cytoplasmic and nuclear protein extraction kit  (Boster Bio)


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    Boster Bio cytoplasmic and nuclear protein extraction kit
    EA inhibited the NF-κB signalling pathway via the upregulation of OTULIN expression. a Western blotting was used to detect OTULIN, p-IκBα, IκBα, <t>and</t> cytoplasm/nucleus-p65 proteins. β-Actin served as a loading control for total or <t>cytoplasmic</t> <t>protein,</t> and Lamin B served as a <t>nuclear</t> protein. b , n = 3) Quantitative analysis of OTULIN protein, the phosphorylation ratio of IκBα, and nuclear/cytoplasmic NF-κB p65. c , n = 6) Immunohistochemistry was performed to detect IκBα and NF-κB p65 proteins. Red arrows indicate IκBα- or NF-κB p65-positive cells. Scale bar = 100 μm. P
    Cytoplasmic And Nuclear Protein Extraction Kit, supplied by Boster Bio, 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/cytoplasmic and nuclear protein extraction kit/product/Boster Bio
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cytoplasmic and nuclear protein extraction kit - by Bioz Stars, 2022-07
    94/100 stars

    Images

    1) Product Images from "OTULIN is a new target of EA treatment in the alleviation of brain injury and glial cell activation via suppression of the NF-κB signalling pathway in acute ischaemic stroke rats"

    Article Title: OTULIN is a new target of EA treatment in the alleviation of brain injury and glial cell activation via suppression of the NF-κB signalling pathway in acute ischaemic stroke rats

    Journal: Molecular Medicine

    doi: 10.1186/s10020-021-00297-0

    EA inhibited the NF-κB signalling pathway via the upregulation of OTULIN expression. a Western blotting was used to detect OTULIN, p-IκBα, IκBα, and cytoplasm/nucleus-p65 proteins. β-Actin served as a loading control for total or cytoplasmic protein, and Lamin B served as a nuclear protein. b , n = 3) Quantitative analysis of OTULIN protein, the phosphorylation ratio of IκBα, and nuclear/cytoplasmic NF-κB p65. c , n = 6) Immunohistochemistry was performed to detect IκBα and NF-κB p65 proteins. Red arrows indicate IκBα- or NF-κB p65-positive cells. Scale bar = 100 μm. P
    Figure Legend Snippet: EA inhibited the NF-κB signalling pathway via the upregulation of OTULIN expression. a Western blotting was used to detect OTULIN, p-IκBα, IκBα, and cytoplasm/nucleus-p65 proteins. β-Actin served as a loading control for total or cytoplasmic protein, and Lamin B served as a nuclear protein. b , n = 3) Quantitative analysis of OTULIN protein, the phosphorylation ratio of IκBα, and nuclear/cytoplasmic NF-κB p65. c , n = 6) Immunohistochemistry was performed to detect IκBα and NF-κB p65 proteins. Red arrows indicate IκBα- or NF-κB p65-positive cells. Scale bar = 100 μm. P

    Techniques Used: Expressing, Western Blot, Immunohistochemistry

    2) Product Images from "Neuroprotective Effects of Celastrol on Transient Global Cerebral Ischemia Rats via Regulating HMGB1/NF-κB Signaling Pathway"

    Article Title: Neuroprotective Effects of Celastrol on Transient Global Cerebral Ischemia Rats via Regulating HMGB1/NF-κB Signaling Pathway

    Journal: Frontiers in Neuroscience

    doi: 10.3389/fnins.2020.00847

    Schematic diagram illustrating possible neuroprotective mechanisms of celastrol against glial activation, oxidative stress and neuroinflammation in tGCI/R rats via the high mobility group box 1 (HMGB1) and Toll-like receptor 4 (TLR4) /nuclear factor (NF-κB) pathway. Cerebral ischemia induced HMGB1 nuclear-cytoplasmic translocation and activate TLR4/RAGE, promote the phosphorylation of IκBα, thus inducing the translocation of NF-κB from the cytoplasm to the nucleus, promote gene expression and generate a series of cytokines, thus promoting glial activation, neuroinflammation, oxidative stress, and caspase activation, eventually lead to apoptotic neuronal death. GFAP, glial fibrillary acid protein; Iba-1, ionized calcium binding adaptor molecular 1; ROS, reactive oxygen species; MDA, malondialdehyde; TNF-α, tumor necrosis factor α; IL-β, interleukin-β; IL-6, interleukin-6; IL-10, interleukin-10.
    Figure Legend Snippet: Schematic diagram illustrating possible neuroprotective mechanisms of celastrol against glial activation, oxidative stress and neuroinflammation in tGCI/R rats via the high mobility group box 1 (HMGB1) and Toll-like receptor 4 (TLR4) /nuclear factor (NF-κB) pathway. Cerebral ischemia induced HMGB1 nuclear-cytoplasmic translocation and activate TLR4/RAGE, promote the phosphorylation of IκBα, thus inducing the translocation of NF-κB from the cytoplasm to the nucleus, promote gene expression and generate a series of cytokines, thus promoting glial activation, neuroinflammation, oxidative stress, and caspase activation, eventually lead to apoptotic neuronal death. GFAP, glial fibrillary acid protein; Iba-1, ionized calcium binding adaptor molecular 1; ROS, reactive oxygen species; MDA, malondialdehyde; TNF-α, tumor necrosis factor α; IL-β, interleukin-β; IL-6, interleukin-6; IL-10, interleukin-10.

    Techniques Used: Activation Assay, Translocation Assay, Expressing, Binding Assay, Multiple Displacement Amplification

    3) Product Images from "Secreted stromal protein ISLR promotes intestinal regeneration by suppressing epithelial Hippo signaling"

    Article Title: Secreted stromal protein ISLR promotes intestinal regeneration by suppressing epithelial Hippo signaling

    Journal: The EMBO Journal

    doi: 10.15252/embj.2019103255

    Deletion of Islr in stromal cells suppressed epithelial Yap activity A Heatmap of the altered Hippo‐related genes in colons from control and cKO mice 1 day after 5‐day DSS treatment. The parameter of the color key indicated the fold changes converted to log2 of signal value normalized. B qRT–PCR analysis validates the altered Hippo‐related genes in control and cKO mice; n = 4. C Western blotting for pMst1/2, Mst1, pMob1, and Mob1 in colon epithelium from control and cKO mice 2 days after 5‐day DSS treatment. β‐actin was used as a loading control. The quantification of pMst1/2 versus Mst1 and pMob1 versus Mob1 was shown under the corresponding protein bands. D Western blotting for Yap1 in nuclear and cytoplasmic proteins isolated from intestinal epithelial cells from control and cKO mice 2 days after 5‐day DSS treatment. Histone H3, a positive control for nuclear proteins. α‐Tubulin, a positive control for cytoplasmic proteins. The quantification of Yap1 versus Histone H3 in nuclear proteins was shown under the corresponding band. E, F Double immunofluorescence for Yap1 and β‐catenin in the colons from control ( n = 4) and cKO ( n = 4) mice 2 days after DSS removal (E), and in AOM/DSS tumors from control ( n = 4) and cKO ( n = 4) mice (F). The percentage of nuclear Yap1 + cells versus epithelial cells was quantified. Scale bar: 50 μm. G Western blotting for Yap1 and pYap1 in colon epithelial cells from control and cKO mice 2 days after 5‐day DSS treatment. β‐actin was used as a loading control. The ratio of Yap1/pYap1 was quantified; n = 3. H The growth curve of HCT116 colorectal cancer cells cultured in the supernatant from WT or cKO IMCs, concomitantly transfected with PCDH empty vector or PCDH‐YAP1‐5SA vector; n = 4 technical replicates. I Pearson correlation analysis of ISLR and CTGF ( P
    Figure Legend Snippet: Deletion of Islr in stromal cells suppressed epithelial Yap activity A Heatmap of the altered Hippo‐related genes in colons from control and cKO mice 1 day after 5‐day DSS treatment. The parameter of the color key indicated the fold changes converted to log2 of signal value normalized. B qRT–PCR analysis validates the altered Hippo‐related genes in control and cKO mice; n = 4. C Western blotting for pMst1/2, Mst1, pMob1, and Mob1 in colon epithelium from control and cKO mice 2 days after 5‐day DSS treatment. β‐actin was used as a loading control. The quantification of pMst1/2 versus Mst1 and pMob1 versus Mob1 was shown under the corresponding protein bands. D Western blotting for Yap1 in nuclear and cytoplasmic proteins isolated from intestinal epithelial cells from control and cKO mice 2 days after 5‐day DSS treatment. Histone H3, a positive control for nuclear proteins. α‐Tubulin, a positive control for cytoplasmic proteins. The quantification of Yap1 versus Histone H3 in nuclear proteins was shown under the corresponding band. E, F Double immunofluorescence for Yap1 and β‐catenin in the colons from control ( n = 4) and cKO ( n = 4) mice 2 days after DSS removal (E), and in AOM/DSS tumors from control ( n = 4) and cKO ( n = 4) mice (F). The percentage of nuclear Yap1 + cells versus epithelial cells was quantified. Scale bar: 50 μm. G Western blotting for Yap1 and pYap1 in colon epithelial cells from control and cKO mice 2 days after 5‐day DSS treatment. β‐actin was used as a loading control. The ratio of Yap1/pYap1 was quantified; n = 3. H The growth curve of HCT116 colorectal cancer cells cultured in the supernatant from WT or cKO IMCs, concomitantly transfected with PCDH empty vector or PCDH‐YAP1‐5SA vector; n = 4 technical replicates. I Pearson correlation analysis of ISLR and CTGF ( P

    Techniques Used: Activity Assay, Mouse Assay, Quantitative RT-PCR, Western Blot, Isolation, Positive Control, Immunofluorescence, Cell Culture, Transfection, Plasmid Preparation

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    Boster Bio cytoplasmic and nuclear protein extraction kit
    EA inhibited the NF-κB signalling pathway via the upregulation of OTULIN expression. a Western blotting was used to detect OTULIN, p-IκBα, IκBα, <t>and</t> cytoplasm/nucleus-p65 proteins. β-Actin served as a loading control for total or <t>cytoplasmic</t> <t>protein,</t> and Lamin B served as a <t>nuclear</t> protein. b , n = 3) Quantitative analysis of OTULIN protein, the phosphorylation ratio of IκBα, and nuclear/cytoplasmic NF-κB p65. c , n = 6) Immunohistochemistry was performed to detect IκBα and NF-κB p65 proteins. Red arrows indicate IκBα- or NF-κB p65-positive cells. Scale bar = 100 μm. P
    Cytoplasmic And Nuclear Protein Extraction Kit, supplied by Boster Bio, 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/cytoplasmic and nuclear protein extraction kit/product/Boster Bio
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cytoplasmic and nuclear protein extraction kit - by Bioz Stars, 2022-07
    94/100 stars
      Buy from Supplier

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    EA inhibited the NF-κB signalling pathway via the upregulation of OTULIN expression. a Western blotting was used to detect OTULIN, p-IκBα, IκBα, and cytoplasm/nucleus-p65 proteins. β-Actin served as a loading control for total or cytoplasmic protein, and Lamin B served as a nuclear protein. b , n = 3) Quantitative analysis of OTULIN protein, the phosphorylation ratio of IκBα, and nuclear/cytoplasmic NF-κB p65. c , n = 6) Immunohistochemistry was performed to detect IκBα and NF-κB p65 proteins. Red arrows indicate IκBα- or NF-κB p65-positive cells. Scale bar = 100 μm. P

    Journal: Molecular Medicine

    Article Title: OTULIN is a new target of EA treatment in the alleviation of brain injury and glial cell activation via suppression of the NF-κB signalling pathway in acute ischaemic stroke rats

    doi: 10.1186/s10020-021-00297-0

    Figure Lengend Snippet: EA inhibited the NF-κB signalling pathway via the upregulation of OTULIN expression. a Western blotting was used to detect OTULIN, p-IκBα, IκBα, and cytoplasm/nucleus-p65 proteins. β-Actin served as a loading control for total or cytoplasmic protein, and Lamin B served as a nuclear protein. b , n = 3) Quantitative analysis of OTULIN protein, the phosphorylation ratio of IκBα, and nuclear/cytoplasmic NF-κB p65. c , n = 6) Immunohistochemistry was performed to detect IκBα and NF-κB p65 proteins. Red arrows indicate IκBα- or NF-κB p65-positive cells. Scale bar = 100 μm. P

    Article Snippet: The nuclear and cytoplasmic proteins were extracted using a Nuclear and Cytoplasmic Protein Extraction Kit (no. AR0106, Boster, Beijing, China), and the protein concentrations were detected using a BAC kit (Beyotime, Shanghai, China).

    Techniques: Expressing, Western Blot, Immunohistochemistry

    Schematic diagram illustrating possible neuroprotective mechanisms of celastrol against glial activation, oxidative stress and neuroinflammation in tGCI/R rats via the high mobility group box 1 (HMGB1) and Toll-like receptor 4 (TLR4) /nuclear factor (NF-κB) pathway. Cerebral ischemia induced HMGB1 nuclear-cytoplasmic translocation and activate TLR4/RAGE, promote the phosphorylation of IκBα, thus inducing the translocation of NF-κB from the cytoplasm to the nucleus, promote gene expression and generate a series of cytokines, thus promoting glial activation, neuroinflammation, oxidative stress, and caspase activation, eventually lead to apoptotic neuronal death. GFAP, glial fibrillary acid protein; Iba-1, ionized calcium binding adaptor molecular 1; ROS, reactive oxygen species; MDA, malondialdehyde; TNF-α, tumor necrosis factor α; IL-β, interleukin-β; IL-6, interleukin-6; IL-10, interleukin-10.

    Journal: Frontiers in Neuroscience

    Article Title: Neuroprotective Effects of Celastrol on Transient Global Cerebral Ischemia Rats via Regulating HMGB1/NF-κB Signaling Pathway

    doi: 10.3389/fnins.2020.00847

    Figure Lengend Snippet: Schematic diagram illustrating possible neuroprotective mechanisms of celastrol against glial activation, oxidative stress and neuroinflammation in tGCI/R rats via the high mobility group box 1 (HMGB1) and Toll-like receptor 4 (TLR4) /nuclear factor (NF-κB) pathway. Cerebral ischemia induced HMGB1 nuclear-cytoplasmic translocation and activate TLR4/RAGE, promote the phosphorylation of IκBα, thus inducing the translocation of NF-κB from the cytoplasm to the nucleus, promote gene expression and generate a series of cytokines, thus promoting glial activation, neuroinflammation, oxidative stress, and caspase activation, eventually lead to apoptotic neuronal death. GFAP, glial fibrillary acid protein; Iba-1, ionized calcium binding adaptor molecular 1; ROS, reactive oxygen species; MDA, malondialdehyde; TNF-α, tumor necrosis factor α; IL-β, interleukin-β; IL-6, interleukin-6; IL-10, interleukin-10.

    Article Snippet: Immunofluorescent Staining Three days (72 h) after tGCI/R, rat brains (n = 4) were freshly removed and divided into two halves with a sharp blade on ice, one half was used for immunofluorescent analysis and the other was used for nuclear/cytoplasmic protein extraction.

    Techniques: Activation Assay, Translocation Assay, Expressing, Binding Assay, Multiple Displacement Amplification

    Deletion of Islr in stromal cells suppressed epithelial Yap activity A Heatmap of the altered Hippo‐related genes in colons from control and cKO mice 1 day after 5‐day DSS treatment. The parameter of the color key indicated the fold changes converted to log2 of signal value normalized. B qRT–PCR analysis validates the altered Hippo‐related genes in control and cKO mice; n = 4. C Western blotting for pMst1/2, Mst1, pMob1, and Mob1 in colon epithelium from control and cKO mice 2 days after 5‐day DSS treatment. β‐actin was used as a loading control. The quantification of pMst1/2 versus Mst1 and pMob1 versus Mob1 was shown under the corresponding protein bands. D Western blotting for Yap1 in nuclear and cytoplasmic proteins isolated from intestinal epithelial cells from control and cKO mice 2 days after 5‐day DSS treatment. Histone H3, a positive control for nuclear proteins. α‐Tubulin, a positive control for cytoplasmic proteins. The quantification of Yap1 versus Histone H3 in nuclear proteins was shown under the corresponding band. E, F Double immunofluorescence for Yap1 and β‐catenin in the colons from control ( n = 4) and cKO ( n = 4) mice 2 days after DSS removal (E), and in AOM/DSS tumors from control ( n = 4) and cKO ( n = 4) mice (F). The percentage of nuclear Yap1 + cells versus epithelial cells was quantified. Scale bar: 50 μm. G Western blotting for Yap1 and pYap1 in colon epithelial cells from control and cKO mice 2 days after 5‐day DSS treatment. β‐actin was used as a loading control. The ratio of Yap1/pYap1 was quantified; n = 3. H The growth curve of HCT116 colorectal cancer cells cultured in the supernatant from WT or cKO IMCs, concomitantly transfected with PCDH empty vector or PCDH‐YAP1‐5SA vector; n = 4 technical replicates. I Pearson correlation analysis of ISLR and CTGF ( P

    Journal: The EMBO Journal

    Article Title: Secreted stromal protein ISLR promotes intestinal regeneration by suppressing epithelial Hippo signaling

    doi: 10.15252/embj.2019103255

    Figure Lengend Snippet: Deletion of Islr in stromal cells suppressed epithelial Yap activity A Heatmap of the altered Hippo‐related genes in colons from control and cKO mice 1 day after 5‐day DSS treatment. The parameter of the color key indicated the fold changes converted to log2 of signal value normalized. B qRT–PCR analysis validates the altered Hippo‐related genes in control and cKO mice; n = 4. C Western blotting for pMst1/2, Mst1, pMob1, and Mob1 in colon epithelium from control and cKO mice 2 days after 5‐day DSS treatment. β‐actin was used as a loading control. The quantification of pMst1/2 versus Mst1 and pMob1 versus Mob1 was shown under the corresponding protein bands. D Western blotting for Yap1 in nuclear and cytoplasmic proteins isolated from intestinal epithelial cells from control and cKO mice 2 days after 5‐day DSS treatment. Histone H3, a positive control for nuclear proteins. α‐Tubulin, a positive control for cytoplasmic proteins. The quantification of Yap1 versus Histone H3 in nuclear proteins was shown under the corresponding band. E, F Double immunofluorescence for Yap1 and β‐catenin in the colons from control ( n = 4) and cKO ( n = 4) mice 2 days after DSS removal (E), and in AOM/DSS tumors from control ( n = 4) and cKO ( n = 4) mice (F). The percentage of nuclear Yap1 + cells versus epithelial cells was quantified. Scale bar: 50 μm. G Western blotting for Yap1 and pYap1 in colon epithelial cells from control and cKO mice 2 days after 5‐day DSS treatment. β‐actin was used as a loading control. The ratio of Yap1/pYap1 was quantified; n = 3. H The growth curve of HCT116 colorectal cancer cells cultured in the supernatant from WT or cKO IMCs, concomitantly transfected with PCDH empty vector or PCDH‐YAP1‐5SA vector; n = 4 technical replicates. I Pearson correlation analysis of ISLR and CTGF ( P

    Article Snippet: Nucleoprotein extraction Nucleoprotein was isolated from cells using a nucleoprotein extraction kit (AR0106, BosterBio, USA) according to the manufacturer's instructions.

    Techniques: Activity Assay, Mouse Assay, Quantitative RT-PCR, Western Blot, Isolation, Positive Control, Immunofluorescence, Cell Culture, Transfection, Plasmid Preparation