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hif1 alpha antibody / hif1a  (NSJ Bioreagents)
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Hif1 Alpha Antibody / Hif1a, supplied by NSJ Bioreagents, 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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hif1a shrna  (Santa Cruz Biotechnology)
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HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of <t>Hif1a</t> and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .
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HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of <t>Hif1a</t> and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .
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hif 1α  (Proteintech)
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HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of <t>Hif1a</t> and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .
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mutant mut hif1a hif1a 3 utr fragments  (Sangon Biotech)
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HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of <t>Hif1a</t> and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .
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hif1a floxed mice  (Shanghai Model Organisms Center)
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HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of <t>Hif1a</t> and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .
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gene exp hif1a gg03364519 m1  (Thermo Fisher)
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HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of <t>Hif1a</t> and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .
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HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of <t>Hif1a</t> and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .
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HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of <t>Hif1a</t> and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .
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HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of Hif1a and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .

Journal: Advanced Science

Article Title: Early‐Life Manganese Overexposure Activates Microglial Phagocytosis through the YY1/TREM2 Axis Leading to Hippocampal Synaptic Remodeling in Mice

doi: 10.1002/advs.78036

Figure Lengend Snippet: HIF1α regulation and dysfunction of SMURF2‐mediated ubiquitin degradation are responsible for YY1 upregulation. (A) Predicted HIF1α binding sites in the Yy1 promoter region from the JASPAR database. (B) Co‐expression analysis of Hif1a and Yy1 in the hippocampus by GEPIA database. (C) ChIP assay showing the binding between HIF1α and the Yy1 promoter. (D,E) Representative immunofluorescence images and quantitative analysis showing the nuclear expression of YY1 under different treatments. Scale bar, 20 µm, magnification scale bar, 10 µm. (F,G) Western blot analysis of nuclear YY1 protein levels in microglia from different treatment groups. (H) RT‐qPCR analysis of Yy1 , Trem2 , and phagolysosomal pathway‐related genes ( Rab7 and Lamp1 ) under various treatments. (I–M) Western blot and quantification of YY1, TREM2, and phagolysosome (RAB7 and LAMP1) proteins under different treatments. (N,O) Western blot showing YY1 protein degradation dynamics following CHX treatment at different time points under Mn exposure. (P) Immunoprecipitation analysis of YY1 ubiquitination levels in microglia. (Q) Identification of the E3 ubiquitin ligase SMURF2 targeting YY1 by the UbiBrowser 2.0 database. (R) Relative mRNA expression level of Smurf2 in Mn treatment assessed by RT‐qPCR. (S,T) Western blot and quantification of SMURF2 relative protein expression level under Mn treatment. (U) Molecular docking prediction of potential Mn 2 + binding sites within SMURF2. (V,W) Co‐immunoprecipitation assays revealing the interaction strength between SMURF2 and YY1 under different treatments. (X) Analysis of YY1 ubiquitination levels after immunoprecipitation across different experimental groups. mRNA expressions were normalized to Gapdh and relative to Control, proteins expressions were normalized to Histone H3 or β‐actin and relative to Control. Data were expressed as mean ± SD. For in vitro experiments, n = 3 independent experiments for Western blot analysis, and n = 4 independent experiments for all other assays. Data were analyzed by two‐way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01 versus Control group. ## p < 0.01 versus Mn (25 µ m ) group. See also Figure .

Article Snippet: Lentiviruses directing the expression of Yy1 shRNA (sc‐36864‐V, Santa Cruz) and Hif1a shRNA (sc‐44308‐V, Santa Cruz) were obtained from Santa Cruz Biotechnology (USA).

Techniques: Ubiquitin Proteomics, Binding Assay, Expressing, Analysis, Immunofluorescence, Western Blot, Quantitative RT-PCR, Immunoprecipitation, Docking Assay, Co-Immunoprecipitation Assay, Control, In Vitro