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  • 98
    Millipore lentivirus particles
    PPARγ knockdown does not prevent the anti-inflammatory effects of TZDs in HASM cells. ( A ) PPARγ mRNA level in HASM cells that were transduced with <t>lentivirus</t> transduction particles containing nontarget short hairpin RNA (shRNA) (control; Ctr) or PPARγ-target shRNA. Successfully transduced cells were selected by puromycin, expanded, and used in this study. ( B , C ) Pooled results of all four constructs from two donor cell lines. Results are normalized to maximal release of cytokine with IL-1β stimulation from the same donor treated with control shRNA, and are presented as mean ± SE. * P
    Lentivirus Particles, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 735 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Cyagen Biosciences lentivirus particles
    Effect of intra‐articular NR4A3 overexpression and knockdown on rat OA model. Seventy‐five rats were used here, and they were randomly divided into five groups (15 rats in each group). The rats in the Sham group received sham surgery as blank control. The other 60 rats received surgical remove of medial meniscus and were regarded as OA rats. Twenty μL <t>lentivirus‐overexpressing</t> NR4A3 particles (1 × 10 8 TU/mL) were injected intra‐articularly in OA rats every 2 wk in the Lenti‐OE group 1 wk post‐surgery. Lentivirus‐control particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐NC group. <t>Lentivirus‐shNR4A3</t> particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐KD group. Lentivirus‐shcontrol particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐shCon group. (A) Microscopic images of safranin O‐stained and NR4A3‐ and COX‐2‐stained immunofluorescence analysis of rat knee joint sections. (B) Quantitation of immunofluorescence analysis (obtained from experiments of 5 knees each group) and OARSI grading system (0‐6) (obtained from experiments of 10 knees each group) was used to evaluate the sections. * P
    Lentivirus Particles, supplied by Cyagen Biosciences, used in various techniques. Bioz Stars score: 96/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Santa Cruz Biotechnology lentivirus particles
    Effect of intra‐articular NR4A3 overexpression and knockdown on rat OA model. Seventy‐five rats were used here, and they were randomly divided into five groups (15 rats in each group). The rats in the Sham group received sham surgery as blank control. The other 60 rats received surgical remove of medial meniscus and were regarded as OA rats. Twenty μL <t>lentivirus‐overexpressing</t> NR4A3 particles (1 × 10 8 TU/mL) were injected intra‐articularly in OA rats every 2 wk in the Lenti‐OE group 1 wk post‐surgery. Lentivirus‐control particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐NC group. <t>Lentivirus‐shNR4A3</t> particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐KD group. Lentivirus‐shcontrol particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐shCon group. (A) Microscopic images of safranin O‐stained and NR4A3‐ and COX‐2‐stained immunofluorescence analysis of rat knee joint sections. (B) Quantitation of immunofluorescence analysis (obtained from experiments of 5 knees each group) and OARSI grading system (0‐6) (obtained from experiments of 10 knees each group) was used to evaluate the sections. * P
    Lentivirus Particles, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 77 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher lentivirus particles
    Reduced proliferation in CENP-A and PLK1 knockdown β-cell lines (A) Western blot of CENP-A and α-tubulin in β-cell lines transduced with <t>lentivirus</t> expressing sh-scramble or sh-CENP-A. (B) MTT assay in indicated cells. *p
    Lentivirus Particles, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 698 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Horizon Discovery lentivirus particles
    Reduced proliferation in CENP-A and PLK1 knockdown β-cell lines (A) Western blot of CENP-A and α-tubulin in β-cell lines transduced with <t>lentivirus</t> expressing sh-scramble or sh-CENP-A. (B) MTT assay in indicated cells. *p
    Lentivirus Particles, supplied by Horizon Discovery, used in various techniques. Bioz Stars score: 93/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Shanghai GenePharma particles lentivirus
    Reduced proliferation in CENP-A and PLK1 knockdown β-cell lines (A) Western blot of CENP-A and α-tubulin in β-cell lines transduced with <t>lentivirus</t> expressing sh-scramble or sh-CENP-A. (B) MTT assay in indicated cells. *p
    Particles Lentivirus, supplied by Shanghai GenePharma, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Genechem lentivirus particles
    miR-3174 Suppresses Cellular Autophagy and Inhibits Autophagic Cell Death in GC Cells (A) Cells infected with <t>lentivirus</t> particles for expression of GFP-mRFP-LC3 were plated into a 35-mm confocal culture dish, and cellular puncta were observed using confocal microscopy (63× objective magnification; scale bar, 20 μm) after 48 hr. The areas enclosed in white squares were further amplified. (B) Yellow and red puncta were counted as mentioned in the Materials and Methods . (C) Transmission electron microscopy (TEM) detection of autophagic microstructures in cells. The green arrows refer to cellular autophagosome that has a double layer structure or autolysosome generated by fusion of autophagosome with lysosome. The areas enclosed within green squares were further amplified with TEM (2,500× and 8,800× magnification; scale bar, 2 μm and 500 nm). (D and E) LC3-II protein levels were calculated in MKN45 (D) and BGC823 (E) cells with or without chloroquine (CQ, 10 μM for 2 hr) or 3-methyladenine (3-MA, 2 mM for 24 hr) treatment or nutritional deprivation for 48 hr. The upper band of LC3, LC3-I; the lower band, LC3-II. (F) The protein levels of BECN1 and SQSTM1/p62 were assessed with western blotting. (G) LC3-II levels were detected after transfected BGC823 cells with siATG5, siBECN1, or siNC and treated cells with 3-methyladenine (3-MA, 2 mM for 24 hr), Wortmannin (WMT, 10 μM for 24 hr), or DMSO. (H) Cell viability was quantified in BGC823 cells with the same treatment and with or without miR-3174 inhibition. β-actin was used as an internal control. Graph represents mean ± SEM; *p
    Lentivirus Particles, supplied by Genechem, used in various techniques. Bioz Stars score: 93/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Shanghai Genechem lentivirus particles
    DEPDC1 depletion inhibits tumor growth in vivo (A) CNE-1 cells were infected with <t>lentivirus</t> particles expressing negative control and DEPDC1 shRNA, and then subjected to establish the negative control (shNC) and DEPDC1 stable knockdown (shDEPDC1) cells with puromycin selection. Quantitative RT-PCR and immunoblotting were used to confirm the stable knockdown effect of DEPDC1 expression. Optical densities (O.D.) of individual bands on immunoblots were quantified as described in Figure 2B . (B) The stable control cells (shNC) and DEPDC1 knockdown cells (shDEPDC1) were injected subcutaneously into the right and left dorsal flank of nude mice, respectively. The mice were sacrificed thirty days after injection. (C) The tumor weight was measured at the end of the experiment, and the tumor size was measured about twice a week for tumor growth curve construction. ( P *
    Lentivirus Particles, supplied by Shanghai Genechem, used in various techniques. Bioz Stars score: 91/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    OriGene shcdk2 lentivirus particles
    DEPDC1 depletion inhibits tumor growth in vivo (A) CNE-1 cells were infected with <t>lentivirus</t> particles expressing negative control and DEPDC1 shRNA, and then subjected to establish the negative control (shNC) and DEPDC1 stable knockdown (shDEPDC1) cells with puromycin selection. Quantitative RT-PCR and immunoblotting were used to confirm the stable knockdown effect of DEPDC1 expression. Optical densities (O.D.) of individual bands on immunoblots were quantified as described in Figure 2B . (B) The stable control cells (shNC) and DEPDC1 knockdown cells (shDEPDC1) were injected subcutaneously into the right and left dorsal flank of nude mice, respectively. The mice were sacrificed thirty days after injection. (C) The tumor weight was measured at the end of the experiment, and the tumor size was measured about twice a week for tumor growth curve construction. ( P *
    Shcdk2 Lentivirus Particles, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    TaKaRa generation lentivirus particles
    DEPDC1 depletion inhibits tumor growth in vivo (A) CNE-1 cells were infected with <t>lentivirus</t> particles expressing negative control and DEPDC1 shRNA, and then subjected to establish the negative control (shNC) and DEPDC1 stable knockdown (shDEPDC1) cells with puromycin selection. Quantitative RT-PCR and immunoblotting were used to confirm the stable knockdown effect of DEPDC1 expression. Optical densities (O.D.) of individual bands on immunoblots were quantified as described in Figure 2B . (B) The stable control cells (shNC) and DEPDC1 knockdown cells (shDEPDC1) were injected subcutaneously into the right and left dorsal flank of nude mice, respectively. The mice were sacrificed thirty days after injection. (C) The tumor weight was measured at the end of the experiment, and the tumor size was measured about twice a week for tumor growth curve construction. ( P *
    Generation Lentivirus Particles, supplied by TaKaRa, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Santa Cruz Biotechnology lentivirus mif shrna lentiviral particles
    HIF1A Regulated Chondro-Osteogenic Differentiation of CESCs by <t>MIF</t> CESCs assigned to normoxia + PBS (NP) and hypoxia + YC1 (HY) groups, in which MIF expression should have been relatively low, were transfected with MIF -overexpressing <t>lentiviral</t> vector system (M+) and its scramble control (Scr). CESCs assigned to normoxia + DMOG (ND) and hypoxia + PBS (HP) groups in which MIF expression should had been relatively high were transfected with MIF <t>-shRNA</t> (M−) and its scramble control (Scr). (A) SOX9 , COL2 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in CIM. (B and C) Western blot analysis of the expression of SOX9, COL2, HIF1A, and MIF in samples treated under the conditions in (A). (D) RUNX2 , COL1 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in OIM. (E and F) Western blot analysis of the expression of RUNX2, COL1, HIF1A, and MIF in the samples treated under the conditions in (D). (G) Macrographs of alizarin red staining and ALP staining of CESCs treated under the conditions in (D). Data represent the mean ± SD (n = 3 independent experiments, t test). ∗ p
    Lentivirus Mif Shrna Lentiviral Particles, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher gipz lentivirus particles
    HIF1A Regulated Chondro-Osteogenic Differentiation of CESCs by <t>MIF</t> CESCs assigned to normoxia + PBS (NP) and hypoxia + YC1 (HY) groups, in which MIF expression should have been relatively low, were transfected with MIF -overexpressing <t>lentiviral</t> vector system (M+) and its scramble control (Scr). CESCs assigned to normoxia + DMOG (ND) and hypoxia + PBS (HP) groups in which MIF expression should had been relatively high were transfected with MIF <t>-shRNA</t> (M−) and its scramble control (Scr). (A) SOX9 , COL2 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in CIM. (B and C) Western blot analysis of the expression of SOX9, COL2, HIF1A, and MIF in samples treated under the conditions in (A). (D) RUNX2 , COL1 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in OIM. (E and F) Western blot analysis of the expression of RUNX2, COL1, HIF1A, and MIF in the samples treated under the conditions in (D). (G) Macrographs of alizarin red staining and ALP staining of CESCs treated under the conditions in (D). Data represent the mean ± SD (n = 3 independent experiments, t test). ∗ p
    Gipz Lentivirus Particles, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    GenTarget camk4 inducible lentivirus particles
    HIF1A Regulated Chondro-Osteogenic Differentiation of CESCs by <t>MIF</t> CESCs assigned to normoxia + PBS (NP) and hypoxia + YC1 (HY) groups, in which MIF expression should have been relatively low, were transfected with MIF -overexpressing <t>lentiviral</t> vector system (M+) and its scramble control (Scr). CESCs assigned to normoxia + DMOG (ND) and hypoxia + PBS (HP) groups in which MIF expression should had been relatively high were transfected with MIF <t>-shRNA</t> (M−) and its scramble control (Scr). (A) SOX9 , COL2 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in CIM. (B and C) Western blot analysis of the expression of SOX9, COL2, HIF1A, and MIF in samples treated under the conditions in (A). (D) RUNX2 , COL1 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in OIM. (E and F) Western blot analysis of the expression of RUNX2, COL1, HIF1A, and MIF in the samples treated under the conditions in (D). (G) Macrographs of alizarin red staining and ALP staining of CESCs treated under the conditions in (D). Data represent the mean ± SD (n = 3 independent experiments, t test). ∗ p
    Camk4 Inducible Lentivirus Particles, supplied by GenTarget, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Santa Cruz Biotechnology copgfp control lentivirus particles
    HIF1A Regulated Chondro-Osteogenic Differentiation of CESCs by <t>MIF</t> CESCs assigned to normoxia + PBS (NP) and hypoxia + YC1 (HY) groups, in which MIF expression should have been relatively low, were transfected with MIF -overexpressing <t>lentiviral</t> vector system (M+) and its scramble control (Scr). CESCs assigned to normoxia + DMOG (ND) and hypoxia + PBS (HP) groups in which MIF expression should had been relatively high were transfected with MIF <t>-shRNA</t> (M−) and its scramble control (Scr). (A) SOX9 , COL2 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in CIM. (B and C) Western blot analysis of the expression of SOX9, COL2, HIF1A, and MIF in samples treated under the conditions in (A). (D) RUNX2 , COL1 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in OIM. (E and F) Western blot analysis of the expression of RUNX2, COL1, HIF1A, and MIF in the samples treated under the conditions in (D). (G) Macrographs of alizarin red staining and ALP staining of CESCs treated under the conditions in (D). Data represent the mean ± SD (n = 3 independent experiments, t test). ∗ p
    Copgfp Control Lentivirus Particles, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    GenePharma Company c10orf99 overexpressing lentivirus particles
    <t>C10orf99</t> regulates the keratinocyte proliferation by activating ERK1/2 and NF-κB pathways. ( a ) HaCaT cells were treated with M5 for 15, 30 and 60 min, and the phosphorylation of NF-κB p65, ERK1/2 and AKT were detected by western blot. ( b ) HaCaT cells were transfected with C10orf99 siRNAs for 48 h and then incubated with M5 for 30 min. Cells were lysed for western blot analysis on indicated proteins. ( c ) Phosphorylation of NF-κB p65, ERK1/2 and AKT were analysed by western blot in HaCaT cells transduced with lentiviral particles. β-actin was used as an internal control. Date are representative of three independent experiments. Ctrl, control; BLK, blank transfected group; LV-Ctrl, vector transfected group; LV-C10orf99, C10orf99-expressing <t>lentiviruses</t> transfected group.
    C10orf99 Overexpressing Lentivirus Particles, supplied by GenePharma Company, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    GenTarget gfp lentivirus particles
    <t>C10orf99</t> regulates the keratinocyte proliferation by activating ERK1/2 and NF-κB pathways. ( a ) HaCaT cells were treated with M5 for 15, 30 and 60 min, and the phosphorylation of NF-κB p65, ERK1/2 and AKT were detected by western blot. ( b ) HaCaT cells were transfected with C10orf99 siRNAs for 48 h and then incubated with M5 for 30 min. Cells were lysed for western blot analysis on indicated proteins. ( c ) Phosphorylation of NF-κB p65, ERK1/2 and AKT were analysed by western blot in HaCaT cells transduced with lentiviral particles. β-actin was used as an internal control. Date are representative of three independent experiments. Ctrl, control; BLK, blank transfected group; LV-Ctrl, vector transfected group; LV-C10orf99, C10orf99-expressing <t>lentiviruses</t> transfected group.
    Gfp Lentivirus Particles, supplied by GenTarget, used in various techniques. Bioz Stars score: 91/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    GenTarget tβrii inducible lentivirus particles
    <t>C10orf99</t> regulates the keratinocyte proliferation by activating ERK1/2 and NF-κB pathways. ( a ) HaCaT cells were treated with M5 for 15, 30 and 60 min, and the phosphorylation of NF-κB p65, ERK1/2 and AKT were detected by western blot. ( b ) HaCaT cells were transfected with C10orf99 siRNAs for 48 h and then incubated with M5 for 30 min. Cells were lysed for western blot analysis on indicated proteins. ( c ) Phosphorylation of NF-κB p65, ERK1/2 and AKT were analysed by western blot in HaCaT cells transduced with lentiviral particles. β-actin was used as an internal control. Date are representative of three independent experiments. Ctrl, control; BLK, blank transfected group; LV-Ctrl, vector transfected group; LV-C10orf99, C10orf99-expressing <t>lentiviruses</t> transfected group.
    Tβrii Inducible Lentivirus Particles, supplied by GenTarget, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore lentivirus transduction particles
    <t>C10orf99</t> regulates the keratinocyte proliferation by activating ERK1/2 and NF-κB pathways. ( a ) HaCaT cells were treated with M5 for 15, 30 and 60 min, and the phosphorylation of NF-κB p65, ERK1/2 and AKT were detected by western blot. ( b ) HaCaT cells were transfected with C10orf99 siRNAs for 48 h and then incubated with M5 for 30 min. Cells were lysed for western blot analysis on indicated proteins. ( c ) Phosphorylation of NF-κB p65, ERK1/2 and AKT were analysed by western blot in HaCaT cells transduced with lentiviral particles. β-actin was used as an internal control. Date are representative of three independent experiments. Ctrl, control; BLK, blank transfected group; LV-Ctrl, vector transfected group; LV-C10orf99, C10orf99-expressing <t>lentiviruses</t> transfected group.
    Lentivirus Transduction Particles, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Genecopoeia lentivirus particles
    Inhibition of Cx43 expression increases cellular resistance to VacA toxicity. (A) AZ-521 cells were transduced with <t>lentivirus</t> particles encoding nontargeting (NT) shRNA or two different Cx43-specific shRNAs (83010 and 83012), and cells stably expressing the shRNAs were selected. Expression of the Cx43 protein was analyzed by Western blotting using an anti-Cx43 antibody. Expression of β-actin was monitored to ensure equal loading. The effect of shRNA treatment on Cx43 production was evaluated by densitometry. Cx43 expression was decreased in Cx43 shRNA-expressing cells compared to that in cells expressing NT shRNA. (B to E) Control AZ-521 cells (NT) and cells expressing Cx43-specific shRNA (83010 or 83012) were incubated with serial dilutions of H. pylori broth culture supernatants containing WT VacA (B and D) or the inactive mutant protein VacA-G14A (C and E). After 24 h, cell viability was determined by the ATPlite assay. The Cx43-specific shRNA conferred a protective effect in the experiments shown in panels B and D but not in the experiments shown in panels C and E. A low level of cell death in response to high concentrations of supernatants containing VacA-G14A is attributed to nonspecific effects. Error bars represent means plus standard errors from combined results of two independent experiments, each performed in triplicate. Asterisks indicate P
    Lentivirus Particles, supplied by Genecopoeia, used in various techniques. Bioz Stars score: 92/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Addgene inc lentivirus particles
    C-terminal fragment of iOPN binds to TRAF3. ( A ) Schematic structure of iOPN-WT and its mutant iOPN-N and iOPN-C containing the N-terminal and C-terminal fragment of iOPN divided in the thrombin cleaved site. ( B ) TRAF3, Flag-iOPN-WT, Flag-iOPN-N, Flag-iOPN-C protein were obtained by in vitro transcription and translation. Interaction between TRAF3 and iOPN truncations was assayed by mixing TRAF3 and iOPN truncations together followed by IP with Flag antibody and western blot with TRAF3 antibody. ( C ) TRAF3, Triad3A, Flag-iOPN-WT, Flag-iOPN-N, Flag-iOPN-C protein were obtained by in vitro transcription and translation. In vitro ubiquitination assays were performed in the presence of Ub, E1, UbcH5c, TRAF3, Triad3A and iOPN-WT, iOPN-N or iOPN-C. The ubiquitination of TRAF3 was examined by western blot with TRAF3 antibody. ( D ) Peritoneal macrophages from WT and OPN-deficient ( Spp1 −/− ) mice which were infected with <t>lentivirus</t> (MOI, 50) containing iOPN-WT expression plasmid or control plasmid, 4 days later, OPN protein level were assayed by using WB. ( E ) Peritoneal macrophages from WT and OPN-deficient ( Spp1 −/− ) mice were infected with lentivirus (MOI, 50) containing control vector, iOPN-WT, iOPN-N or iOPN-C for 4 days, then infected with SeV for 8 h or left uninfected, qRT-PCR analysis of IFN-β was performed. The data are representative of three biological replicates (mean ± S.D. in E ).
    Lentivirus Particles, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 432 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    TaKaRa lentivirus particles
    APLNR regulates CXCR4 expression through miR-139-5p. ( a , b ) CXCR4 expression in response to shear stress exposure in HUVECs, with or without concurrent APLNR knockdown. mRNA ( a ) and protein levels ( b ) are shown. ( c ) CXCR4 expression in response to AGO2 knockdown. ( d ) CXCR4 expression in response to shear stress exposure in HUVECs, with or without concurrent AGO2 knockdown. ( e ) Determination of miR-139-5p levels in FACS sorted ECs from P5 retinas of Aplnr −/− , Apln −/− mice and respective littermates. n= 3 retinas per genotype. ( f ) CXCR4 expression in HUVECs overexpressing miR-139-5p mimic or non-targeting control anti-miR. ( g ) Expression levels of miR-139-5p in response to shear stress, with or without concurrent APLNR knockdown. ( h ) CXCR4 expression in HUVECs in response to shear stress exposure, with or without concurrent miR-139-5p inhibition via anti-miR. ( i ) Sprouting assay using HUVEC covered beads transduced with miR-139-5p or control <t>lentivirus</t> in response to SDF-1α or VEGF 165. Scale bar, 175 μm. ( j ) Migration assay of HUVECs transduced with miR-139-5p or control lentivirus in response to SDF-1α. Scale bar, 200 μm. * P
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    PPARγ knockdown does not prevent the anti-inflammatory effects of TZDs in HASM cells. ( A ) PPARγ mRNA level in HASM cells that were transduced with lentivirus transduction particles containing nontarget short hairpin RNA (shRNA) (control; Ctr) or PPARγ-target shRNA. Successfully transduced cells were selected by puromycin, expanded, and used in this study. ( B , C ) Pooled results of all four constructs from two donor cell lines. Results are normalized to maximal release of cytokine with IL-1β stimulation from the same donor treated with control shRNA, and are presented as mean ± SE. * P

    Journal: American Journal of Respiratory Cell and Molecular Biology

    Article Title: Anti-inflammatory Effects of Thiazolidinediones in Human Airway Smooth Muscle Cells

    doi: 10.1165/rcmb.2009-0445OC

    Figure Lengend Snippet: PPARγ knockdown does not prevent the anti-inflammatory effects of TZDs in HASM cells. ( A ) PPARγ mRNA level in HASM cells that were transduced with lentivirus transduction particles containing nontarget short hairpin RNA (shRNA) (control; Ctr) or PPARγ-target shRNA. Successfully transduced cells were selected by puromycin, expanded, and used in this study. ( B , C ) Pooled results of all four constructs from two donor cell lines. Results are normalized to maximal release of cytokine with IL-1β stimulation from the same donor treated with control shRNA, and are presented as mean ± SE. * P

    Article Snippet: Short hairpin RNA against human PPARγ (the National Center for Biotechnology Information (NCBI) accession number ) was delivered via vectors in lentivirus particles (Mission Lentiviral Transduction Particles; Sigma Chemical Co.) (see online supplement for details).

    Techniques: Transduction, shRNA, Construct

    Effect of intra‐articular NR4A3 overexpression and knockdown on rat OA model. Seventy‐five rats were used here, and they were randomly divided into five groups (15 rats in each group). The rats in the Sham group received sham surgery as blank control. The other 60 rats received surgical remove of medial meniscus and were regarded as OA rats. Twenty μL lentivirus‐overexpressing NR4A3 particles (1 × 10 8 TU/mL) were injected intra‐articularly in OA rats every 2 wk in the Lenti‐OE group 1 wk post‐surgery. Lentivirus‐control particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐NC group. Lentivirus‐shNR4A3 particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐KD group. Lentivirus‐shcontrol particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐shCon group. (A) Microscopic images of safranin O‐stained and NR4A3‐ and COX‐2‐stained immunofluorescence analysis of rat knee joint sections. (B) Quantitation of immunofluorescence analysis (obtained from experiments of 5 knees each group) and OARSI grading system (0‐6) (obtained from experiments of 10 knees each group) was used to evaluate the sections. * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: The pro‐inflammatory effect of NR4A3 in osteoarthritis, et al. The pro‐inflammatory effect of NR4A3 in osteoarthritis

    doi: 10.1111/jcmm.14804

    Figure Lengend Snippet: Effect of intra‐articular NR4A3 overexpression and knockdown on rat OA model. Seventy‐five rats were used here, and they were randomly divided into five groups (15 rats in each group). The rats in the Sham group received sham surgery as blank control. The other 60 rats received surgical remove of medial meniscus and were regarded as OA rats. Twenty μL lentivirus‐overexpressing NR4A3 particles (1 × 10 8 TU/mL) were injected intra‐articularly in OA rats every 2 wk in the Lenti‐OE group 1 wk post‐surgery. Lentivirus‐control particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐NC group. Lentivirus‐shNR4A3 particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐KD group. Lentivirus‐shcontrol particles at the same dose were injected intra‐articularly in OA rats in the Lenti‐shCon group. (A) Microscopic images of safranin O‐stained and NR4A3‐ and COX‐2‐stained immunofluorescence analysis of rat knee joint sections. (B) Quantitation of immunofluorescence analysis (obtained from experiments of 5 knees each group) and OARSI grading system (0‐6) (obtained from experiments of 10 knees each group) was used to evaluate the sections. * P

    Article Snippet: Lentivirus‐shNR4A3 particles were prepared by Cyagen Biosciences Inc The sequence (sense: 5′‐GCGUACAGAUAGUCUGAAATT‐3′, loop: CTCGAG, antisense: 5′‐UUUCAGACUAUCUGUACGCTT‐3′) was designed according to the sequence of siRNA used in knockdown experiments in vitro.

    Techniques: Over Expression, Injection, Staining, Immunofluorescence, Quantitation Assay

    Reduced proliferation in CENP-A and PLK1 knockdown β-cell lines (A) Western blot of CENP-A and α-tubulin in β-cell lines transduced with lentivirus expressing sh-scramble or sh-CENP-A. (B) MTT assay in indicated cells. *p

    Journal: Cell metabolism

    Article Title: Insulin signaling regulates the FoxM1/PLK1/CENP-A pathway to promote adaptive pancreatic β-cell proliferation

    doi: 10.1016/j.cmet.2017.02.004

    Figure Lengend Snippet: Reduced proliferation in CENP-A and PLK1 knockdown β-cell lines (A) Western blot of CENP-A and α-tubulin in β-cell lines transduced with lentivirus expressing sh-scramble or sh-CENP-A. (B) MTT assay in indicated cells. *p

    Article Snippet: Lentivirus particles were generated by following the manufacturer’s recommendation (Open Biosystems).

    Techniques: Western Blot, Transduction, Expressing, MTT Assay

    miR-3174 Suppresses Cellular Autophagy and Inhibits Autophagic Cell Death in GC Cells (A) Cells infected with lentivirus particles for expression of GFP-mRFP-LC3 were plated into a 35-mm confocal culture dish, and cellular puncta were observed using confocal microscopy (63× objective magnification; scale bar, 20 μm) after 48 hr. The areas enclosed in white squares were further amplified. (B) Yellow and red puncta were counted as mentioned in the Materials and Methods . (C) Transmission electron microscopy (TEM) detection of autophagic microstructures in cells. The green arrows refer to cellular autophagosome that has a double layer structure or autolysosome generated by fusion of autophagosome with lysosome. The areas enclosed within green squares were further amplified with TEM (2,500× and 8,800× magnification; scale bar, 2 μm and 500 nm). (D and E) LC3-II protein levels were calculated in MKN45 (D) and BGC823 (E) cells with or without chloroquine (CQ, 10 μM for 2 hr) or 3-methyladenine (3-MA, 2 mM for 24 hr) treatment or nutritional deprivation for 48 hr. The upper band of LC3, LC3-I; the lower band, LC3-II. (F) The protein levels of BECN1 and SQSTM1/p62 were assessed with western blotting. (G) LC3-II levels were detected after transfected BGC823 cells with siATG5, siBECN1, or siNC and treated cells with 3-methyladenine (3-MA, 2 mM for 24 hr), Wortmannin (WMT, 10 μM for 24 hr), or DMSO. (H) Cell viability was quantified in BGC823 cells with the same treatment and with or without miR-3174 inhibition. β-actin was used as an internal control. Graph represents mean ± SEM; *p

    Journal: Molecular Therapy. Nucleic Acids

    Article Title: miR-3174 Contributes to Apoptosis and Autophagic Cell Death Defects in Gastric Cancer Cells by Targeting ARHGAP10

    doi: 10.1016/j.omtn.2017.10.008

    Figure Lengend Snippet: miR-3174 Suppresses Cellular Autophagy and Inhibits Autophagic Cell Death in GC Cells (A) Cells infected with lentivirus particles for expression of GFP-mRFP-LC3 were plated into a 35-mm confocal culture dish, and cellular puncta were observed using confocal microscopy (63× objective magnification; scale bar, 20 μm) after 48 hr. The areas enclosed in white squares were further amplified. (B) Yellow and red puncta were counted as mentioned in the Materials and Methods . (C) Transmission electron microscopy (TEM) detection of autophagic microstructures in cells. The green arrows refer to cellular autophagosome that has a double layer structure or autolysosome generated by fusion of autophagosome with lysosome. The areas enclosed within green squares were further amplified with TEM (2,500× and 8,800× magnification; scale bar, 2 μm and 500 nm). (D and E) LC3-II protein levels were calculated in MKN45 (D) and BGC823 (E) cells with or without chloroquine (CQ, 10 μM for 2 hr) or 3-methyladenine (3-MA, 2 mM for 24 hr) treatment or nutritional deprivation for 48 hr. The upper band of LC3, LC3-I; the lower band, LC3-II. (F) The protein levels of BECN1 and SQSTM1/p62 were assessed with western blotting. (G) LC3-II levels were detected after transfected BGC823 cells with siATG5, siBECN1, or siNC and treated cells with 3-methyladenine (3-MA, 2 mM for 24 hr), Wortmannin (WMT, 10 μM for 24 hr), or DMSO. (H) Cell viability was quantified in BGC823 cells with the same treatment and with or without miR-3174 inhibition. β-actin was used as an internal control. Graph represents mean ± SEM; *p

    Article Snippet: AP Detection by Using GFP-mRFP-LC3 After transfection with different lentiviruses encoding miR-3174 or ARHGAP10-expression plasmids, GC cells were infected with lentivirus particles for expression of GFP-mRFP-LC3 (Genechem, Shanghai, China) and subjected to puromycin selection for another 2 months.

    Techniques: Infection, Expressing, Confocal Microscopy, Amplification, Transmission Assay, Electron Microscopy, Transmission Electron Microscopy, Generated, Western Blot, Transfection, Inhibition

    DEPDC1 depletion inhibits tumor growth in vivo (A) CNE-1 cells were infected with lentivirus particles expressing negative control and DEPDC1 shRNA, and then subjected to establish the negative control (shNC) and DEPDC1 stable knockdown (shDEPDC1) cells with puromycin selection. Quantitative RT-PCR and immunoblotting were used to confirm the stable knockdown effect of DEPDC1 expression. Optical densities (O.D.) of individual bands on immunoblots were quantified as described in Figure 2B . (B) The stable control cells (shNC) and DEPDC1 knockdown cells (shDEPDC1) were injected subcutaneously into the right and left dorsal flank of nude mice, respectively. The mice were sacrificed thirty days after injection. (C) The tumor weight was measured at the end of the experiment, and the tumor size was measured about twice a week for tumor growth curve construction. ( P *

    Journal: Oncotarget

    Article Title: DEPDC1 is required for cell cycle progression and motility in nasopharyngeal carcinoma

    doi: 10.18632/oncotarget.18868

    Figure Lengend Snippet: DEPDC1 depletion inhibits tumor growth in vivo (A) CNE-1 cells were infected with lentivirus particles expressing negative control and DEPDC1 shRNA, and then subjected to establish the negative control (shNC) and DEPDC1 stable knockdown (shDEPDC1) cells with puromycin selection. Quantitative RT-PCR and immunoblotting were used to confirm the stable knockdown effect of DEPDC1 expression. Optical densities (O.D.) of individual bands on immunoblots were quantified as described in Figure 2B . (B) The stable control cells (shNC) and DEPDC1 knockdown cells (shDEPDC1) were injected subcutaneously into the right and left dorsal flank of nude mice, respectively. The mice were sacrificed thirty days after injection. (C) The tumor weight was measured at the end of the experiment, and the tumor size was measured about twice a week for tumor growth curve construction. ( P *

    Article Snippet: The lentivirus particles were packaged and prepared by cotransfection of the lentiviral vectors and pHelper vectors (Shanghai Genechem) into 293T cells by Lipofectamine 2000 (Invitrogen), followed by routine culture supernatant collection and concentration.

    Techniques: In Vivo, Infection, Expressing, Negative Control, shRNA, Selection, Quantitative RT-PCR, Western Blot, Injection, Mouse Assay

    HIF1A Regulated Chondro-Osteogenic Differentiation of CESCs by MIF CESCs assigned to normoxia + PBS (NP) and hypoxia + YC1 (HY) groups, in which MIF expression should have been relatively low, were transfected with MIF -overexpressing lentiviral vector system (M+) and its scramble control (Scr). CESCs assigned to normoxia + DMOG (ND) and hypoxia + PBS (HP) groups in which MIF expression should had been relatively high were transfected with MIF -shRNA (M−) and its scramble control (Scr). (A) SOX9 , COL2 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in CIM. (B and C) Western blot analysis of the expression of SOX9, COL2, HIF1A, and MIF in samples treated under the conditions in (A). (D) RUNX2 , COL1 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in OIM. (E and F) Western blot analysis of the expression of RUNX2, COL1, HIF1A, and MIF in the samples treated under the conditions in (D). (G) Macrographs of alizarin red staining and ALP staining of CESCs treated under the conditions in (D). Data represent the mean ± SD (n = 3 independent experiments, t test). ∗ p

    Journal: Stem Cell Reports

    Article Title: MIF Plays a Key Role in Regulating Tissue-Specific Chondro-Osteogenic Differentiation Fate of Human Cartilage Endplate Stem Cells under Hypoxia

    doi: 10.1016/j.stemcr.2016.07.003

    Figure Lengend Snippet: HIF1A Regulated Chondro-Osteogenic Differentiation of CESCs by MIF CESCs assigned to normoxia + PBS (NP) and hypoxia + YC1 (HY) groups, in which MIF expression should have been relatively low, were transfected with MIF -overexpressing lentiviral vector system (M+) and its scramble control (Scr). CESCs assigned to normoxia + DMOG (ND) and hypoxia + PBS (HP) groups in which MIF expression should had been relatively high were transfected with MIF -shRNA (M−) and its scramble control (Scr). (A) SOX9 , COL2 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in CIM. (B and C) Western blot analysis of the expression of SOX9, COL2, HIF1A, and MIF in samples treated under the conditions in (A). (D) RUNX2 , COL1 , HIF1A , and MIF gene expression were assessed by RT-PCR of mRNA from CESCs induced in OIM. (E and F) Western blot analysis of the expression of RUNX2, COL1, HIF1A, and MIF in the samples treated under the conditions in (D). (G) Macrographs of alizarin red staining and ALP staining of CESCs treated under the conditions in (D). Data represent the mean ± SD (n = 3 independent experiments, t test). ∗ p

    Article Snippet: Lentivirus MIF shRNA lentiviral particles (Santa Cruz Biotechnology, sc-37137-V) and scrambled shRNA lentiviral particles (Santa Cruz, sc-108080) were purchased for the knockdown of MIF expression (accession no. Genbank: NM_002415.1 ).

    Techniques: Expressing, Transfection, Plasmid Preparation, shRNA, Reverse Transcription Polymerase Chain Reaction, Western Blot, Staining, ALP Assay

    C10orf99 regulates the keratinocyte proliferation by activating ERK1/2 and NF-κB pathways. ( a ) HaCaT cells were treated with M5 for 15, 30 and 60 min, and the phosphorylation of NF-κB p65, ERK1/2 and AKT were detected by western blot. ( b ) HaCaT cells were transfected with C10orf99 siRNAs for 48 h and then incubated with M5 for 30 min. Cells were lysed for western blot analysis on indicated proteins. ( c ) Phosphorylation of NF-κB p65, ERK1/2 and AKT were analysed by western blot in HaCaT cells transduced with lentiviral particles. β-actin was used as an internal control. Date are representative of three independent experiments. Ctrl, control; BLK, blank transfected group; LV-Ctrl, vector transfected group; LV-C10orf99, C10orf99-expressing lentiviruses transfected group.

    Journal: Scientific Reports

    Article Title: C10orf99 contributes to the development of psoriasis by promoting the proliferation of keratinocytes

    doi: 10.1038/s41598-018-26996-z

    Figure Lengend Snippet: C10orf99 regulates the keratinocyte proliferation by activating ERK1/2 and NF-κB pathways. ( a ) HaCaT cells were treated with M5 for 15, 30 and 60 min, and the phosphorylation of NF-κB p65, ERK1/2 and AKT were detected by western blot. ( b ) HaCaT cells were transfected with C10orf99 siRNAs for 48 h and then incubated with M5 for 30 min. Cells were lysed for western blot analysis on indicated proteins. ( c ) Phosphorylation of NF-κB p65, ERK1/2 and AKT were analysed by western blot in HaCaT cells transduced with lentiviral particles. β-actin was used as an internal control. Date are representative of three independent experiments. Ctrl, control; BLK, blank transfected group; LV-Ctrl, vector transfected group; LV-C10orf99, C10orf99-expressing lentiviruses transfected group.

    Article Snippet: The C10orf99-overexpressing lentivirus particles were purchased from GenePharma (Shanghai, China).

    Techniques: Western Blot, Transfection, Incubation, Transduction, Plasmid Preparation, Expressing

    Effect of C10orf99 overexpression on cell proliferation. ( a ) C10orf99 mRNA and ( b ) protein expressions were determined after lentiviral particles transduction in HaCaT cells. ( c ) MTT assays on HaCaT cells transduced with control or C10orf99-expressing lentiviruses. ( d ) Cell cycle distribution was analyzed by flow cytometry, and the percentages of cells in different cycle phases were calculated. ( e ) Protein expression levels of cell cycle regulators were analyzed. Date are representative of at least three independent experiments. ** P

    Journal: Scientific Reports

    Article Title: C10orf99 contributes to the development of psoriasis by promoting the proliferation of keratinocytes

    doi: 10.1038/s41598-018-26996-z

    Figure Lengend Snippet: Effect of C10orf99 overexpression on cell proliferation. ( a ) C10orf99 mRNA and ( b ) protein expressions were determined after lentiviral particles transduction in HaCaT cells. ( c ) MTT assays on HaCaT cells transduced with control or C10orf99-expressing lentiviruses. ( d ) Cell cycle distribution was analyzed by flow cytometry, and the percentages of cells in different cycle phases were calculated. ( e ) Protein expression levels of cell cycle regulators were analyzed. Date are representative of at least three independent experiments. ** P

    Article Snippet: The C10orf99-overexpressing lentivirus particles were purchased from GenePharma (Shanghai, China).

    Techniques: Over Expression, Transduction, MTT Assay, Expressing, Flow Cytometry, Cytometry

    C10orf99 knockdown reduced the epidermal thickness of IMQ-induced psoriasis mouse model. ( a ) qRT-PCR analysis of mC10orf99 expression in the back skins of mice infected with the lentiviruses and treated with IMQ (7 days). ( b ) Phenotypic presentation of the back skins of mice after lentivirus infection and IMQ treatment for 7 days. ( c ) Reprsentative histological sections of the back skins of control (Ctrl) (n = 6) or IMQ-induced psoriatic mice injected intradermally with C10orf99 shRNA (sh-C10orf99) (n = 6) or negative control shRNA (sh-Ctrl) (n = 6) examined by hematoxylin and eosin staining. Bar = 600 μm. ( d ) Epidermal thickness of the mouse back skins was measured. Each point represents one mouse skin sample. ( e ) Western blot analysis of Cyclin A, Cyclin D1, NF-κB p65, phosphorylation of NF-κB p65, AKT, ERK1/2 in skin tissues from control and IMQ-induced psoriatic mice. ( f ) Western blot analysis of Cyclin A, Cyclin D1, VEGF and phosphorylation of NF-κB p65, AKT, ERK1/2 in skin tissues from IMQ-induced psoriatic mice injected intradermally with lentiviruses. β-actin was used as an internal control. Date are representative of three independent experiments. ** P

    Journal: Scientific Reports

    Article Title: C10orf99 contributes to the development of psoriasis by promoting the proliferation of keratinocytes

    doi: 10.1038/s41598-018-26996-z

    Figure Lengend Snippet: C10orf99 knockdown reduced the epidermal thickness of IMQ-induced psoriasis mouse model. ( a ) qRT-PCR analysis of mC10orf99 expression in the back skins of mice infected with the lentiviruses and treated with IMQ (7 days). ( b ) Phenotypic presentation of the back skins of mice after lentivirus infection and IMQ treatment for 7 days. ( c ) Reprsentative histological sections of the back skins of control (Ctrl) (n = 6) or IMQ-induced psoriatic mice injected intradermally with C10orf99 shRNA (sh-C10orf99) (n = 6) or negative control shRNA (sh-Ctrl) (n = 6) examined by hematoxylin and eosin staining. Bar = 600 μm. ( d ) Epidermal thickness of the mouse back skins was measured. Each point represents one mouse skin sample. ( e ) Western blot analysis of Cyclin A, Cyclin D1, NF-κB p65, phosphorylation of NF-κB p65, AKT, ERK1/2 in skin tissues from control and IMQ-induced psoriatic mice. ( f ) Western blot analysis of Cyclin A, Cyclin D1, VEGF and phosphorylation of NF-κB p65, AKT, ERK1/2 in skin tissues from IMQ-induced psoriatic mice injected intradermally with lentiviruses. β-actin was used as an internal control. Date are representative of three independent experiments. ** P

    Article Snippet: The C10orf99-overexpressing lentivirus particles were purchased from GenePharma (Shanghai, China).

    Techniques: Quantitative RT-PCR, Expressing, Mouse Assay, Infection, Injection, shRNA, Negative Control, Staining, Western Blot

    Inhibition of Cx43 expression increases cellular resistance to VacA toxicity. (A) AZ-521 cells were transduced with lentivirus particles encoding nontargeting (NT) shRNA or two different Cx43-specific shRNAs (83010 and 83012), and cells stably expressing the shRNAs were selected. Expression of the Cx43 protein was analyzed by Western blotting using an anti-Cx43 antibody. Expression of β-actin was monitored to ensure equal loading. The effect of shRNA treatment on Cx43 production was evaluated by densitometry. Cx43 expression was decreased in Cx43 shRNA-expressing cells compared to that in cells expressing NT shRNA. (B to E) Control AZ-521 cells (NT) and cells expressing Cx43-specific shRNA (83010 or 83012) were incubated with serial dilutions of H. pylori broth culture supernatants containing WT VacA (B and D) or the inactive mutant protein VacA-G14A (C and E). After 24 h, cell viability was determined by the ATPlite assay. The Cx43-specific shRNA conferred a protective effect in the experiments shown in panels B and D but not in the experiments shown in panels C and E. A low level of cell death in response to high concentrations of supernatants containing VacA-G14A is attributed to nonspecific effects. Error bars represent means plus standard errors from combined results of two independent experiments, each performed in triplicate. Asterisks indicate P

    Journal: Infection and Immunity

    Article Title: Role of Connexin 43 in Helicobacter pylori VacA-Induced Cell Death

    doi: 10.1128/IAI.00827-13

    Figure Lengend Snippet: Inhibition of Cx43 expression increases cellular resistance to VacA toxicity. (A) AZ-521 cells were transduced with lentivirus particles encoding nontargeting (NT) shRNA or two different Cx43-specific shRNAs (83010 and 83012), and cells stably expressing the shRNAs were selected. Expression of the Cx43 protein was analyzed by Western blotting using an anti-Cx43 antibody. Expression of β-actin was monitored to ensure equal loading. The effect of shRNA treatment on Cx43 production was evaluated by densitometry. Cx43 expression was decreased in Cx43 shRNA-expressing cells compared to that in cells expressing NT shRNA. (B to E) Control AZ-521 cells (NT) and cells expressing Cx43-specific shRNA (83010 or 83012) were incubated with serial dilutions of H. pylori broth culture supernatants containing WT VacA (B and D) or the inactive mutant protein VacA-G14A (C and E). After 24 h, cell viability was determined by the ATPlite assay. The Cx43-specific shRNA conferred a protective effect in the experiments shown in panels B and D but not in the experiments shown in panels C and E. A low level of cell death in response to high concentrations of supernatants containing VacA-G14A is attributed to nonspecific effects. Error bars represent means plus standard errors from combined results of two independent experiments, each performed in triplicate. Asterisks indicate P

    Article Snippet: HeLa cells were transduced with lentivirus particles encoding human Cx43 or with negative-control Lentifect lentivirus particles (GeneCopoeia) at an MOI of 5.

    Techniques: Inhibition, Expressing, Transduction, shRNA, Stable Transfection, Western Blot, Incubation, Mutagenesis

    Expression of Cx43 in HeLa cells increases susceptibility to VacA. HeLa cells were transduced with lentivirus particles expressing Cx43 or a control lentivirus, and transduced cells were then selected (designated HeLa-Cx43 or HeLa-control, respectively). (A) Expression of Cx43 in AZ-521, HeLa-Cx43, and HeLa-control cells was analyzed by Western blotting using an anti-Cx43 antibody. Expression of β-actin was monitored to ensure equal loading. Levels of Cx43 were analyzed by densitometry. (B and C) HeLa-Cx43 and HeLa-control cells were incubated with serial dilutions of H. pylori broth culture supernatants containing WT VacA (B) or VacA-G14A (C) for 24 h, and cell viability was determined by the ATPlite assay. HeLa cells expressing Cx43 exhibited increased susceptibility to VacA-induced cell death compared to HeLa cells transduced with the control lentivirus. Error bars represent means plus standard errors from combined results of three independent experiments, each performed in triplicate. Asterisks indicate P

    Journal: Infection and Immunity

    Article Title: Role of Connexin 43 in Helicobacter pylori VacA-Induced Cell Death

    doi: 10.1128/IAI.00827-13

    Figure Lengend Snippet: Expression of Cx43 in HeLa cells increases susceptibility to VacA. HeLa cells were transduced with lentivirus particles expressing Cx43 or a control lentivirus, and transduced cells were then selected (designated HeLa-Cx43 or HeLa-control, respectively). (A) Expression of Cx43 in AZ-521, HeLa-Cx43, and HeLa-control cells was analyzed by Western blotting using an anti-Cx43 antibody. Expression of β-actin was monitored to ensure equal loading. Levels of Cx43 were analyzed by densitometry. (B and C) HeLa-Cx43 and HeLa-control cells were incubated with serial dilutions of H. pylori broth culture supernatants containing WT VacA (B) or VacA-G14A (C) for 24 h, and cell viability was determined by the ATPlite assay. HeLa cells expressing Cx43 exhibited increased susceptibility to VacA-induced cell death compared to HeLa cells transduced with the control lentivirus. Error bars represent means plus standard errors from combined results of three independent experiments, each performed in triplicate. Asterisks indicate P

    Article Snippet: HeLa cells were transduced with lentivirus particles encoding human Cx43 or with negative-control Lentifect lentivirus particles (GeneCopoeia) at an MOI of 5.

    Techniques: Expressing, Transduction, Western Blot, Incubation

    Expression and localization of Cx43 in AZ-521 and HeLa cells. HeLa cells were transduced with lentiviral particles expressing Cx43 or a control lentivirus, and transduced cells were then selected (designated HeLa-Cx43 or HeLa-control, respectively). AZ-521, HeLa-control, and HeLa-Cx43 cells were examined for expression and localization of Cx43. AZ-521, HeLa-control, and HeLa-Cx43 cells were fixed, permeabilized, and stained to detect Cx43, as described in Materials and Methods. The nucleus is shown in blue, and Cx43 is shown in red. Bars, 10 μm. Cx43 was detected in AZ-521 cells (A) and HeLa-Cx43 cells (C) but not in HeLa-control cells (B).

    Journal: Infection and Immunity

    Article Title: Role of Connexin 43 in Helicobacter pylori VacA-Induced Cell Death

    doi: 10.1128/IAI.00827-13

    Figure Lengend Snippet: Expression and localization of Cx43 in AZ-521 and HeLa cells. HeLa cells were transduced with lentiviral particles expressing Cx43 or a control lentivirus, and transduced cells were then selected (designated HeLa-Cx43 or HeLa-control, respectively). AZ-521, HeLa-control, and HeLa-Cx43 cells were examined for expression and localization of Cx43. AZ-521, HeLa-control, and HeLa-Cx43 cells were fixed, permeabilized, and stained to detect Cx43, as described in Materials and Methods. The nucleus is shown in blue, and Cx43 is shown in red. Bars, 10 μm. Cx43 was detected in AZ-521 cells (A) and HeLa-Cx43 cells (C) but not in HeLa-control cells (B).

    Article Snippet: HeLa cells were transduced with lentivirus particles encoding human Cx43 or with negative-control Lentifect lentivirus particles (GeneCopoeia) at an MOI of 5.

    Techniques: Expressing, Transduction, Staining

    C-terminal fragment of iOPN binds to TRAF3. ( A ) Schematic structure of iOPN-WT and its mutant iOPN-N and iOPN-C containing the N-terminal and C-terminal fragment of iOPN divided in the thrombin cleaved site. ( B ) TRAF3, Flag-iOPN-WT, Flag-iOPN-N, Flag-iOPN-C protein were obtained by in vitro transcription and translation. Interaction between TRAF3 and iOPN truncations was assayed by mixing TRAF3 and iOPN truncations together followed by IP with Flag antibody and western blot with TRAF3 antibody. ( C ) TRAF3, Triad3A, Flag-iOPN-WT, Flag-iOPN-N, Flag-iOPN-C protein were obtained by in vitro transcription and translation. In vitro ubiquitination assays were performed in the presence of Ub, E1, UbcH5c, TRAF3, Triad3A and iOPN-WT, iOPN-N or iOPN-C. The ubiquitination of TRAF3 was examined by western blot with TRAF3 antibody. ( D ) Peritoneal macrophages from WT and OPN-deficient ( Spp1 −/− ) mice which were infected with lentivirus (MOI, 50) containing iOPN-WT expression plasmid or control plasmid, 4 days later, OPN protein level were assayed by using WB. ( E ) Peritoneal macrophages from WT and OPN-deficient ( Spp1 −/− ) mice were infected with lentivirus (MOI, 50) containing control vector, iOPN-WT, iOPN-N or iOPN-C for 4 days, then infected with SeV for 8 h or left uninfected, qRT-PCR analysis of IFN-β was performed. The data are representative of three biological replicates (mean ± S.D. in E ).

    Journal: Scientific Reports

    Article Title: Intracellular osteopontin stabilizes TRAF3 to positively regulate innate antiviral response

    doi: 10.1038/srep23771

    Figure Lengend Snippet: C-terminal fragment of iOPN binds to TRAF3. ( A ) Schematic structure of iOPN-WT and its mutant iOPN-N and iOPN-C containing the N-terminal and C-terminal fragment of iOPN divided in the thrombin cleaved site. ( B ) TRAF3, Flag-iOPN-WT, Flag-iOPN-N, Flag-iOPN-C protein were obtained by in vitro transcription and translation. Interaction between TRAF3 and iOPN truncations was assayed by mixing TRAF3 and iOPN truncations together followed by IP with Flag antibody and western blot with TRAF3 antibody. ( C ) TRAF3, Triad3A, Flag-iOPN-WT, Flag-iOPN-N, Flag-iOPN-C protein were obtained by in vitro transcription and translation. In vitro ubiquitination assays were performed in the presence of Ub, E1, UbcH5c, TRAF3, Triad3A and iOPN-WT, iOPN-N or iOPN-C. The ubiquitination of TRAF3 was examined by western blot with TRAF3 antibody. ( D ) Peritoneal macrophages from WT and OPN-deficient ( Spp1 −/− ) mice which were infected with lentivirus (MOI, 50) containing iOPN-WT expression plasmid or control plasmid, 4 days later, OPN protein level were assayed by using WB. ( E ) Peritoneal macrophages from WT and OPN-deficient ( Spp1 −/− ) mice were infected with lentivirus (MOI, 50) containing control vector, iOPN-WT, iOPN-N or iOPN-C for 4 days, then infected with SeV for 8 h or left uninfected, qRT-PCR analysis of IFN-β was performed. The data are representative of three biological replicates (mean ± S.D. in E ).

    Article Snippet: Lentivirus particles were produced through transfection of pWPXL-OPN, psPAX2 and pMD2.G plasmids (addgene) with a proportion of 20:15:7 into HEK293T cells, 3 days later the culture was harvested and enriched by PEG8000.

    Techniques: Mutagenesis, In Vitro, Western Blot, Mouse Assay, Infection, Expressing, Plasmid Preparation, Quantitative RT-PCR

    APLNR regulates CXCR4 expression through miR-139-5p. ( a , b ) CXCR4 expression in response to shear stress exposure in HUVECs, with or without concurrent APLNR knockdown. mRNA ( a ) and protein levels ( b ) are shown. ( c ) CXCR4 expression in response to AGO2 knockdown. ( d ) CXCR4 expression in response to shear stress exposure in HUVECs, with or without concurrent AGO2 knockdown. ( e ) Determination of miR-139-5p levels in FACS sorted ECs from P5 retinas of Aplnr −/− , Apln −/− mice and respective littermates. n= 3 retinas per genotype. ( f ) CXCR4 expression in HUVECs overexpressing miR-139-5p mimic or non-targeting control anti-miR. ( g ) Expression levels of miR-139-5p in response to shear stress, with or without concurrent APLNR knockdown. ( h ) CXCR4 expression in HUVECs in response to shear stress exposure, with or without concurrent miR-139-5p inhibition via anti-miR. ( i ) Sprouting assay using HUVEC covered beads transduced with miR-139-5p or control lentivirus in response to SDF-1α or VEGF 165. Scale bar, 175 μm. ( j ) Migration assay of HUVECs transduced with miR-139-5p or control lentivirus in response to SDF-1α. Scale bar, 200 μm. * P

    Journal: Nature Communications

    Article Title: MicroRNA 139-5p coordinates APLNR-CXCR4 crosstalk during vascular maturation

    doi: 10.1038/ncomms11268

    Figure Lengend Snippet: APLNR regulates CXCR4 expression through miR-139-5p. ( a , b ) CXCR4 expression in response to shear stress exposure in HUVECs, with or without concurrent APLNR knockdown. mRNA ( a ) and protein levels ( b ) are shown. ( c ) CXCR4 expression in response to AGO2 knockdown. ( d ) CXCR4 expression in response to shear stress exposure in HUVECs, with or without concurrent AGO2 knockdown. ( e ) Determination of miR-139-5p levels in FACS sorted ECs from P5 retinas of Aplnr −/− , Apln −/− mice and respective littermates. n= 3 retinas per genotype. ( f ) CXCR4 expression in HUVECs overexpressing miR-139-5p mimic or non-targeting control anti-miR. ( g ) Expression levels of miR-139-5p in response to shear stress, with or without concurrent APLNR knockdown. ( h ) CXCR4 expression in HUVECs in response to shear stress exposure, with or without concurrent miR-139-5p inhibition via anti-miR. ( i ) Sprouting assay using HUVEC covered beads transduced with miR-139-5p or control lentivirus in response to SDF-1α or VEGF 165. Scale bar, 175 μm. ( j ) Migration assay of HUVECs transduced with miR-139-5p or control lentivirus in response to SDF-1α. Scale bar, 200 μm. * P

    Article Snippet: Control and miR-139 lentivirus constructs (System Biosciences) were used to generate lentivirus particles with the Lenti-X HTX Packaging System (Clontech) with Lenti-X Concentrator.

    Techniques: Expressing, FACS, Mouse Assay, Inhibition, Transduction, Migration