars show SEM (n = 7). (B-C), TNF-α and IL-10 concentrations were detected in the tissue homogenates from naïve and CIA mice paws by ELISA (day 53). Error bars show SEM. Data are representative of two experiments. (D-E), tissue homogenates were prepared from naïve and CIA mice paws and expression of phosphorylated IKKα /β, NF-κB p65, p50, HSP70 and HIF-1α were detected by Western blotting. Each lane represents different mice. The graph shows the ratio of the band intensity of proteins normalized to β-actin. * p

    Techniques Used: Concentration Assay, Mouse Assay, Enzyme-linked Immunosorbent Assay, Expressing, Western Blot

    In vitro heat treatment increases HSF-1 and HSP 70 expression which may regulate TNF-α production in activated macrophages. Peritoneal macrophages were harvested from LPS-challenged mice, recovered overnight and re-stimulated with LPS (100 ng/mL) and IFN-γ (25 U) at 37°C or 39.5°C for indicated times. Cell lysates were prepared from these cells to detect HSF-1 and HSP70 by Western blotting. Cells stimulated at 42°C for 30 min were used as positive controls. The graph shows the ratio of the band intensity normalized to β-actin. Data are mean ± SEM. Data are representative of two independent experiments. * p
    Figure Legend Snippet: In vitro heat treatment increases HSF-1 and HSP 70 expression which may regulate TNF-α production in activated macrophages. Peritoneal macrophages were harvested from LPS-challenged mice, recovered overnight and re-stimulated with LPS (100 ng/mL) and IFN-γ (25 U) at 37°C or 39.5°C for indicated times. Cell lysates were prepared from these cells to detect HSF-1 and HSP70 by Western blotting. Cells stimulated at 42°C for 30 min were used as positive controls. The graph shows the ratio of the band intensity normalized to β-actin. Data are mean ± SEM. Data are representative of two independent experiments. * p

    Techniques Used: In Vitro, Expressing, Mouse Assay, Western Blot

    Related Articles

    Cell Culture:

    Article Title: Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera
    Article Snippet: .. Eventual proof of concept of the importance of HSP in this disease was achieved by inhibiting the proliferation/apoptotic ratio and the blockade of JAK/STAT activation in cultured PV patient cells, after incubating these cells with the HSP inhibitor, KNK437 or siRNA. ..

    Activation Assay:

    Article Title: Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera
    Article Snippet: .. Eventual proof of concept of the importance of HSP in this disease was achieved by inhibiting the proliferation/apoptotic ratio and the blockade of JAK/STAT activation in cultured PV patient cells, after incubating these cells with the HSP inhibitor, KNK437 or siRNA. ..

    other:

    Article Title: Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera
    Article Snippet: ET patients (ratio in ET without treatment: 66.19; ratio in ET with KNK437 , 50 μM: 59.82).

    Article Title: Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera
    Article Snippet: Moreover, the other MAPK phospho-protein, phospho-p38, was differentially expressed with and without KNK437 treatment in samples from PV patients (ratio in PV without treatment: 7.30; ratio in PV with KNK437 , 50 μM: 4.18), but was unchanged in ET patients.

    Article Title: A non-enzymatic function of Golgi glycosyltransferases: Mediation of Golgi fragmentation by interaction with non-muscle myosin IIA
    Article Snippet: Blebbistatin, TM, KNK437, Ndz, Cyt D, BFA and M G-132 were dissolved in dimethyl DMSO immediately before use.

    Article Title: Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera
    Article Snippet: We demonstrated that KNK437 , a HSP70 inhibitor, increased erythroid apoptosis in cell cultures from PV patients (Figure A-B).

    Ex Vivo:

    Article Title: Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera
    Article Snippet: .. HSP70 inhibition in an ex-vivo cell line To confirm the molecular mechanism of the HSP70 inhibitor in the JAK2/STAT and MAPK pathways, we performed Western blot on HEL and Ba/F3 JAK2 V617F cell lines proteomes, with and without KNK437 (10-50-100 μM) treatment (Figure D). ..

    Western Blot:

    Article Title: Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera
    Article Snippet: .. HSP70 inhibition in an ex-vivo cell line To confirm the molecular mechanism of the HSP70 inhibitor in the JAK2/STAT and MAPK pathways, we performed Western blot on HEL and Ba/F3 JAK2 V617F cell lines proteomes, with and without KNK437 (10-50-100 μM) treatment (Figure D). ..

    Inhibition:

    Article Title: Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera
    Article Snippet: .. HSP70 inhibition in an ex-vivo cell line To confirm the molecular mechanism of the HSP70 inhibitor in the JAK2/STAT and MAPK pathways, we performed Western blot on HEL and Ba/F3 JAK2 V617F cell lines proteomes, with and without KNK437 (10-50-100 μM) treatment (Figure D). ..

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  • 94
    Millipore hsp70 inhibitors
    <t>HSP70</t> plays a role in mediating thermally-enhanced TNF-α production in macrophages. A , Peritoneal macrophages were isolated from LPS-challenged mice after 2 hour heat treatment. Cells were recovered overnight and re-stimulated (1×10 6 /well) in vitro with LPS and IFN-γ at 37°C for 4 hours, then HSP70 mRNA level was measured by quantitative real-time PCR. The results are presented relative to GAPDH and baseline expression in unstimulated cells from RT-mice. B , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 2, 6 or 24 hours to examine HSP70 secretion by ELISA. C , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 6 hours with or without HSP70 inhibitors: KNK437 (20, 10 µM) or Pifithrin-µ (5, 1 µM) to detect TNF-α production by ELISA. Cells from each treatment condition were pooled from 2–4 mice and measured in triplicate. Data are mean ± SD. Data are representative of two independent experiments. * In comparison of cells with and without HSP70 inhibitors from WBH-mice. ** In comparison of cells with and without HSP70 inhibitors from RT-mice. *, ** p
    Hsp70 Inhibitors, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hsp70 inhibitors/product/Millipore
    Average 94 stars, based on 27 article reviews
    Price from $9.99 to $1999.99
    hsp70 inhibitors - by Bioz Stars, 2020-10
    94/100 stars
      Buy from Supplier

    Image Search Results


    HSP70 plays a role in mediating thermally-enhanced TNF-α production in macrophages. A , Peritoneal macrophages were isolated from LPS-challenged mice after 2 hour heat treatment. Cells were recovered overnight and re-stimulated (1×10 6 /well) in vitro with LPS and IFN-γ at 37°C for 4 hours, then HSP70 mRNA level was measured by quantitative real-time PCR. The results are presented relative to GAPDH and baseline expression in unstimulated cells from RT-mice. B , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 2, 6 or 24 hours to examine HSP70 secretion by ELISA. C , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 6 hours with or without HSP70 inhibitors: KNK437 (20, 10 µM) or Pifithrin-µ (5, 1 µM) to detect TNF-α production by ELISA. Cells from each treatment condition were pooled from 2–4 mice and measured in triplicate. Data are mean ± SD. Data are representative of two independent experiments. * In comparison of cells with and without HSP70 inhibitors from WBH-mice. ** In comparison of cells with and without HSP70 inhibitors from RT-mice. *, ** p

    Journal: PLoS ONE

    Article Title: Elevation in Body Temperature to Fever Range Enhances and Prolongs Subsequent Responsiveness of Macrophages to Endotoxin Challenge

    doi: 10.1371/journal.pone.0030077

    Figure Lengend Snippet: HSP70 plays a role in mediating thermally-enhanced TNF-α production in macrophages. A , Peritoneal macrophages were isolated from LPS-challenged mice after 2 hour heat treatment. Cells were recovered overnight and re-stimulated (1×10 6 /well) in vitro with LPS and IFN-γ at 37°C for 4 hours, then HSP70 mRNA level was measured by quantitative real-time PCR. The results are presented relative to GAPDH and baseline expression in unstimulated cells from RT-mice. B , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 2, 6 or 24 hours to examine HSP70 secretion by ELISA. C , Macrophages (2×10 5 /well) from LPS-challenged mice were re-stimulated with LPS and IFN-γ at 37°C for 6 hours with or without HSP70 inhibitors: KNK437 (20, 10 µM) or Pifithrin-µ (5, 1 µM) to detect TNF-α production by ELISA. Cells from each treatment condition were pooled from 2–4 mice and measured in triplicate. Data are mean ± SD. Data are representative of two independent experiments. * In comparison of cells with and without HSP70 inhibitors from WBH-mice. ** In comparison of cells with and without HSP70 inhibitors from RT-mice. *, ** p

    Article Snippet: In some experiments, macrophages were treated with HSP70 inhibitors (KNK437, EMD chemicals; Pifithrin-µ, Sigma-Aldrich) together with 100 ng/mL LPS and 25 U IFN-γ.

    Techniques: Isolation, Mouse Assay, In Vitro, Real-time Polymerase Chain Reaction, Expressing, Enzyme-linked Immunosorbent Assay

    HSP70 regulates NOD2's stability in the cell. A, HEK293T-NOD2Myc/Tet-op cells were incubated with 100 μ m GGA or 100 μ m KNK437 or DMSO for 2 h, and lysates were collected after cycloheximide treatment during the indicated time intervals.

    Journal: The Journal of Biological Chemistry

    Article Title: The Molecular Chaperone HSP70 Binds to and Stabilizes NOD2, an Important Protein Involved in Crohn Disease *

    doi: 10.1074/jbc.M114.557686

    Figure Lengend Snippet: HSP70 regulates NOD2's stability in the cell. A, HEK293T-NOD2Myc/Tet-op cells were incubated with 100 μ m GGA or 100 μ m KNK437 or DMSO for 2 h, and lysates were collected after cycloheximide treatment during the indicated time intervals.

    Article Snippet: HSP70 inhibitor KNK437 was obtained from Calbiochem.

    Techniques: Incubation

    Hsp70/AIF interaction and the effects of NAC and KNK437 on the Hsp70/AIF interaction in hyperoxic PAECs. PAECs were exposed to normoxia (nor) and hyperoxia (hyper) in the absence and presence of NAC (5 mM) or KNK437 (50–100 μM) for 48 h after which co-immunoprecipitations of Hsp70 and AIF in the cytosolic fraction of cell lysates were performed. (A and C) Representative immunoblots of Hsp70 and AIF. (B and D) Bar graph depicting the changes in Hsp70/AIF ratio. Results are expressed as mean ± SE; n = 4. * P

    Journal: PLoS ONE

    Article Title: Heat Shock Protein 70 Prevents Hyperoxia-Induced Disruption of Lung Endothelial Barrier via Caspase-Dependent and AIF-Dependent Pathways

    doi: 10.1371/journal.pone.0129343

    Figure Lengend Snippet: Hsp70/AIF interaction and the effects of NAC and KNK437 on the Hsp70/AIF interaction in hyperoxic PAECs. PAECs were exposed to normoxia (nor) and hyperoxia (hyper) in the absence and presence of NAC (5 mM) or KNK437 (50–100 μM) for 48 h after which co-immunoprecipitations of Hsp70 and AIF in the cytosolic fraction of cell lysates were performed. (A and C) Representative immunoblots of Hsp70 and AIF. (B and D) Bar graph depicting the changes in Hsp70/AIF ratio. Results are expressed as mean ± SE; n = 4. * P

    Article Snippet: The Hsp70 inhibitor KNK437 and the caspase inhibitor-I Z-VAD-FMK were from EMD Millipore (Billerica, MA).

    Techniques: Western Blot

    Hsp70 inhibitor KNK437exaggerates hyperoxia-induced lung endothelial barrier disruption. PAECs were treated with and without KNK437 (50 μM) and exposed to normoxia and hyperoxia for 48 h. TEER was continuously monitored as described in Materials and Methods. Results are expressed as mean ± SE; n = 4. * P

    Journal: PLoS ONE

    Article Title: Heat Shock Protein 70 Prevents Hyperoxia-Induced Disruption of Lung Endothelial Barrier via Caspase-Dependent and AIF-Dependent Pathways

    doi: 10.1371/journal.pone.0129343

    Figure Lengend Snippet: Hsp70 inhibitor KNK437exaggerates hyperoxia-induced lung endothelial barrier disruption. PAECs were treated with and without KNK437 (50 μM) and exposed to normoxia and hyperoxia for 48 h. TEER was continuously monitored as described in Materials and Methods. Results are expressed as mean ± SE; n = 4. * P

    Article Snippet: The Hsp70 inhibitor KNK437 and the caspase inhibitor-I Z-VAD-FMK were from EMD Millipore (Billerica, MA).

    Techniques:

    The effect of vaccination on inducible HSP70 in CD4 + TSCM and DC before and 28 weeks after immunization. ( A ) CD4 + TSCM, ( B ) HSP70 in CD4 + TSCM, ( C ) HSP70 in DC, ( D ) membrane associated (ma)IL-15 in DC. ( A–D ) Assays were performed on cells from the same vaccinees (n = 11). ( E ) Gating strategy used to identify DC. ( F ) Flow cytometry identifying HSP70 and IL-15 in DC, and HSP70 in TSCM. ( G ) The effect of stimulating CD4 + TSCM with microbial (m) HSP70 before and ( H ) after immunization. ( I ) The effect of dose dependent inhibition of HSP70 with PES in unstimulated and microbial (m)HSP70 stimulated CD4 + TSCM; *p value = 0.02, when compared with the untreated (0) µM of cells. ( J ) The effect of stimulating CD4 + TSCM with HIVgp140, compared with unstimulated cells on IFN-γ, IL-2 and IL-17 (n = 10 samples from different subjects).

    Journal: Scientific Reports

    Article Title: A novel mechanism linking memory stem cells with innate immunity in protection against HIV-1 infection

    doi: 10.1038/s41598-017-01188-3

    Figure Lengend Snippet: The effect of vaccination on inducible HSP70 in CD4 + TSCM and DC before and 28 weeks after immunization. ( A ) CD4 + TSCM, ( B ) HSP70 in CD4 + TSCM, ( C ) HSP70 in DC, ( D ) membrane associated (ma)IL-15 in DC. ( A–D ) Assays were performed on cells from the same vaccinees (n = 11). ( E ) Gating strategy used to identify DC. ( F ) Flow cytometry identifying HSP70 and IL-15 in DC, and HSP70 in TSCM. ( G ) The effect of stimulating CD4 + TSCM with microbial (m) HSP70 before and ( H ) after immunization. ( I ) The effect of dose dependent inhibition of HSP70 with PES in unstimulated and microbial (m)HSP70 stimulated CD4 + TSCM; *p value = 0.02, when compared with the untreated (0) µM of cells. ( J ) The effect of stimulating CD4 + TSCM with HIVgp140, compared with unstimulated cells on IFN-γ, IL-2 and IL-17 (n = 10 samples from different subjects).

    Article Snippet: To determine the specificity of HSP70 in stimulating TSCM, dose dependent inhibition was carried out with the HSP70 inhibitor, 2-phenylethynesulfonamide (PES, Calbiochem, Merck, UK).

    Techniques: Flow Cytometry, Cytometry, Inhibition

    Identification of TSCM CD45RO − CCR7 + CD95 + CD4 + and CD8 + T cells. ( A ) CD4 + TSCM and ( B ) CD8 + TSCM cells pre- immunization, 2 and 28 weeks after the last immunization (n = 12–18), all from different immunized subjects. ( C ) The specificity of TSCM was examined by in vitro stimulation with HIVgp140 and compared with recombinant IL-15 and microbial (m) HSP70. ( D ) Shows significant increase in CD4 + TSCM 28 weeks after the last immunization in the vaccinated cohort, but not in the CCR7 + central (CM), CCR7- effector memory (EM) or naïve CD4 + T cells (n = 10 in each group, ( E , F , G ). ( H ) Identification of TSCM and gating.

    Journal: Scientific Reports

    Article Title: A novel mechanism linking memory stem cells with innate immunity in protection against HIV-1 infection

    doi: 10.1038/s41598-017-01188-3

    Figure Lengend Snippet: Identification of TSCM CD45RO − CCR7 + CD95 + CD4 + and CD8 + T cells. ( A ) CD4 + TSCM and ( B ) CD8 + TSCM cells pre- immunization, 2 and 28 weeks after the last immunization (n = 12–18), all from different immunized subjects. ( C ) The specificity of TSCM was examined by in vitro stimulation with HIVgp140 and compared with recombinant IL-15 and microbial (m) HSP70. ( D ) Shows significant increase in CD4 + TSCM 28 weeks after the last immunization in the vaccinated cohort, but not in the CCR7 + central (CM), CCR7- effector memory (EM) or naïve CD4 + T cells (n = 10 in each group, ( E , F , G ). ( H ) Identification of TSCM and gating.

    Article Snippet: To determine the specificity of HSP70 in stimulating TSCM, dose dependent inhibition was carried out with the HSP70 inhibitor, 2-phenylethynesulfonamide (PES, Calbiochem, Merck, UK).

    Techniques: In Vitro, Recombinant