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shcontrol plasmid  (PSICOR Inc)

 
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    PSICOR Inc shcontrol plasmid
    RGS12 can strengthen the transcriptional regulation of COX2 via NF-κB. (A) Western blot analysis of RGS12 expression. Primary BMMs were transfected with pCMV-empty (control) or pCMV-RGS12 (RGS12 OE) plasmids by Lipofectamine 3000 for 24 hours, and the expression levels of RGS12 were analyzed. **, P<0.01 vs. the control group, n=3. (B) Relative mRNA expression of COX2 was analyzed by real-time PCR. Primary BMMs were treated as described in (A), and the expression levels of COX2 were analyzed. **, P<0.01, ***, P<0.001 compared with the control group. The values are the mean ± SEM (n=5). (C) COX2 expression levels in BMMs were analyzed by ELISA. Primary BMMs were treated as described in (A), and COX2 expression levels were analyzed. Note that RGS12 OE enhanced the expression level of COX2. **, P<0.01, ***, P<0.001 compared with the control group. (D) Relative protein levels of NF-κBp65. RAW264.7 cells were transfected with <t>shControl</t> (pSicoR-empty) or shNF-κB plasmids (pSicoR-shNFκBp65-1 and pSicoR-shNFκBp65-2) for 24 hours. β-Actin was used as an internal reference. The data are presented as the means ± SEM. ***, P<0.001 vs. shControl group, n=3. (E) Western blot analysis of NF-κBp65. RAW264.7 cells were transfected with pcDNA3.1-empty (control) or pcDNA3.1-NF-κBp65 (NF-κBp65 OE) plasmids for 24 hours. β-Actin was used as an internal reference. The data are presented as the means ± SEM. ***, P<0.001 vs. the control group, n=3. (F) RAW 264.7 cells were transfected with pUC-shNF-κBp65 and/or pCMV-RGS12 for 24 hours and then induced with TNFα for 24 hours. Relative mRNA expression was measured by real-time PCR. Note that RGS12 could not increase COX2 expression when NF-κB expression was decreased. The values are the mean ± SEM. ***, P<0.001, n=5. (G) Analysis of the interactions between RGS12-PTB and NF-κBp65 by pulldown assay. RAW264.7 cells were transfected with pCMV-Flag or pCMV-PTB-Flag plasmids, and cell lysates were precipitated with anti-Flag affinity gel and immunoblotted (IB) with anti-NF-κB p65 and anti-Flag antibodies. (H) RGS12 promotes the transcriptional activity of NF-κB and COX2 expression (luciferase assay). Stable knockdown of NF-κB in RAW264.7 cells was achieved via the transfection of pSicoR-shNFκBp65-1 and pSicoR-shNFκBp65-2 vectors. The stably transfected RAW264.7 cells were treated with COX2-Luc, pcDNA3.1-NF-κBp65, pCMV-RGS12 and/or pCMV-PTB for 48 hours. *, P<0.05, ***, P<0.001 versus the control. The data are presented as the means ± SEM. Note that RGS12 or PTB could increase the transcriptional activity of NF-κB.
    Shcontrol Plasmid, supplied by PSICOR Inc, 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/product/shcontrol/shcontrol+plasmid/pmc08039686-292-5-6
    Average 90 stars, based on 1 article reviews
    shcontrol plasmid - by Bioz Stars, 2026-08
    90/100 stars

    Images

    1) Product Images from "Macrophage regulator of G-protein signaling 12 contributes to inflammatory pain hypersensitivity"

    Article Title: Macrophage regulator of G-protein signaling 12 contributes to inflammatory pain hypersensitivity

    Journal: Annals of Translational Medicine

    doi: 10.21037/atm-20-5729

    RGS12 can strengthen the transcriptional regulation of COX2 via NF-κB. (A) Western blot analysis of RGS12 expression. Primary BMMs were transfected with pCMV-empty (control) or pCMV-RGS12 (RGS12 OE) plasmids by Lipofectamine 3000 for 24 hours, and the expression levels of RGS12 were analyzed. **, P<0.01 vs. the control group, n=3. (B) Relative mRNA expression of COX2 was analyzed by real-time PCR. Primary BMMs were treated as described in (A), and the expression levels of COX2 were analyzed. **, P<0.01, ***, P<0.001 compared with the control group. The values are the mean ± SEM (n=5). (C) COX2 expression levels in BMMs were analyzed by ELISA. Primary BMMs were treated as described in (A), and COX2 expression levels were analyzed. Note that RGS12 OE enhanced the expression level of COX2. **, P<0.01, ***, P<0.001 compared with the control group. (D) Relative protein levels of NF-κBp65. RAW264.7 cells were transfected with shControl (pSicoR-empty) or shNF-κB plasmids (pSicoR-shNFκBp65-1 and pSicoR-shNFκBp65-2) for 24 hours. β-Actin was used as an internal reference. The data are presented as the means ± SEM. ***, P<0.001 vs. shControl group, n=3. (E) Western blot analysis of NF-κBp65. RAW264.7 cells were transfected with pcDNA3.1-empty (control) or pcDNA3.1-NF-κBp65 (NF-κBp65 OE) plasmids for 24 hours. β-Actin was used as an internal reference. The data are presented as the means ± SEM. ***, P<0.001 vs. the control group, n=3. (F) RAW 264.7 cells were transfected with pUC-shNF-κBp65 and/or pCMV-RGS12 for 24 hours and then induced with TNFα for 24 hours. Relative mRNA expression was measured by real-time PCR. Note that RGS12 could not increase COX2 expression when NF-κB expression was decreased. The values are the mean ± SEM. ***, P<0.001, n=5. (G) Analysis of the interactions between RGS12-PTB and NF-κBp65 by pulldown assay. RAW264.7 cells were transfected with pCMV-Flag or pCMV-PTB-Flag plasmids, and cell lysates were precipitated with anti-Flag affinity gel and immunoblotted (IB) with anti-NF-κB p65 and anti-Flag antibodies. (H) RGS12 promotes the transcriptional activity of NF-κB and COX2 expression (luciferase assay). Stable knockdown of NF-κB in RAW264.7 cells was achieved via the transfection of pSicoR-shNFκBp65-1 and pSicoR-shNFκBp65-2 vectors. The stably transfected RAW264.7 cells were treated with COX2-Luc, pcDNA3.1-NF-κBp65, pCMV-RGS12 and/or pCMV-PTB for 48 hours. *, P<0.05, ***, P<0.001 versus the control. The data are presented as the means ± SEM. Note that RGS12 or PTB could increase the transcriptional activity of NF-κB.
    Figure Legend Snippet: RGS12 can strengthen the transcriptional regulation of COX2 via NF-κB. (A) Western blot analysis of RGS12 expression. Primary BMMs were transfected with pCMV-empty (control) or pCMV-RGS12 (RGS12 OE) plasmids by Lipofectamine 3000 for 24 hours, and the expression levels of RGS12 were analyzed. **, P<0.01 vs. the control group, n=3. (B) Relative mRNA expression of COX2 was analyzed by real-time PCR. Primary BMMs were treated as described in (A), and the expression levels of COX2 were analyzed. **, P<0.01, ***, P<0.001 compared with the control group. The values are the mean ± SEM (n=5). (C) COX2 expression levels in BMMs were analyzed by ELISA. Primary BMMs were treated as described in (A), and COX2 expression levels were analyzed. Note that RGS12 OE enhanced the expression level of COX2. **, P<0.01, ***, P<0.001 compared with the control group. (D) Relative protein levels of NF-κBp65. RAW264.7 cells were transfected with shControl (pSicoR-empty) or shNF-κB plasmids (pSicoR-shNFκBp65-1 and pSicoR-shNFκBp65-2) for 24 hours. β-Actin was used as an internal reference. The data are presented as the means ± SEM. ***, P<0.001 vs. shControl group, n=3. (E) Western blot analysis of NF-κBp65. RAW264.7 cells were transfected with pcDNA3.1-empty (control) or pcDNA3.1-NF-κBp65 (NF-κBp65 OE) plasmids for 24 hours. β-Actin was used as an internal reference. The data are presented as the means ± SEM. ***, P<0.001 vs. the control group, n=3. (F) RAW 264.7 cells were transfected with pUC-shNF-κBp65 and/or pCMV-RGS12 for 24 hours and then induced with TNFα for 24 hours. Relative mRNA expression was measured by real-time PCR. Note that RGS12 could not increase COX2 expression when NF-κB expression was decreased. The values are the mean ± SEM. ***, P<0.001, n=5. (G) Analysis of the interactions between RGS12-PTB and NF-κBp65 by pulldown assay. RAW264.7 cells were transfected with pCMV-Flag or pCMV-PTB-Flag plasmids, and cell lysates were precipitated with anti-Flag affinity gel and immunoblotted (IB) with anti-NF-κB p65 and anti-Flag antibodies. (H) RGS12 promotes the transcriptional activity of NF-κB and COX2 expression (luciferase assay). Stable knockdown of NF-κB in RAW264.7 cells was achieved via the transfection of pSicoR-shNFκBp65-1 and pSicoR-shNFκBp65-2 vectors. The stably transfected RAW264.7 cells were treated with COX2-Luc, pcDNA3.1-NF-κBp65, pCMV-RGS12 and/or pCMV-PTB for 48 hours. *, P<0.05, ***, P<0.001 versus the control. The data are presented as the means ± SEM. Note that RGS12 or PTB could increase the transcriptional activity of NF-κB.

    Techniques Used: Western Blot, Expressing, Transfection, Control, Real-time Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay, Activity Assay, Luciferase, Knockdown, Stable Transfection



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    Ribavirin has synergistic effects on 5′-adenosine monophosphate (AMP)-activated protein kinase (AMPK) downregulation. (A) Three AMPK-targeting short hairpin RNAs (shRNAs) were screened to evaluate their knockdown efficiency and suppress AMPK expression in lung cancer cells. The data shown are representative of n = 3 biological replicates. (B) Tumor anatomy of mouse Lewis lung carcinoma (LLC) cells subcutaneous tumor-bearing mice in different treatment groups. (C) Tumor volume of LLC subcutaneous tumor-bearing mice in different treatment groups. Statistical significance between datasets was assessed by one-way analysis of variance (ANOVA), followed by Tukey’s multiple comparisons post hoc test between all groups. The values are the means ± standard error of the mean (SEM); n = 8 mice per group, with differences denoted by ∗ P < 0.05 and ∗∗ P < 0.01. (D) Tumor weights of LLC subcutaneous tumor-bearing mice in different treatment groups. Statistical significance between datasets was assessed by one-way ANOVA, followed by Tukey’s multiple comparisons post hoc test between all groups. The values are the means ± SEM; n = 8 mice per group, with differences denoted by ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001. (E) Schematic illustration of the mechanism by which Ribavirin regulates AMPK activation. AMPK is phosphorylated in response to an increased AMP/adenosine triphosphate (ATP) or adenosine diphosphate (ADP)/ATP ratio, influencing cell growth and proliferation by inactivating mechanistic target of rapamycin complex 1 (mTORC1). Ribavirin exerts its regulatory effect by inhibiting AMPK phosphorylation. Created with www.BioRender.com . shControl: non-targeting control short hairpin RNA; shAMPKα: AMPKα-targeting short hairpin RNA; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; PBS: phosphate buffered saline; mTOR: mechanistic target of rapamycin; Raptor: regulatory-associated protein of mTOR; Deptor: DEP domain-containing mTOR-interacting protein; PRAS40: proline-rich Akt substrate of 40 kDa; mLST8: mammalian lethal with SEC13 protein 8; 4EBP1:eukaryotic translation initiation factor 4E-binding protein 1; P: phosphorylation.

    Journal: Journal of Pharmaceutical Analysis

    Article Title: Oblique-incidence reflectivity difference technology identifies the antiviral drug Ribavirin as an inhibitor of lung tumor progression by targeting AMPK signaling

    doi: 10.1016/j.jpha.2025.101306

    Figure Lengend Snippet: Ribavirin has synergistic effects on 5′-adenosine monophosphate (AMP)-activated protein kinase (AMPK) downregulation. (A) Three AMPK-targeting short hairpin RNAs (shRNAs) were screened to evaluate their knockdown efficiency and suppress AMPK expression in lung cancer cells. The data shown are representative of n = 3 biological replicates. (B) Tumor anatomy of mouse Lewis lung carcinoma (LLC) cells subcutaneous tumor-bearing mice in different treatment groups. (C) Tumor volume of LLC subcutaneous tumor-bearing mice in different treatment groups. Statistical significance between datasets was assessed by one-way analysis of variance (ANOVA), followed by Tukey’s multiple comparisons post hoc test between all groups. The values are the means ± standard error of the mean (SEM); n = 8 mice per group, with differences denoted by ∗ P < 0.05 and ∗∗ P < 0.01. (D) Tumor weights of LLC subcutaneous tumor-bearing mice in different treatment groups. Statistical significance between datasets was assessed by one-way ANOVA, followed by Tukey’s multiple comparisons post hoc test between all groups. The values are the means ± SEM; n = 8 mice per group, with differences denoted by ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001. (E) Schematic illustration of the mechanism by which Ribavirin regulates AMPK activation. AMPK is phosphorylated in response to an increased AMP/adenosine triphosphate (ATP) or adenosine diphosphate (ADP)/ATP ratio, influencing cell growth and proliferation by inactivating mechanistic target of rapamycin complex 1 (mTORC1). Ribavirin exerts its regulatory effect by inhibiting AMPK phosphorylation. Created with www.BioRender.com . shControl: non-targeting control short hairpin RNA; shAMPKα: AMPKα-targeting short hairpin RNA; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; PBS: phosphate buffered saline; mTOR: mechanistic target of rapamycin; Raptor: regulatory-associated protein of mTOR; Deptor: DEP domain-containing mTOR-interacting protein; PRAS40: proline-rich Akt substrate of 40 kDa; mLST8: mammalian lethal with SEC13 protein 8; 4EBP1:eukaryotic translation initiation factor 4E-binding protein 1; P: phosphorylation.

    Article Snippet: The mice were randomly divided into four groups ( n = 8): the non-targeting control short hairpin RNA (shControl)-LLC + phosphate buffered saline (PBS) (Sangon Biotech, Shanghai, China) group, shControl-LLC + Ribavirin group, shAMPKα-LLC + PBS group, and shAMPKα-LLC + Ribavirin group.

    Techniques: Knockdown, Expressing, Activation Assay, Phospho-proteomics, Control, shRNA, Saline, Binding Assay