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renilla luciferase plasmid prl-null  (Promega)

 
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    Structured Review

    Promega renilla luciferase plasmid prl-null
    (A-B) IFN-β and NF-κB promoter activities are downregulated in DF-1 TLR3 KO cells but can be rescued by exogenous expression of TLR3. DF-1 and DF-1 TLR3 KO cells were co-transfected with pLucter (100 ng) and pR-null (30 ng) plasmids (A) , or with pSI-chNFκB-Luc (50 ng) plasmid (B) together with different amounts (100, 200, 400 or 800 ng) of the plasmid expressing chTLR3-His. At 8 h pt the cells were transfected with 250 ng of Poly I:C, and harvested at 24 h after plasmid transfection. A control consisting in cells co-transfected with pLucter, pR-null and the empty pCDNA3, or with the pSI-chNFκB-Luc, and the empty pCDNA3 plasmid (800 ng) was included in each assay. The samples were analyzed by the dual <t>luciferase</t> assay kit. Each determination was carried out in duplicate, and the firefly luciferase expression level of each sample was normalized by <t>Renilla</t> values. Results are expressed as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not transfected with poly I:C. (C-D) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) (C) or with the plasmid pSI-chNFκB-Luc (50 ng) (D). At 8 h pt, cells were either treated with Poly I:C (20 µg) added directly to the culture medium or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase activity quantification. (E) DF-1 and DF-1 TLR3 KO cells were transfected with a siRNA specifically silencing the expression of MDA5 protein, or with a control siRNA. At 24 h pt, the cultures were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) and 8 h later cells were either treated with poly I:C (20μg) or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase assay. (F) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng). At 8 h pt, cells were transfected with 250 ng of Poly I:C and subsequently treated with BFA (50μM) or the vehicle DMSO 1 h later. The samples were harvested at 24 h after plasmid transfection and analyzed using the dual luciferase assay kit. In panels C-F values are presented as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not treated with Poly I:C. Bars indicate means ± standard deviations based on data of duplicate samples from three independent experiments. *, ** and *** indicate p values of <0.05, <0.01 and <0.001, respectively, as determined by unpaired Student’s test. ns, not significant.
    Renilla Luciferase Plasmid Prl Null, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/renilla luciferase plasmid prl-null/product/Promega
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    renilla luciferase plasmid prl-null - by Bioz Stars, 2026-03
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    Images

    1) Product Images from "Key role of TLR3 in type I IFN expression and apoptosis induction in IBDV-infected chicken fibroblast cells"

    Article Title: Key role of TLR3 in type I IFN expression and apoptosis induction in IBDV-infected chicken fibroblast cells

    Journal: bioRxiv

    doi: 10.1101/2025.07.16.665101

    (A-B) IFN-β and NF-κB promoter activities are downregulated in DF-1 TLR3 KO cells but can be rescued by exogenous expression of TLR3. DF-1 and DF-1 TLR3 KO cells were co-transfected with pLucter (100 ng) and pR-null (30 ng) plasmids (A) , or with pSI-chNFκB-Luc (50 ng) plasmid (B) together with different amounts (100, 200, 400 or 800 ng) of the plasmid expressing chTLR3-His. At 8 h pt the cells were transfected with 250 ng of Poly I:C, and harvested at 24 h after plasmid transfection. A control consisting in cells co-transfected with pLucter, pR-null and the empty pCDNA3, or with the pSI-chNFκB-Luc, and the empty pCDNA3 plasmid (800 ng) was included in each assay. The samples were analyzed by the dual luciferase assay kit. Each determination was carried out in duplicate, and the firefly luciferase expression level of each sample was normalized by Renilla values. Results are expressed as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not transfected with poly I:C. (C-D) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) (C) or with the plasmid pSI-chNFκB-Luc (50 ng) (D). At 8 h pt, cells were either treated with Poly I:C (20 µg) added directly to the culture medium or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase activity quantification. (E) DF-1 and DF-1 TLR3 KO cells were transfected with a siRNA specifically silencing the expression of MDA5 protein, or with a control siRNA. At 24 h pt, the cultures were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) and 8 h later cells were either treated with poly I:C (20μg) or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase assay. (F) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng). At 8 h pt, cells were transfected with 250 ng of Poly I:C and subsequently treated with BFA (50μM) or the vehicle DMSO 1 h later. The samples were harvested at 24 h after plasmid transfection and analyzed using the dual luciferase assay kit. In panels C-F values are presented as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not treated with Poly I:C. Bars indicate means ± standard deviations based on data of duplicate samples from three independent experiments. *, ** and *** indicate p values of <0.05, <0.01 and <0.001, respectively, as determined by unpaired Student’s test. ns, not significant.
    Figure Legend Snippet: (A-B) IFN-β and NF-κB promoter activities are downregulated in DF-1 TLR3 KO cells but can be rescued by exogenous expression of TLR3. DF-1 and DF-1 TLR3 KO cells were co-transfected with pLucter (100 ng) and pR-null (30 ng) plasmids (A) , or with pSI-chNFκB-Luc (50 ng) plasmid (B) together with different amounts (100, 200, 400 or 800 ng) of the plasmid expressing chTLR3-His. At 8 h pt the cells were transfected with 250 ng of Poly I:C, and harvested at 24 h after plasmid transfection. A control consisting in cells co-transfected with pLucter, pR-null and the empty pCDNA3, or with the pSI-chNFκB-Luc, and the empty pCDNA3 plasmid (800 ng) was included in each assay. The samples were analyzed by the dual luciferase assay kit. Each determination was carried out in duplicate, and the firefly luciferase expression level of each sample was normalized by Renilla values. Results are expressed as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not transfected with poly I:C. (C-D) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) (C) or with the plasmid pSI-chNFκB-Luc (50 ng) (D). At 8 h pt, cells were either treated with Poly I:C (20 µg) added directly to the culture medium or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase activity quantification. (E) DF-1 and DF-1 TLR3 KO cells were transfected with a siRNA specifically silencing the expression of MDA5 protein, or with a control siRNA. At 24 h pt, the cultures were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) and 8 h later cells were either treated with poly I:C (20μg) or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase assay. (F) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng). At 8 h pt, cells were transfected with 250 ng of Poly I:C and subsequently treated with BFA (50μM) or the vehicle DMSO 1 h later. The samples were harvested at 24 h after plasmid transfection and analyzed using the dual luciferase assay kit. In panels C-F values are presented as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not treated with Poly I:C. Bars indicate means ± standard deviations based on data of duplicate samples from three independent experiments. *, ** and *** indicate p values of <0.05, <0.01 and <0.001, respectively, as determined by unpaired Student’s test. ns, not significant.

    Techniques Used: Expressing, Transfection, Plasmid Preparation, Control, Luciferase, Activity Assay



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    renilla luciferase plasmid prl-null  (Promega)
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    Promega renilla luciferase plasmid prl-null
    (A-B) IFN-β and NF-κB promoter activities are downregulated in DF-1 TLR3 KO cells but can be rescued by exogenous expression of TLR3. DF-1 and DF-1 TLR3 KO cells were co-transfected with pLucter (100 ng) and pR-null (30 ng) plasmids (A) , or with pSI-chNFκB-Luc (50 ng) plasmid (B) together with different amounts (100, 200, 400 or 800 ng) of the plasmid expressing chTLR3-His. At 8 h pt the cells were transfected with 250 ng of Poly I:C, and harvested at 24 h after plasmid transfection. A control consisting in cells co-transfected with pLucter, pR-null and the empty pCDNA3, or with the pSI-chNFκB-Luc, and the empty pCDNA3 plasmid (800 ng) was included in each assay. The samples were analyzed by the dual <t>luciferase</t> assay kit. Each determination was carried out in duplicate, and the firefly luciferase expression level of each sample was normalized by <t>Renilla</t> values. Results are expressed as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not transfected with poly I:C. (C-D) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) (C) or with the plasmid pSI-chNFκB-Luc (50 ng) (D). At 8 h pt, cells were either treated with Poly I:C (20 µg) added directly to the culture medium or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase activity quantification. (E) DF-1 and DF-1 TLR3 KO cells were transfected with a siRNA specifically silencing the expression of MDA5 protein, or with a control siRNA. At 24 h pt, the cultures were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) and 8 h later cells were either treated with poly I:C (20μg) or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase assay. (F) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng). At 8 h pt, cells were transfected with 250 ng of Poly I:C and subsequently treated with BFA (50μM) or the vehicle DMSO 1 h later. The samples were harvested at 24 h after plasmid transfection and analyzed using the dual luciferase assay kit. In panels C-F values are presented as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not treated with Poly I:C. Bars indicate means ± standard deviations based on data of duplicate samples from three independent experiments. *, ** and *** indicate p values of <0.05, <0.01 and <0.001, respectively, as determined by unpaired Student’s test. ns, not significant.
    Renilla Luciferase Plasmid Prl Null, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    plasmid prl-null  (Promega)
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    (A-B) IFN-β and NF-κB promoter activities are downregulated in DF-1 TLR3 KO cells but can be rescued by exogenous expression of TLR3. DF-1 and DF-1 TLR3 KO cells were co-transfected with pLucter (100 ng) and pR-null (30 ng) plasmids (A) , or with pSI-chNFκB-Luc (50 ng) plasmid (B) together with different amounts (100, 200, 400 or 800 ng) of the plasmid expressing chTLR3-His. At 8 h pt the cells were transfected with 250 ng of Poly I:C, and harvested at 24 h after plasmid transfection. A control consisting in cells co-transfected with pLucter, pR-null and the empty pCDNA3, or with the pSI-chNFκB-Luc, and the empty pCDNA3 plasmid (800 ng) was included in each assay. The samples were analyzed by the dual <t>luciferase</t> assay kit. Each determination was carried out in duplicate, and the firefly luciferase expression level of each sample was normalized by <t>Renilla</t> values. Results are expressed as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not transfected with poly I:C. (C-D) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) (C) or with the plasmid pSI-chNFκB-Luc (50 ng) (D). At 8 h pt, cells were either treated with Poly I:C (20 µg) added directly to the culture medium or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase activity quantification. (E) DF-1 and DF-1 TLR3 KO cells were transfected with a siRNA specifically silencing the expression of MDA5 protein, or with a control siRNA. At 24 h pt, the cultures were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) and 8 h later cells were either treated with poly I:C (20μg) or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase assay. (F) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng). At 8 h pt, cells were transfected with 250 ng of Poly I:C and subsequently treated with BFA (50μM) or the vehicle DMSO 1 h later. The samples were harvested at 24 h after plasmid transfection and analyzed using the dual luciferase assay kit. In panels C-F values are presented as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not treated with Poly I:C. Bars indicate means ± standard deviations based on data of duplicate samples from three independent experiments. *, ** and *** indicate p values of <0.05, <0.01 and <0.001, respectively, as determined by unpaired Student’s test. ns, not significant.
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    prl-null renilla luciferase control reporter  (Promega)
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    Promega prl-null renilla luciferase control reporter
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    prl null  (Promega)
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    prl-null plasmid  (Promega)
    90
    Promega prl-null plasmid
    Fbxo16 forms a CRL1 complex, binds to p65 and negatively regulates NF-κB signaling. (A) Interaction of Fbxo16 and Cullins in whole cell lysates of HEK293T cells, transfected with c-Myc-Fbxo16, then immunoprecipitated with anti-Flag, and immunoblotted with anti-Cullin 1, Cullin 2 or Cullin 3. (B) Interaction of Fbxo16 and Skp1 in whole cell lysates of HEK293T cells, transfected with c-Myc-Fbxo16, then immunoprecipitated with anti-c-Myc, and immunoblotted with anti-Skp1. (C) Interaction of Fbxo16 and p65 in whole cell lysates of HEK293T cells, transfected with a Flag-p65 or p50 along without or with c-Myc-Fbxo16, then immunoprecipitated with anti-c-Myc, and immunoblotted with anti-p65 or p50. (D) Interaction of Fbxo16 and PDLIM2 in whole cell lysates of HEK293T cells, transfected with a Flag-PDLIM2 along without or with c-Myc-Fbxo16, then immunoprecipitated with anti-c-Myc, and immunoblotted with anti-Flag. (E) Luciferase assay in MEFs transfected with ELAM−1 luciferase reporter and pRL-Null <t>renilla</t> constructs along with increasing amounts (wedge) of Fbxo16, then left untreated or stimulated with LPS for 5 hr. (F) Luciferase assay in HEK293T cells transfected with ELAM−1 luciferase reporter and pRL-Null renilla constructs without or with MyD88, IKKβ, TRAF6 or p65 along with increasing amounts (wedge) of Fbxo16. Data are representative of three (A, B) , four (C, D) or three ( E, F ; means ± SD, **P<0.01) independent experiments.
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    https://www.bioz.com/result/prl-null plasmid/product/Promega
    Average 90 stars, based on 1 article reviews
    prl-null plasmid - by Bioz Stars, 2026-03
    90/100 stars
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    Image Search Results


    (A-B) IFN-β and NF-κB promoter activities are downregulated in DF-1 TLR3 KO cells but can be rescued by exogenous expression of TLR3. DF-1 and DF-1 TLR3 KO cells were co-transfected with pLucter (100 ng) and pR-null (30 ng) plasmids (A) , or with pSI-chNFκB-Luc (50 ng) plasmid (B) together with different amounts (100, 200, 400 or 800 ng) of the plasmid expressing chTLR3-His. At 8 h pt the cells were transfected with 250 ng of Poly I:C, and harvested at 24 h after plasmid transfection. A control consisting in cells co-transfected with pLucter, pR-null and the empty pCDNA3, or with the pSI-chNFκB-Luc, and the empty pCDNA3 plasmid (800 ng) was included in each assay. The samples were analyzed by the dual luciferase assay kit. Each determination was carried out in duplicate, and the firefly luciferase expression level of each sample was normalized by Renilla values. Results are expressed as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not transfected with poly I:C. (C-D) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) (C) or with the plasmid pSI-chNFκB-Luc (50 ng) (D). At 8 h pt, cells were either treated with Poly I:C (20 µg) added directly to the culture medium or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase activity quantification. (E) DF-1 and DF-1 TLR3 KO cells were transfected with a siRNA specifically silencing the expression of MDA5 protein, or with a control siRNA. At 24 h pt, the cultures were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) and 8 h later cells were either treated with poly I:C (20μg) or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase assay. (F) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng). At 8 h pt, cells were transfected with 250 ng of Poly I:C and subsequently treated with BFA (50μM) or the vehicle DMSO 1 h later. The samples were harvested at 24 h after plasmid transfection and analyzed using the dual luciferase assay kit. In panels C-F values are presented as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not treated with Poly I:C. Bars indicate means ± standard deviations based on data of duplicate samples from three independent experiments. *, ** and *** indicate p values of <0.05, <0.01 and <0.001, respectively, as determined by unpaired Student’s test. ns, not significant.

    Journal: bioRxiv

    Article Title: Key role of TLR3 in type I IFN expression and apoptosis induction in IBDV-infected chicken fibroblast cells

    doi: 10.1101/2025.07.16.665101

    Figure Lengend Snippet: (A-B) IFN-β and NF-κB promoter activities are downregulated in DF-1 TLR3 KO cells but can be rescued by exogenous expression of TLR3. DF-1 and DF-1 TLR3 KO cells were co-transfected with pLucter (100 ng) and pR-null (30 ng) plasmids (A) , or with pSI-chNFκB-Luc (50 ng) plasmid (B) together with different amounts (100, 200, 400 or 800 ng) of the plasmid expressing chTLR3-His. At 8 h pt the cells were transfected with 250 ng of Poly I:C, and harvested at 24 h after plasmid transfection. A control consisting in cells co-transfected with pLucter, pR-null and the empty pCDNA3, or with the pSI-chNFκB-Luc, and the empty pCDNA3 plasmid (800 ng) was included in each assay. The samples were analyzed by the dual luciferase assay kit. Each determination was carried out in duplicate, and the firefly luciferase expression level of each sample was normalized by Renilla values. Results are expressed as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not transfected with poly I:C. (C-D) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) (C) or with the plasmid pSI-chNFκB-Luc (50 ng) (D). At 8 h pt, cells were either treated with Poly I:C (20 µg) added directly to the culture medium or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase activity quantification. (E) DF-1 and DF-1 TLR3 KO cells were transfected with a siRNA specifically silencing the expression of MDA5 protein, or with a control siRNA. At 24 h pt, the cultures were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng) and 8 h later cells were either treated with poly I:C (20μg) or transfected with increasing amounts (100, 200 and 300 ng) of Poly I:C. The samples were harvested at 24 h after plasmid transfection and used for luciferase assay. (F) DF-1 and DF-1 TLR3 KO cells were transfected with the plasmids pLucter (100 ng) and pR-null (30 ng). At 8 h pt, cells were transfected with 250 ng of Poly I:C and subsequently treated with BFA (50μM) or the vehicle DMSO 1 h later. The samples were harvested at 24 h after plasmid transfection and analyzed using the dual luciferase assay kit. In panels C-F values are presented as the fold induction over the level found in the control DF-1 or DF-1 TLR3 KO cells not treated with Poly I:C. Bars indicate means ± standard deviations based on data of duplicate samples from three independent experiments. *, ** and *** indicate p values of <0.05, <0.01 and <0.001, respectively, as determined by unpaired Student’s test. ns, not significant.

    Article Snippet: The Renilla luciferase plasmid (pRL-null; Promega) was kindly provided for Dr. Pablo Gastaminza.

    Techniques: Expressing, Transfection, Plasmid Preparation, Control, Luciferase, Activity Assay

    Fbxo16 forms a CRL1 complex, binds to p65 and negatively regulates NF-κB signaling. (A) Interaction of Fbxo16 and Cullins in whole cell lysates of HEK293T cells, transfected with c-Myc-Fbxo16, then immunoprecipitated with anti-Flag, and immunoblotted with anti-Cullin 1, Cullin 2 or Cullin 3. (B) Interaction of Fbxo16 and Skp1 in whole cell lysates of HEK293T cells, transfected with c-Myc-Fbxo16, then immunoprecipitated with anti-c-Myc, and immunoblotted with anti-Skp1. (C) Interaction of Fbxo16 and p65 in whole cell lysates of HEK293T cells, transfected with a Flag-p65 or p50 along without or with c-Myc-Fbxo16, then immunoprecipitated with anti-c-Myc, and immunoblotted with anti-p65 or p50. (D) Interaction of Fbxo16 and PDLIM2 in whole cell lysates of HEK293T cells, transfected with a Flag-PDLIM2 along without or with c-Myc-Fbxo16, then immunoprecipitated with anti-c-Myc, and immunoblotted with anti-Flag. (E) Luciferase assay in MEFs transfected with ELAM−1 luciferase reporter and pRL-Null renilla constructs along with increasing amounts (wedge) of Fbxo16, then left untreated or stimulated with LPS for 5 hr. (F) Luciferase assay in HEK293T cells transfected with ELAM−1 luciferase reporter and pRL-Null renilla constructs without or with MyD88, IKKβ, TRAF6 or p65 along with increasing amounts (wedge) of Fbxo16. Data are representative of three (A, B) , four (C, D) or three ( E, F ; means ± SD, **P<0.01) independent experiments.

    Journal: Frontiers in Immunology

    Article Title: Fbxo16 mediates degradation of NF-κB p65 subunit and inhibits inflammatory response in dendritic cells

    doi: 10.3389/fimmu.2025.1524110

    Figure Lengend Snippet: Fbxo16 forms a CRL1 complex, binds to p65 and negatively regulates NF-κB signaling. (A) Interaction of Fbxo16 and Cullins in whole cell lysates of HEK293T cells, transfected with c-Myc-Fbxo16, then immunoprecipitated with anti-Flag, and immunoblotted with anti-Cullin 1, Cullin 2 or Cullin 3. (B) Interaction of Fbxo16 and Skp1 in whole cell lysates of HEK293T cells, transfected with c-Myc-Fbxo16, then immunoprecipitated with anti-c-Myc, and immunoblotted with anti-Skp1. (C) Interaction of Fbxo16 and p65 in whole cell lysates of HEK293T cells, transfected with a Flag-p65 or p50 along without or with c-Myc-Fbxo16, then immunoprecipitated with anti-c-Myc, and immunoblotted with anti-p65 or p50. (D) Interaction of Fbxo16 and PDLIM2 in whole cell lysates of HEK293T cells, transfected with a Flag-PDLIM2 along without or with c-Myc-Fbxo16, then immunoprecipitated with anti-c-Myc, and immunoblotted with anti-Flag. (E) Luciferase assay in MEFs transfected with ELAM−1 luciferase reporter and pRL-Null renilla constructs along with increasing amounts (wedge) of Fbxo16, then left untreated or stimulated with LPS for 5 hr. (F) Luciferase assay in HEK293T cells transfected with ELAM−1 luciferase reporter and pRL-Null renilla constructs without or with MyD88, IKKβ, TRAF6 or p65 along with increasing amounts (wedge) of Fbxo16. Data are representative of three (A, B) , four (C, D) or three ( E, F ; means ± SD, **P<0.01) independent experiments.

    Article Snippet: The pRL-Null renilla construct (#E2271) was purchased from Promega.

    Techniques: Transfection, Immunoprecipitation, Luciferase, Construct

    Fbxo16 mediates the polyubiquitination and degradation of p65 through its F-box domain. (A) Ubiquitination assay of p65 in HEK293T cells transfected with His-ubiquitin (His-Ub), p65 and increasing amounts (wedge) of Fbxo16. The purified ubiquitinated proteins were analyzed by immunoblot with anti-p65. (B) Effect of Fbxo16 on soluble and insoluble nuclear p65 in HEK293T cells transfected with Flag-p65 and increasing amounts (wedge) of c-Myc-Fbxo16, analyzed by immunoblot with ant-Flag antibody. (C) Effect of proteasome inhibitor on PDLIM2-mediated p65 degradation in soluble and insoluble nuclear extracts of HEK293T cells, transfected with Flag-p65 without or with c-Myc-Fbxo16, then left untreated or treated for 4 h with MG132 (10μM) and analyzed by immunoblot with anti-Flag antibody. (D) The structure of the wild-type Fbxo16 protein and Fbxo16 mutant lacking the F-box domain (ΔF). (E) Effect of the deletion of F-box domain on the interaction of Fbxo16 and Cullin 1 (top) or PDLIM2 (bottom) in HEK293T cells, transfected without or with c-Myc-wild-type or ΔF Fbxo16, immunoprecipitated with anti-c-Myc and immunoblotted with anti-Cullin 1 antibody (top), or transfected with Flag-PDLIM2 along with or without c-Myc-wild-type or ΔF Fbxo16, immunoprecipitated with anti-c-Myc and immunoblotted with anti-Flag antibody (bottom). (F) Ubiquitination assay of p65 in HEK293T cells cotransfected with His-ubiquitin, p65 along without or with wild-type or ΔF Fbxo16. The purified ubiquitinated proteins were analyzed by immunoblot with anti-p65. (G) Effect of the deletion of F-box domain on Fbxo16-mediated p65 degradation in soluble and insoluble nuclear extracts of HEK293T cells transfected with Flag-p65, along without or with wild-type or ΔF Fbxo16 and analyzed by immunoblot with anti-Flag antibody. (H) Luciferase assay in HEK293T cells transfected with ELAM−1 luciferase reporter, pRL-Null renilla constructs and Flag-p65 without or with wild-type or ΔF Fbxo16. Data are representative of three (A–C , E–G) or three ( H ; means ± SD, **P<0.01) independent experiments.

    Journal: Frontiers in Immunology

    Article Title: Fbxo16 mediates degradation of NF-κB p65 subunit and inhibits inflammatory response in dendritic cells

    doi: 10.3389/fimmu.2025.1524110

    Figure Lengend Snippet: Fbxo16 mediates the polyubiquitination and degradation of p65 through its F-box domain. (A) Ubiquitination assay of p65 in HEK293T cells transfected with His-ubiquitin (His-Ub), p65 and increasing amounts (wedge) of Fbxo16. The purified ubiquitinated proteins were analyzed by immunoblot with anti-p65. (B) Effect of Fbxo16 on soluble and insoluble nuclear p65 in HEK293T cells transfected with Flag-p65 and increasing amounts (wedge) of c-Myc-Fbxo16, analyzed by immunoblot with ant-Flag antibody. (C) Effect of proteasome inhibitor on PDLIM2-mediated p65 degradation in soluble and insoluble nuclear extracts of HEK293T cells, transfected with Flag-p65 without or with c-Myc-Fbxo16, then left untreated or treated for 4 h with MG132 (10μM) and analyzed by immunoblot with anti-Flag antibody. (D) The structure of the wild-type Fbxo16 protein and Fbxo16 mutant lacking the F-box domain (ΔF). (E) Effect of the deletion of F-box domain on the interaction of Fbxo16 and Cullin 1 (top) or PDLIM2 (bottom) in HEK293T cells, transfected without or with c-Myc-wild-type or ΔF Fbxo16, immunoprecipitated with anti-c-Myc and immunoblotted with anti-Cullin 1 antibody (top), or transfected with Flag-PDLIM2 along with or without c-Myc-wild-type or ΔF Fbxo16, immunoprecipitated with anti-c-Myc and immunoblotted with anti-Flag antibody (bottom). (F) Ubiquitination assay of p65 in HEK293T cells cotransfected with His-ubiquitin, p65 along without or with wild-type or ΔF Fbxo16. The purified ubiquitinated proteins were analyzed by immunoblot with anti-p65. (G) Effect of the deletion of F-box domain on Fbxo16-mediated p65 degradation in soluble and insoluble nuclear extracts of HEK293T cells transfected with Flag-p65, along without or with wild-type or ΔF Fbxo16 and analyzed by immunoblot with anti-Flag antibody. (H) Luciferase assay in HEK293T cells transfected with ELAM−1 luciferase reporter, pRL-Null renilla constructs and Flag-p65 without or with wild-type or ΔF Fbxo16. Data are representative of three (A–C , E–G) or three ( H ; means ± SD, **P<0.01) independent experiments.

    Article Snippet: The pRL-Null renilla construct (#E2271) was purchased from Promega.

    Techniques: Ubiquitin Proteomics, Transfection, Purification, Western Blot, Mutagenesis, Immunoprecipitation, Luciferase, Construct