18s rna (Thermo Fisher)
Thermo Fisher is a verified supplier 
99
|
Name:
QuantumRNA Universal 18S Internal Standard
Description:
The Ambion QuantumRNA 18S Internal Standard with Competimer technology uses specially modified Competimer s of the same sequence as the normal 18S primers that cannot be extended By adjusting the ratio of 18S Competimer s to normal 18S mRNA primers the signal for 18S mRNA can be attenuated to the level of very rare messages They are used for quantitative end point RT PCR and include sufficient reagents for 100 reactions Because of its invariant expression across tissues and treatments 18S ribosomal RNA is an ideal internal control for quantitative RNA analysis The Universal 18S Internal Standards function across the broadest range of eukaryotes including animals plants and many protozoa and produce a 315 bp PCR product Accessory Products The QuantumRNA Classic 18S Internal Standard SKU AM1716 produce a different 489 bp PCR product and the QuantumRNA Classic II 18S Internal Standard SKU AM1717 produce a 324 bp PCR product
Catalog Number:
am1718
Price:
None
Applications:
General RT-PCR Reagents & Accessories|PCR & Real-Time PCR
Category:
Standards Ladders Controls
|
Buy from Supplier |
Structured Review
Thermo Fisher
18s rna
The Ambion QuantumRNA 18S Internal Standard with Competimer technology uses specially modified Competimer s of the same sequence as the normal 18S primers that cannot be extended By adjusting the ratio of 18S Competimer s to normal 18S mRNA primers the signal for 18S mRNA can be attenuated to the level of very rare messages They are used for quantitative end point RT PCR and include sufficient reagents for 100 reactions Because of its invariant expression across tissues and treatments 18S ribosomal RNA is an ideal internal control for quantitative RNA analysis The Universal 18S Internal Standards function across the broadest range of eukaryotes including animals plants and many protozoa and produce a 315 bp PCR product Accessory Products The QuantumRNA Classic 18S Internal Standard SKU AM1716 produce a different 489 bp PCR product and the QuantumRNA Classic II 18S Internal Standard SKU AM1717 produce a 324 bp PCR product
https://www.bioz.com/result/18s rna/product/Thermo Fisher
Average 99 stars, based on 69 article reviews
Price from $9.99 to $1999.99
The Ambion QuantumRNA 18S Internal Standard with Competimer technology uses specially modified Competimer s of the same sequence as the normal 18S primers that cannot be extended By adjusting the ratio of 18S Competimer s to normal 18S mRNA primers the signal for 18S mRNA can be attenuated to the level of very rare messages They are used for quantitative end point RT PCR and include sufficient reagents for 100 reactions Because of its invariant expression across tissues and treatments 18S ribosomal RNA is an ideal internal control for quantitative RNA analysis The Universal 18S Internal Standards function across the broadest range of eukaryotes including animals plants and many protozoa and produce a 315 bp PCR product Accessory Products The QuantumRNA Classic 18S Internal Standard SKU AM1716 produce a different 489 bp PCR product and the QuantumRNA Classic II 18S Internal Standard SKU AM1717 produce a 324 bp PCR product
https://www.bioz.com/result/18s rna/product/Thermo Fisher
Average 99 stars, based on 69 article reviews
Price from $9.99 to $1999.99
18s rna - by Bioz Stars,
2021-01
99/100 stars
Related Products / Commonly Used Together
Images
1) Product Images from "Induction of apoptosis by in vitro and in vivo plant extracts derived from Menyanthes trifoliata L. in human cancer cells"
Article Title: Induction of apoptosis by in vitro and in vivo plant extracts derived from Menyanthes trifoliata L. in human cancer cells
Journal: Cytotechnology
doi: 10.1007/s10616-018-0274-9
Figure Legend Snippet: a Expression of genes Bax, Bcl - 2, Cas - 3 and TP53 in human grade IV glioma cells after treatment with 1.5 mg mL −1 Mt RV in vitro plant extract of Menyathes trifoliata . The transcript level of each gene was normalized to the expression of a reference gene ( 18S RNA ). Data is presented as fold change in human grade IV glioma cells after treatment of Menyanthes trifoliata extract versus untreated human grade IV glioma cells, in which expression levels of the genes were set as 1. b Mitochondrial membrane potential in human grade IV glioma cells after treatment with 1.5 mg mL −1 Mt RV in vitro plant extract of Menyathes trifoliata . MMP is expressed as 530 nm/590 nm to 485 nm/538 nm (aggregates to monomer) fluorescence ratio, as quantified with a fluorescent plate reader after JC-1 staining). The mean values ± SD were calculated from three independent experiments. p
Techniques Used: Expressing, In Vitro, Fluorescence, Staining
2) Product Images from "Estrogen receptors activate atrial natriuretic peptide in the rat heart"
Article Title: Estrogen receptors activate atrial natriuretic peptide in the rat heart
Journal: Proceedings of the National Academy of Sciences of the United States of America
doi: 10.1073/pnas.201394198
Figure Legend Snippet: RT-PCR analysis of ERα and β transcripts in the heart chambers of newborn (4-day-old) and adult (55-day-old) female rats. Total RNA (1 μg) was reverse-transcribed, and cDNA was exponentially amplified in the presence of gene-specific primers. ( A ) A PhosphorImager scan after separation of the radioactive PCR product by electrophoresis in 1.5% agarose. Representative bands obtained from three RNA samples of the right atrium (RA) and left ventricle (LV) are shown. ( B ) Bar graphs depict ERα mRNA ( Left ) and ERβ mRNA ( Right ) levels verified by 18S RNA product used as internal standard. The results were calculated as a ratio of the signal given by radioactive bands of ERα mRNA or ERβ mRNA to the corresponding 18S band. RNA samples from the whole heart of newborn (1-day-old) rats were included in each experiment and used as a standard (100%) for calibration of ERα mRNA or ERβ mRNA levels. Values are means ± SEM for the right atrium and left ventricle, as well as for the left atrium (LA) and right ventricle (RV). n = 6; §, P
Techniques Used: Reverse Transcription Polymerase Chain Reaction, Amplification, Polymerase Chain Reaction, Electrophoresis
Figure Legend Snippet: ( A ) were subjected to SDS/PAGE, immunoblotted with an anti-ERα mAb, and visualized by the chemiluminescence technique. ( B and C ) RT-PCR analysis of ER transcripts and ANP in the left atrium ( B ) and right atrium ( C ) of sham-operated (sham), ovariectomized (ovx), and ovariectomized rats supplemented with 17-β-estradiol (ovxE). Total RNA (1 μg) was reverse-transcribed and cDNA was exponentially amplified in the presence of gene-specific primers. A PhosphorImager scan is presented after separation of the radioactive PCR product by electrophoresis in 1.5% agarose. Representative bands obtained in three RNA representative samples from sham, ovx, and ovxE rats are presented. The results were calculated as the ratio of the signal given by radioactive bands of ERα mRNA or ERβ mRNA to the corresponding 18S band. Values are means ± SEM adjusted to the values (in percentage) of sham-operated rats (100%). n = 6; *, P
Techniques Used: SDS Page, Reverse Transcription Polymerase Chain Reaction, Aqueous Normal-phase Chromatography, Amplification, Polymerase Chain Reaction, Electrophoresis
3) Product Images from "Social stress in mice induces voiding dysfunction and bladder wall remodeling"
Article Title: Social stress in mice induces voiding dysfunction and bladder wall remodeling
Journal:
doi: 10.1152/ajprenal.90749.2008
Figure Legend Snippet: Social stress leads to increased expression of the myosin heavy chain B and A mRNA isoforms. A representative gel with normalization to 18S RNA is shown. These values represent the average ± SD from 6 control (only 4 are shown) and 6 stressed
Techniques Used: Expressing
4) Product Images from "Neuronal megalin mediates synaptic plasticity—a novel mechanism underlying intellectual disabilities in megalin gene pathologies"
Article Title: Neuronal megalin mediates synaptic plasticity—a novel mechanism underlying intellectual disabilities in megalin gene pathologies
Journal: Brain Communications
doi: 10.1093/braincomms/fcaa135
![TTR rescues megalin downregulation in TTR KO hippocampal neuronal cultures, in a megalin-dependent way. ( A ) Total RNA was extracted from WT ( n = 11) and TTR KO ( n = 10) hippocampal neuronal cultures (7 DIV), and megalin and 18S mRNA levels were semi-quantified through real-time PCR, showing a reduction in megalin mRNA levels in hippocampal neurons of TTR KO mice. ( B ) Megalin and tubulin protein levels were determined by western blot in TTR KO ( n = 6) and WT ( n = 8) hippocampal neuronal cultures, with a decrease in megalin protein levels observed in TTR KO neurons. TTR KO cultured hippocampal neurons were stimulated with recombinant mouse TTR [55 µg/ml (1 µM)] for 4 h (mRNA) ( C ) or 14 h (protein) ( D ). When indicated, neurons were treated with TTR, in presence or absence of anti-TTR Nanobodies 169F7 and 165C6 (2 µM), or treated only with the nanobodies ( C ). TTR treatment rescued megalin mRNA ( C , n = 5–7 independent cultures) and protein levels ( D , n = 3 independent cultures) in TTR KO neurons, and the effect was abolished in the presence of the 169F7 nanobody, specific for TTR-megalin interaction epitope ( C ). Megalin (+/−) TTR KO and TTR KO cultured hippocampal neurons (7 DIV) were stimulated with recombinant mutated forms of mouse TTR, I84S (a TTR with low affinity for its ligands) and K15N (55 µg/ml, for 4 h; a TTR mutated in the 169F7 nanobody epitope, affecting TTR-megalin interaction), and megalin and 18S mRNA levels were assessed ( E , n = 6–10 neuronal cultures). TTR-induced effect in increasing megalin levels is independent of TTR ligands but depends on TTR binding to megalin and on megalin levels. (F) WT hippocampal neuronal cultures were stimulated with recombinant mouse TTR (55 µg/ml, for 4 h) in the presence or absence of the inhibitor clathrin-mediated endocytosis Dynasore (80 μM) and megalin mRNA levels were assessed ( n = 5 neuronal cultures). No effect was observed in the presence of the inhibitor, indicating that TTR-induced increase in megalin levels does not involve receptor internalization. ( G ) LRP1 and 18S mRNA levels were determined in TTR KO hippocampal neurons ( n = 4 neuronal cultures), in the presence or absence of recombinant mouse TTR (55 µg/ml, for 4 h). LRP1 levels are not affected by TTR stimulation, indicating a specific effect for LRP2 (megalin). Statistical analysis was performed using Student’s unpaired t -test or one-way ANOVA followed by Bonferroni’s multiple comparison test. * P](https://storage.googleapis.com/bioz_article_images/PMC7667529/fcaa135f2.jpg "... hippocampal neuronal cultures (7 DIV), and megalin and 18S mRNA levels were semi-quantified through real-time PCR, showing ...")
Figure Legend Snippet: TTR rescues megalin downregulation in TTR KO hippocampal neuronal cultures, in a megalin-dependent way. ( A ) Total RNA was extracted from WT ( n = 11) and TTR KO ( n = 10) hippocampal neuronal cultures (7 DIV), and megalin and 18S mRNA levels were semi-quantified through real-time PCR, showing a reduction in megalin mRNA levels in hippocampal neurons of TTR KO mice. ( B ) Megalin and tubulin protein levels were determined by western blot in TTR KO ( n = 6) and WT ( n = 8) hippocampal neuronal cultures, with a decrease in megalin protein levels observed in TTR KO neurons. TTR KO cultured hippocampal neurons were stimulated with recombinant mouse TTR [55 µg/ml (1 µM)] for 4 h (mRNA) ( C ) or 14 h (protein) ( D ). When indicated, neurons were treated with TTR, in presence or absence of anti-TTR Nanobodies 169F7 and 165C6 (2 µM), or treated only with the nanobodies ( C ). TTR treatment rescued megalin mRNA ( C , n = 5–7 independent cultures) and protein levels ( D , n = 3 independent cultures) in TTR KO neurons, and the effect was abolished in the presence of the 169F7 nanobody, specific for TTR-megalin interaction epitope ( C ). Megalin (+/−) TTR KO and TTR KO cultured hippocampal neurons (7 DIV) were stimulated with recombinant mutated forms of mouse TTR, I84S (a TTR with low affinity for its ligands) and K15N (55 µg/ml, for 4 h; a TTR mutated in the 169F7 nanobody epitope, affecting TTR-megalin interaction), and megalin and 18S mRNA levels were assessed ( E , n = 6–10 neuronal cultures). TTR-induced effect in increasing megalin levels is independent of TTR ligands but depends on TTR binding to megalin and on megalin levels. (F) WT hippocampal neuronal cultures were stimulated with recombinant mouse TTR (55 µg/ml, for 4 h) in the presence or absence of the inhibitor clathrin-mediated endocytosis Dynasore (80 μM) and megalin mRNA levels were assessed ( n = 5 neuronal cultures). No effect was observed in the presence of the inhibitor, indicating that TTR-induced increase in megalin levels does not involve receptor internalization. ( G ) LRP1 and 18S mRNA levels were determined in TTR KO hippocampal neurons ( n = 4 neuronal cultures), in the presence or absence of recombinant mouse TTR (55 µg/ml, for 4 h). LRP1 levels are not affected by TTR stimulation, indicating a specific effect for LRP2 (megalin). Statistical analysis was performed using Student’s unpaired t -test or one-way ANOVA followed by Bonferroni’s multiple comparison test. * P
Techniques Used: Real-time Polymerase Chain Reaction, Mouse Assay, Western Blot, Cell Culture, Recombinant, Binding Assay
5) Product Images from "RNA-Seq and differential gene expression analysis in Temora stylifera copepod females with contrasting non-feeding nauplii survival rates: an environmental transcriptomics study"
Article Title: RNA-Seq and differential gene expression analysis in Temora stylifera copepod females with contrasting non-feeding nauplii survival rates: an environmental transcriptomics study
Journal: BMC Genomics
doi: 10.1186/s12864-020-07112-w
Figure Legend Snippet: Comparison between RNA-Seq and RT-qPCR in Temora stylifera . Relative expression ratio (log 2 -Fold-Change, FC) of 9 unigenes ( A5 , Obst , Arih1 , Ppa2 , Arsb , Hsp-70 , Vldlr , Me31b and Crebl2 ) and 3 isoforms ( Mob1b , Vasa and Pafah ) in Temora stylifera from May 23rd vs 30th samples, measured through RNA-Seq (blue bars) or RT-qPCR (yellow bars). For RT-qPCR results, bars represented mean ± SD values and data are normalized to RNA 18S and Ubi reference genes
Techniques Used: RNA Sequencing Assay, Quantitative RT-PCR, Expressing
6) Product Images from "Herpes Simplex Virus 1 MicroRNA miR-H28 Exported to Uninfected Cells in Exosomes Restricts Cell-to-Cell Virus Spread by Inducing Gamma Interferon mRNA"
Article Title: Herpes Simplex Virus 1 MicroRNA miR-H28 Exported to Uninfected Cells in Exosomes Restricts Cell-to-Cell Virus Spread by Inducing Gamma Interferon mRNA
Journal: Journal of Virology
doi: 10.1128/JVI.01005-19
Figure Legend Snippet: Analyses of accumulation of IFN-γ mRNA in HEp-2 and HEK293T cells after HSV-1(F) infection. Replicate cultures of HEp-2 cells (A) and HEK293T cells (B) were mock treated or exposed to 20 PFU of HSV-1(F) per cell. The cells were harvested at the indicated times after infection, and total RNAs from cell lysates were extracted and reverse transcribed to cDNA as described in Materials and Methods. Levels of mRNA encoding IFN-γ were normalized to those of 18S RNA, and results are shown as fold changes, compared with the mRNA levels measured in uninfected HEp-2 or HEK293T cells.
Techniques Used: Infection
Figure Legend Snippet: Accumulation of mRNAs for IFN-α, IFN-β, and IFN-γ with HEp-2 transfection of miR-H28 mimics. Replicate cultures of HEp-2 cells were mock treated or transfected with 100 nM NC, miR-H5-3p, miR-H6-3p, miR-H1-5p, miR-H26, miR-H27, miR-H28, or miR-H29 mimic. The cells were harvested at the indicated times after transfection, and total RNAs from cell lysates were extracted and reverse transcribed to cDNA as described in Materials and Methods. Levels of mRNAs for IFN-α (A), IFN-β (B), and IFN-γ (C) were normalized to those of 18S RNA, and results are shown as fold changes, compared with the mRNA levels measured in HEp-2 cells. NC, miRNA mimic negative control.
Techniques Used: Transfection, Negative Control
Figure Legend Snippet: Temporal patterns of accumulation of mRNAs for 20 genes associated with various aspects of innate immunity. Replicate cultures of HEp-2 cells were mock treated (M) or exposed to 5 PFU of HSV-1(F) per cell. The cells were harvested at the indicated times after infection, and total RNAs were extracted and reverse transcribed to cDNA as described in Materials and Methods. Levels of mRNAs for ATF3, cGAS, CXCL10, HDAC1, HDAC4, IFI16, IFIT1, IFN-α, IFN-β, IFN- γ , IL-6, IRF3, LGP2, LSD1, MDA5, MYD88, PUM1, RIG-I, and STING were normalized to those of 18S RNA, and results are shown as fold changes, compared with the mRNA levels measured in uninfected HEp-2 cells.
Techniques Used: Infection
7) Product Images from "Adipocyte-Specific Glucocorticoid Inactivation Protects Against Diet-Induced Obesity"
Article Title: Adipocyte-Specific Glucocorticoid Inactivation Protects Against Diet-Induced Obesity
Journal:
doi:
Figure Legend Snippet: 11βHSD2 and 11βHSD1 expression and activity. A : h11βHSD2 expression relative to 18S RNA in various adipose tissue depots of 24-week-old transgenic and WT mice ( n = 10 per group) using quantitative real-time PCR with human kidney
Techniques Used: Expressing, Activity Assay, Transgenic Assay, Mouse Assay, Real-time Polymerase Chain Reaction
8) Product Images from "The peroxisome proliferator activated receptor ? is required for the differentiation of THP-1 monocytic cells by phorbol ester"
Article Title: The peroxisome proliferator activated receptor ? is required for the differentiation of THP-1 monocytic cells by phorbol ester
Journal: Nuclear Receptor
doi: 10.1186/1478-1336-1-9
Figure Legend Snippet: PPARδ expression and activity is increased by phorbol ester. A: Time course of induction of PPARδ message in response to phorbol ester. THP-1 cells were plated in RPMI medium supplemented with 10% FCS and 1 nM PMA at a density of 1 × 10 6 per well. At each time point, cells were lyzed and RNA prepared, followed by cDNA synthesis. QPCR analysis was performed using PPARδ-specific primers and probe to determine the amount of message. Results are expressed as total relative to 18S and were performed in triplicate. B: Expression of PPARδ protein by THP-1 cells is up-regulated in response to phorbol ester. THP-1 cells were plated in RPMI medium supplemented with 10% FCS and either 1 nM PMA or vehicle and incubated for 48 h. Cells were then lyzed directly into SDS-PAGE sample buffer for Western blotting. Blots were probed using a rabbit polyclonal anti-serum raised against a GST-PPARδ AB domain fusion protein. C: COS-1 cells were transiently co-transfected with pFABPLuc and pCLDNhPPARδ. Transfection efficiency was controlled for by co-transfection with a plasmid encoding β-galactosidase. Cells thus transfected were treated with increasing concentrations of PMA for 24 h after which luciferase activity was measured. D: PMA-induced δ-activation is mediated through the ligand binding domain. COS-1 cells were transfected with an expression vector encoding a Gal-4/PPARδ ligand-binding domain chimera. Cells were then treated for 24 h with compound F, PMA or vehicle only and luciferase readings obtained.
Techniques Used: Expressing, Activity Assay, Real-time Polymerase Chain Reaction, Incubation, SDS Page, Western Blot, Transfection, Cotransfection, Plasmid Preparation, Luciferase, Activation Assay, Ligand Binding Assay
9) Product Images from "Long Non-Coding RNA Hotairm1 Promotes S100A9 Support of MDSC Expansion during Sepsis"
Article Title: Long Non-Coding RNA Hotairm1 Promotes S100A9 Support of MDSC Expansion during Sepsis
Journal: Journal of clinical & cellular immunology
doi:
Figure Legend Snippet: Knockdown of Hotairm1 in late sepsis MDSCs attenuates their immunosuppressive functions. Gr1 + CD11b + cells were isolated from the bone marrow of late septic mice by positive selection using anti-Gr1 antibody and magnetic beads. The cells were transfected with Hotairm1-specific or scramble siRNAs for 36 hr. (A) Effects of MDSCs on T cell proliferation and activation. CD4 + T cells were isolated from splenocytes of naive mice with anti-CD4 antibody and labeled with the fluorescent dye CFSE. The late sepsis Gr1 + CD11b + cells with Hotairm1 knockdown were then co-cultured (1:1 ratio). T cells were stimulated with anti-CD3 plus anti-CD28 antibodies (1 μg/ml each). After 3 days, the cells were harvested, and T cell proliferation and IFNϒ production were determined as in Figure 2 . (B and C) Effect of exosomes lacking Hotairm1 on T cells. Late sepsis Gr1 + CD11b + cells with Hotairm1 knockdown were cultured for 24 hr in serum-free media. Culture supernatants were harvested, and exosomes were purified using exoEasy Maxi kit. (B) Levels of Hotairm1 in exosomal RNA was determined by RT-qPCR. Values were normalized to 18S RNA. (C) Spleen CD4 + T cells were labeled and cultured with naive Gr1 + CD11b + cells (as described in Figure 2 ) in the presence of Hotairm1-lacking exosomes. T cell proliferation and IFNϒ production were measured as in A. Data are expressed as means ± SD of 5-6 mice/group from three experiments. * p
Techniques Used: Isolation, Mouse Assay, Selection, Magnetic Beads, Transfection, Activation Assay, Labeling, Cell Culture, Purification, Quantitative RT-PCR
Figure Legend Snippet: Hotairm1 expression is increased in late sepsis MDSCs. Gr1 + CD11b + cells were isolated from the bone marrow of sham and septic mice by positive selection using anti-Gr1 antibody and magnetic beads. (A) The cells were cultured for 24 hr in serum-free media. Exosomes were purified from the culture supernatants, and exosomal RNA was extracted with exoRNeasy Starter kit. Levels of Hotairm1 were determined by RT-qPCR using RT lncRNAqPCR Assay Primers (Qiagen). Values were normalized to 18S RNA. (B) Total RNA was isolated from Gr1 + CD11b + cells using TRIzol reagent, and levels of Hotaim1 were determined as in A. Values were normalized to GAPDH RNA. (C) Gr1 + CD11b + cells isolated from naïve mice were cultured for 24 hr without or with exosomes (50 μg/well), purified from late sepsis MDSC culture. The cells were harvested, total RNA was extracted and levels of Hotairm1 were determined as in B. PCR was performed in duplicate. Data are presented relative to sham or media control (1-fold). Data in A and B are expressed as means ± SD of 6-9 mice/group from three experiments. Data in C are expressed as means ± SD of 7 cultures from two experiments. * p
Techniques Used: Expressing, Isolation, Mouse Assay, Selection, Magnetic Beads, Cell Culture, Purification, Quantitative RT-PCR, Polymerase Chain Reaction
Figure Legend Snippet: High levels of Hotairm1 in plasma exosomes and MDSCs from late septic patients. (A) Exosomes were purified from plasma and RNA was extracted using exoRNeasy Starter kit. (B) Peripheral blood CD33 + CD11b+HLA-DR − cells were isolated by magnetic cell separation. PBMCs were first purified and depleted of the HLA-DR + cells. The HLA-DR − cell population was then subjected to positive selection with biotin-coupled anti-CD33 antibody, followed by anti-CD11b antibody. Total RNA was extracted using TRIzol reagent. Levels of Hotairm1 were determined by RT-qPCR as in Figure 3 . Values in A were normalized to 18S RNA, and values in B were normalized to GAPDH RNA. Data are expressed as means ± SD of 7-9 subjects/group and are presented relative to HC (1-fold), * p
Techniques Used: Purification, Isolation, Magnetic Cell Separation, Selection, Quantitative RT-PCR
10) Product Images from "Independent regulation of JNK/p38 mitogen-activated protein kinases by metabolic oxidative stress in the liver"
Article Title: Independent regulation of JNK/p38 mitogen-activated protein kinases by metabolic oxidative stress in the liver
Journal: Proceedings of the National Academy of Sciences of the United States of America
doi:
![Constitutive activity of p38 MAP kinase in the liver is inactivated by metabolic oxidative stress. ( A ) p38 MAP kinase inactivation in CCl 4 -treated liver extracts. The activity of p38 MAP kinase was measured by an immunecomplex protein kinase assay using [γ- 32 P]ATP and GST-ATF-2(1–109) as a substrate. The phosphorylated GST-ATF-2(1–109) was detected after SDS/PAGE by autoradiography. ( B ) p38 MAP kinase phosphorylation during oxidative stress. About 200 μg of liver extracts from control or CCl 4 -treated mice was electrophoresed on a 10% SDS/PAGE gel, blotted, and probed with antisera specific to phospho-p38 (New England Biolabs) or with antisera specific to p38. Arrows indicate specific immune complexes to either phospho-p38 or p38 protein as detected by enhanced chemiluminescence (DuPont). ( C ) Activation of MKP-1 by metabolic oxidative stress. MKP-1 mRNA levels were analyzed by RNase protection assay. MKP-1 mRNA levels were quantitated using a Molecular Dynamics PhosphorImager and normalized for 18S RNA. The mean results of two experiments are shown. ( D ) Localization of MKP-1 mRNA was determined using in situ hybridization. [ 35 S]-labeled MKP-1 antisense probe was hybridized to 7-μm sections of liver tissue from control and 4-hr CCl 4 -treated livers. The same field is shown using both bright-field and dark-field optics. P, portal vein; C, central vein. (×100.)](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC24019/bin/pq2260444004.jpg "... using a Molecular Dynamics PhosphorImager and normalized for 18S RNA. The mean results of two experiments are ...")
Figure Legend Snippet: Constitutive activity of p38 MAP kinase in the liver is inactivated by metabolic oxidative stress. ( A ) p38 MAP kinase inactivation in CCl 4 -treated liver extracts. The activity of p38 MAP kinase was measured by an immunecomplex protein kinase assay using [γ- 32 P]ATP and GST-ATF-2(1–109) as a substrate. The phosphorylated GST-ATF-2(1–109) was detected after SDS/PAGE by autoradiography. ( B ) p38 MAP kinase phosphorylation during oxidative stress. About 200 μg of liver extracts from control or CCl 4 -treated mice was electrophoresed on a 10% SDS/PAGE gel, blotted, and probed with antisera specific to phospho-p38 (New England Biolabs) or with antisera specific to p38. Arrows indicate specific immune complexes to either phospho-p38 or p38 protein as detected by enhanced chemiluminescence (DuPont). ( C ) Activation of MKP-1 by metabolic oxidative stress. MKP-1 mRNA levels were analyzed by RNase protection assay. MKP-1 mRNA levels were quantitated using a Molecular Dynamics PhosphorImager and normalized for 18S RNA. The mean results of two experiments are shown. ( D ) Localization of MKP-1 mRNA was determined using in situ hybridization. [ 35 S]-labeled MKP-1 antisense probe was hybridized to 7-μm sections of liver tissue from control and 4-hr CCl 4 -treated livers. The same field is shown using both bright-field and dark-field optics. P, portal vein; C, central vein. (×100.)
Techniques Used: Activity Assay, Protein Kinase Assay, SDS Page, Autoradiography, Mouse Assay, Activation Assay, Rnase Protection Assay, In Situ Hybridization, Labeling
11) Product Images from "Actin-Related Protein 2 (ARP2) and Virus-Induced Filopodia Facilitate Human Respiratory Syncytial Virus Spread"
Article Title: Actin-Related Protein 2 (ARP2) and Virus-Induced Filopodia Facilitate Human Respiratory Syncytial Virus Spread
Journal: PLoS Pathogens
doi: 10.1371/journal.ppat.1006062
Figure Legend Snippet: ARP2 knockdown in human respiratory epithelial A549 cells. (A) Knockdown of ARP2 protein expression. Replicate monolayers of A549 cells were transfected with siARP2, siControl, or no siRNA, as indicated. At 48 hr post-transfection, one set of monolayers was harvested. The others were infected with RSV-GFP (MOI = 1) or mock-infected, and harvested at 24, 48, and 72 hpi, as indicated. The cells were processed for Western blotting. ARP2 protein was detected using a primary rabbit mAb and an anti-rabbit IgG IRDye800 secondary Ab. Alpha-tubulin, as a loading control, was detected with a primary mouse mAb and an anti-mouse IgG IRDye680 secondary Ab. Bound antibodies were visualized by infrared fluorescence. One representative of four independent experiments is shown. (B) Knockdown of ARP2 mRNA expression. A549 cells were transfected with siARP2, siControl, or no siRNA, as indicated. Sets of monolayers were harvested 24 and 48 hr post-transfection. The remaining monolayers were infected with RSV-GFP (MOI = 1) or mock-infected, and harvested at 24, 48, and 72 hpi, as indicated. Total cell-associated ARP2 mRNA was quantified by real-time PCR using a TaqMan assay for ARP2. 18S ribosomal RNA was used as an endogenous control for normalization of each reaction, and the values of ARP2 expression are shown as fold-change relative to the no-siRNA control 24 hr post-transfection. Each sample was tested in quadruplicate by TaqMan assay and the averages are presented. (C) ARP2 knockdown did not reduce cell viability. A549 cells were transfected with siARP2, siControl or no siRNA for 48 hr. Cell viability was compared using alamarBlue and expressed relative to the no-siRNA control. Data from three independent experiments, each done in triplicate were combined for analysis. Error bars show standard deviation (SD).
Techniques Used: Expressing, Transfection, Infection, Western Blot, Fluorescence, Real-time Polymerase Chain Reaction, TaqMan Assay, Standard Deviation
12) Product Images from "Targeted DNA oxidation by LSD1–SMAD2/3 primes TGF-β1/ EMT genes for activation or repression"
Article Title: Targeted DNA oxidation by LSD1–SMAD2/3 primes TGF-β1/ EMT genes for activation or repression
Journal: Nucleic Acids Research
doi: 10.1093/nar/gkaa599
Figure Legend Snippet: Nuclear G oxidation induced by TGF-β1 through the histone demethylase, LSD1. (A) Immunofluorescence detection of 8-oxo-dG by fluorescein-tagged anti-8-oxo-dG antibody in cells pretreated with 5 mM NAC or 5 μM DPI for 1 h before stimulation with 10 ng/ml TGF-β1 for 30 min. Nuclei were stained with TO-PRO-3 Iodide in red while 8-oxo-dG foci were stained in green, as described in the ‘Materials and Methods’ section. Fluorescence quantization and statistical analysis are shown in Supplementary Figures S1C and S1-Stat3–6 . (B) Immunofluorescence detection of 8-oxo-dG by fluorescein-tagged anti-8-oxo-dG antibody in cells transfected with scrambled short hairpin (shCTRL) and shLSD1 RNAs for 24 h before stimulation with 10 ng/ml TGF-β1 for 30 min. Nuclei were stained with TO-PRO-3 Iodide in red while 8-oxo-dG foci were stained in green. Colocalization was measured using ImageJ (Coloc_2 plugin) as described in the ‘Materials and Methods’ section. Fluorescence quantization and statistical analysis are shown in Supplementary Figures S1D and S1-Stat3–6 . (C) Immunofluorescence microscopy of phalloidin in red and E-cadherin in green in control or LSD1-depleted cells exposed to 10 ng/ml TGF-β1 for 72 h. (D–G) mRNA levels of genes regulated by TGF-β1 in cells treated with shLSD1 or with TCP. Results are the mean of at least three experiments performed three times ( n = 9). MANOVA was used to examine the association between the mRNA levels after TGF-β1 and LSD1 depletion; the interaction was significant (see Supplementary Figure 2-Stat.2 for panel D and Supplementary Figure 2-Stat.4 for panel E). Differences between the means of three or more groups were determined by MANOVA. Differences between three or more samples were determined by one-way ANOVA test. Pairwise comparison was performed with Student’s t -test (see Supplementary Figures -Stat). (D) mRNA levels of SNAI1, CDH2, VIM and PAI genes in cells induced for 90 min with TGF-β1 determined by qPCR. Total RNA was isolated, reverse transcribed and amplified by qPCR with specific primers ( Supplementary Table S1 ). The values were normalized to 18S RNA. RNA was isolated as described in the ‘Materials and Methods’ section. * P
Techniques Used: Immunofluorescence, Staining, Fluorescence, Transfection, Microscopy, Real-time Polymerase Chain Reaction, Isolation, Amplification
13) Product Images from "Role of Muscle c-Jun NH2-Terminal Kinase 1 in Obesity-Induced Insulin Resistance ▿"
Article Title: Role of Muscle c-Jun NH2-Terminal Kinase 1 in Obesity-Induced Insulin Resistance ▿
Journal: Molecular and Cellular Biology
doi: 10.1128/MCB.01162-09
Figure Legend Snippet: Effect of muscle-specific JNK1 deficiency on hepatic lipogenic gene expression. Gene expression in the liver of chow-fed (ND) and HFD-fed (HF) M WT and M KO mice was measured by quantitative RT-PCR analysis of mRNA. Data for the expression of transcription factors ( C/ebp α, C/ebp β, Ppar γ, and Srebp1 ), coactivators ( Pgc1 α and Pgc1 β), fatty acid synthase ( Fas ), and microsomal triglyceride transfer protein ( Mttp ) mRNA are presented. The relative mRNA expression level was calculated by normalization of the data to the amount of 18S RNA in each sample (means ± SD) ( n = 6 to ∼8). Statistically significant differences are indicated (*, P
Techniques Used: Expressing, Mouse Assay, Quantitative RT-PCR
Figure Legend Snippet: Effect of muscle-specific JNK1 deficiency on hepatic inflammatory gene expression. Gene expression in the liver of chow-fed (ND) and HFD-fed (HF) M WT and M KO mice fasted overnight was measured by quantitative RT-PCR analysis of mRNA (TaqMan assays). Data for the expression of Tnf α, Il6 , Ifn γ, Cd68 , Icam1 , Lyzs , and cytochrome p450 2E1 ( Cye2e1 ) mRNAs are presented. The relative mRNA expression level was calculated by normalization of the data to the amount of 18S RNA in each sample (means ± SD) ( n = 6 to ∼8). Statistically significant differences are indicated (*, P
Techniques Used: Expressing, Mouse Assay, Quantitative RT-PCR
14) Product Images from "Regulation of p53 by Hypoxia: Dissociation of Transcriptional Repression and Apoptosis from p53-Dependent Transactivation"
Article Title: Regulation of p53 by Hypoxia: Dissociation of Transcriptional Repression and Apoptosis from p53-Dependent Transactivation
Journal: Molecular and Cellular Biology
doi: 10.1128/MCB.21.4.1297-1310.2001
Figure Legend Snippet: (A) TSA inhibits p53-dependent apoptosis under hypoxia. H1299 cells transfected with a p53 expression vector under the control of the tetracycline promoter were treated with IR or hypoxia. One group of cells did not receive any additional treatment (CON). TSA (25 nM) was added to a second group 1 h prior to treatment. A third group was treated with doxycycline 2 h prior to treatment, while both TSA and doxycycline were added to a fourth group prior to treatments. At the end of the treatment, cells with apoptotic morphology were visualized with Hoechst 3342 and phosphatidyl inositol staining. The total number of cells and the number of apoptotic cells in four different fields in 60-mm-diameter dishes were counted and expressed as the percentage of the total number of cells. Numbers represent the average of three independent experiments. Error bars represent SEM (B) TSA inhibits p53 transrepression under hypoxia. RKO cells were treated as described above, with the exception that cells were lysed 6 h after IR treatment and 12 h after hypoxia treatment. Northern blot analysis was performed on total RNA using a probe for human α-tubulin and 18S rRNA as described above.
Techniques Used: Transfection, Expressing, Plasmid Preparation, Staining, Northern Blot
Figure Legend Snippet: Hypoxia induces p53-dependent transrepression. (A) Doxycycline (200 ng/ml) induces p53 expression in H1299 cells transfected with a tet -inducible construct (clone 30) under normoxic and hypoxic conditions. The slight increase in p53 levels under hypoxia in the absence of doxycycline is probably due to stabilization of residual p53 expressed due to the “leakiness” of the construct. (B) Northern analysis of β-tubulin (β-tubul.) mRNA levels in an H1299 clone expressing a tet -inducible p53 construct and the parental clone transfected with empty vector. Cells were treated with hypoxia, doxycycline, or doxycycline for 2 h followed by treatment with hypoxia. In this cell line, hybridization with the β-tubulin probe results in two signals, probably because of alternative splicing of the β-tubulin. At the bottom, a methylene blue-stained nitrocellulose membrane, indicating levels of 18S and 28S RNA is shown. (C) Northern blot analysis of the p53-transrepressed gene coding for α-tubulin after treatment of p53 +/+ and p53 −/− MEFs with hypoxia or with 10 J of UV radiation/m 2 . Hybridization to 18S rRNA was used as a control. This is a light PhosphorImager scan that better represents the repression levels of α-tubulin. Values represent relative β-tubulin levels.
Techniques Used: Expressing, Transfection, Construct, Northern Blot, Plasmid Preparation, Hybridization, Staining
15) Product Images from "Complete maturation of the plastid protein translocation channel requires a type I signal peptidase"
Article Title: Complete maturation of the plastid protein translocation channel requires a type I signal peptidase
Journal: The Journal of Cell Biology
doi: 10.1083/jcb.200506171
Figure Legend Snippet: Disruption of PLSP1 results in a seedling lethal phenotype and reduction of the development of plastid internal membranes. (A) Structure of PLSP1 . Gray boxes and solid lines indicate exons and introns, respectively. The position of the T-DNA insertion in plsp1-1 was determined experimentally and is indicated with a white arrowhead. Positions of primers used for genomic and RT-PCR are indicated with black arrows. Primers and inserted T-DNA indicated with arrows/arrowhead are not to scale. (B) Seedlings of wild-type (wt), plsp1-1 , and plsp1-1;PLSP1 plants grown on MS media supplemented with 1% sucrose for 2 wk. Bar, 1 cm. (C) Genomic PCR of wild-type and mutant A. thaliana seedlings. E, I, and C indicate reactions specific to amplify endogenous PLSP1 , the T-DNA insertion, and the transgene used to complement the mutation, respectively. Primers that were used are listed as follows: F2 and R1 for E, F2 and R3 for I, and primers from 35S promoter (forward) and nopaline synthase terminator (reverse) for C. (D) RT-PCR analyses of wild-type and mutant A. thaliana seedlings. Each reaction contained two sets of primers: one for PLSP1 cDNA (F1 and R2) that produces a 400-bp fragment and another for cDNA derived from 18S RNA that produces a 315-bp fragment. Images from different portions of the same gel are in separate boxes. (E and F) Plastids in 2-wk-old wild-type (E) and homozygous plsp1-1 (F) cotyledons. Plastoglobules are indicated with asterisks. (G and H) Plastid in 7-wk-old wild-type (G) and homozygous plsp1-1 (H) etiolated seedlings. White and black arrowheads indicate PLB and disorganized membrane structure, respectively. (E–H) Bars, 1 μm.
Techniques Used: Reverse Transcription Polymerase Chain Reaction, Mass Spectrometry, Polymerase Chain Reaction, Mutagenesis, Derivative Assay
16) Product Images from "Both Microtubule-Stabilizing and Microtubule-Destabilizing Drugs Inhibit Hypoxia-Inducible Factor-1α Accumulation and Activity by Disrupting Microtubule Function"
Article Title: Both Microtubule-Stabilizing and Microtubule-Destabilizing Drugs Inhibit Hypoxia-Inducible Factor-1α Accumulation and Activity by Disrupting Microtubule Function
Journal: Cancer research
doi: 10.1158/0008-5472.CAN-04-4095
Figure Legend Snippet: Microtubule-targeting drugs inhibit HIF-1α at the post-transcriptional level. A , total RNA was prepared from treated cells under normoxic and hypoxic conditions. Northern blotting was done with 32 P-labeled probes for HIF-1α and Glut-1. 18S RNA and β-actin are shown as loading controls. B , 1A9 cells were pretreated overnight with either 25 mol/L vincristine or 25 mol/L epothilone B. The cells were then cotreated with MG-132 (10 Amol/L) in the presence or absence of the drugs for the indicated time (minutes). Equal amount of proteins from each lysate was resolved by SDS-PAGE and blotted for HIF-1α protein. The same gels were stripped and reblotted for actin. Arrows , ubiquinated HIF-1α protein species. C , 1A9 cells transiently transfected with pBI-GL V6L (6xHREs of VEGF promoter) were treated with vehicle or 100 nmol/L of each indicated drug under normoxic and hypoxic conditions. Luciferase reporter activity was measured in the cellular extract 16 hours later. Luciferase activity represents arbitrary units per microgram protein in each assay point. *, P
Techniques Used: Northern Blot, Labeling, SDS Page, Transfection, Luciferase, Activity Assay
17) Product Images from "Survey of Human Genes of Retroviral Origin: Identification and Transcriptome of the Genes with Coding Capacity for Complete Envelope Proteins"
Article Title: Survey of Human Genes of Retroviral Origin: Identification and Transcriptome of the Genes with Coding Capacity for Complete Envelope Proteins
Journal: Journal of Virology
doi: 10.1128/JVI.77.19.10414-10422.2003
Figure Legend Snippet: Transcript levels of the coding retroviral envelope genes of the human genome in a panel of 19 healthy human tissues, as determined by real-time quantitative PCR. Each value is expressed as the mean ± standard deviation relative to the value for a reference control plasmid assayed in each real-time PCR experiment (see Materials and Methods), after correction for total RNA content in each tissue extract (using the 18S transcript as an internal control). The code for the logarithmic gray scale is indicated on the right. PBL, peripheral blood lymphocytes.
Techniques Used: Real-time Polymerase Chain Reaction, Standard Deviation, Plasmid Preparation
18) Product Images from "The Extract of Leonurus sibiricus Transgenic Roots with AtPAP1 Transcriptional Factor Induces Apoptosis via DNA Damage and Down Regulation of Selected Epigenetic Factors in Human Cancer Cells"
Article Title: The Extract of Leonurus sibiricus Transgenic Roots with AtPAP1 Transcriptional Factor Induces Apoptosis via DNA Damage and Down Regulation of Selected Epigenetic Factors in Human Cancer Cells
Journal: Neurochemical Research
doi: 10.1007/s11064-018-2551-6
Figure Legend Snippet: Expression profiles of UHRF1 and DNMT1 genes. qRT-PCR analysis of UHRF1 and DNMT1 in glioma cells in IV grade and U87MG cells cultured for 24 h in the presence of L. sibiricus TR and AtPAP1 root extracts. Each gene was normalized to the expression of a 18S RNA- reference gene. Data is presented as fold change in glioma cells in IV grade and U87MG cells vs. untreated cells, in which expression levels of the genes were set as 1. The mean values ± SD were calculated from three independent experiments. * p
Techniques Used: Expressing, Quantitative RT-PCR, Cell Culture
19) Product Images from "The elusive MAESTRO gene: Its human reproductive tissue-specific expression pattern"
Article Title: The elusive MAESTRO gene: Its human reproductive tissue-specific expression pattern
Journal: PLoS ONE
doi: 10.1371/journal.pone.0174873
Figure Legend Snippet: Relative expression of MRO transcripts was analyzed by qPCR. (A) Schematic representation of the MRO splice variants and the position of the TaqMan probes. Overall expression detected by the pQ8/9 probe. pQ1/3 spans exons 1–3 and detects the 'b' isoforms ( MROb 1-4); pQ2/3 spans exons 2/3 and detects isoforms MROa ,c,d. The expression of MRO was normalized to 18s RNA and presented as relative a expression ratio (1/ΔCt). (B) MRO transcripts analysis in GCs and CCs from PCOS and control subjects. The overall expression, shown by exon 8/9 was higher in PCOS cells vs that of controls (* in GCs and * in CCs; p ≤0.05). Inverse expression of exon 1/3 in GCs and CCs vs exon 2/3 was detected. (C) Inverse expression of exon 2/3 vs 1/3 in kidney, liver, brain and post-menopausal ovary.
Techniques Used: Expressing, Real-time Polymerase Chain Reaction
20) Product Images from "The Extract of Leonurus sibiricus Transgenic Roots with AtPAP1 Transcriptional Factor Induces Apoptosis via DNA Damage and Down Regulation of Selected Epigenetic Factors in Human Cancer Cells"
Article Title: The Extract of Leonurus sibiricus Transgenic Roots with AtPAP1 Transcriptional Factor Induces Apoptosis via DNA Damage and Down Regulation of Selected Epigenetic Factors in Human Cancer Cells
Journal: Neurochemical Research
doi: 10.1007/s11064-018-2551-6
Figure Legend Snippet: Expression profiles of UHRF1 and DNMT1 genes. qRT-PCR analysis of UHRF1 and DNMT1 in glioma cells in IV grade and U87MG cells cultured for 24 h in the presence of L. sibiricus TR and AtPAP1 root extracts. Each gene was normalized to the expression of a 18S RNA- reference gene. Data is presented as fold change in glioma cells in IV grade and U87MG cells vs. untreated cells, in which expression levels of the genes were set as 1. The mean values ± SD were calculated from three independent experiments. * p
Techniques Used: Expressing, Quantitative RT-PCR, Cell Culture
21) Product Images from "Disrupted synaptic development in the hypoxic newborn brain"
Article Title: Disrupted synaptic development in the hypoxic newborn brain
Journal: Proceedings of the National Academy of Sciences of the United States of America
doi: 10.1073/pnas.232568799
Figure Legend Snippet: Hypoxia induced VEGF-regulated pathways in both neurons and the microvasculature. ( A ) Composite micrographs of representative sections of P11 brain harvested from Nx and Hx animals. VEGF and its receptor Flk-1 were increased in neurons throughout the cortex, with marked concentrations in the dentate gyrus and in the CA1 region of the hippocampus. Microarray analysis indicated a > 1.4-fold enhancement (Hx/N) at P11 for VEGF (Table 1). This same result was also obtained by conventional Northern blot analysis ( Inset : dark bars, Hx/N by blot; light bars, microarray results), by using freshly extracted mRNA standardized against 18S ribosomal RNA. ( B ) Western blot analysis, standardized against actin, of ARNT and HIF-1α. Note that although ARNT levels remain nearly unchanged, the upstream inducer of VEGF expression, HIF-1α, is up-regulated at P11.
Techniques Used: Microarray, Northern Blot, Western Blot, Expressing
22) Product Images from "HIC1 (Hypermethylated in Cancer 1) modulates the contractile activity of prostate stromal fibroblasts and directly regulates CXCL12 expression"
Article Title: HIC1 (Hypermethylated in Cancer 1) modulates the contractile activity of prostate stromal fibroblasts and directly regulates CXCL12 expression
Journal: Oncotarget
doi: 10.18632/oncotarget.27786
![RT-qPCR analyses of HIC1 expression in normal human prostate and human PCa tissues. ( A ) Profiles of HIC1 expression in 10 pairs of cancerous and matched normal prostate tissues. Total RNAs were extracted and quantitative expression of the two major HIC1 isoforms’ expression was measured by RT-qPCR analyses. Results are normalized to ALAS1 RNA [ 51 ] or 18S rRNA and are presented as means +/− S.D. from two experiments in triplicate. For each patient, the percentage of normal stroma present in the tumor samples which was used as the ranking criteria is indicated below as well as the TNM staging (see Supplementary Table 1 for details). ( B ) Analyses of HIC1 expression in prostate tumors. A cohort of 20 tumors for which the matched normal tissue was not available was analyzed by RT-qPCR analyses (black column) as described above except that the control corresponded to RNAs extracted from the prostate of a healthy young (24 year-old) donor (Biochain) as control. The 10 tumors used in panel A were also included in this study (orange column). ( C ) Quantification of HIC1 expression in the 30 prostate tumors clustered in subgroups according to their stromal content. HIC1 expression measured by RT-qPCR analyses of the 30 tumors in panel B is represented as box plots in comparison with its expression in a normal prostate tissue obtained from a young 24-years old donor. The box area corresponds to the first and third quartile. The median is shown as a horizontal line in the box. The maximum and minimum values are indicated by the whiskers above and below the box.](https://storage.googleapis.com/bioz_article_images/PMC7665237/oncotarget-11-4138-g003.jpg "... normalized to ALAS1 RNA [ 51 ] or 18S rRNA and are presented as means +/− S.D. ...")
Figure Legend Snippet: RT-qPCR analyses of HIC1 expression in normal human prostate and human PCa tissues. ( A ) Profiles of HIC1 expression in 10 pairs of cancerous and matched normal prostate tissues. Total RNAs were extracted and quantitative expression of the two major HIC1 isoforms’ expression was measured by RT-qPCR analyses. Results are normalized to ALAS1 RNA [ 51 ] or 18S rRNA and are presented as means +/− S.D. from two experiments in triplicate. For each patient, the percentage of normal stroma present in the tumor samples which was used as the ranking criteria is indicated below as well as the TNM staging (see Supplementary Table 1 for details). ( B ) Analyses of HIC1 expression in prostate tumors. A cohort of 20 tumors for which the matched normal tissue was not available was analyzed by RT-qPCR analyses (black column) as described above except that the control corresponded to RNAs extracted from the prostate of a healthy young (24 year-old) donor (Biochain) as control. The 10 tumors used in panel A were also included in this study (orange column). ( C ) Quantification of HIC1 expression in the 30 prostate tumors clustered in subgroups according to their stromal content. HIC1 expression measured by RT-qPCR analyses of the 30 tumors in panel B is represented as box plots in comparison with its expression in a normal prostate tissue obtained from a young 24-years old donor. The box area corresponds to the first and third quartile. The median is shown as a horizontal line in the box. The maximum and minimum values are indicated by the whiskers above and below the box.
Techniques Used: Quantitative RT-PCR, Expressing
23) Product Images from "Chicken MBD4 Regulates Immunoglobulin Diversification by Somatic Hypermutation"
Article Title: Chicken MBD4 Regulates Immunoglobulin Diversification by Somatic Hypermutation
Journal: Frontiers in Immunology
doi: 10.3389/fimmu.2019.02540
Figure Legend Snippet: SHM is elevated in DT40 derived MBD4 Δ/Δ clones. (A) Schematic of exons 4, 5, and 6 in the Mbd4 gene and primers F2 and R2 used for RT-PCR analysis. gRNA sequence is indicated by a line (g) in early exon 5 ( upper panel ). Semi-quantitative RT-PCR analysis of Mbd4 exons 5–6 in parental and deleted clones ( middle panel ). QRT-PCR analysis of 18S RNA was used as a loading control ( lower panel ). 18S sample values were normalized to parental values which were set to 1. Samples were assayed in triplicate and were averaged, and SEMs are shown. (B) Cell proliferation assays. Cells (1 × 10 5 /ml) were grown in culture for 96 h and live cells were counted in triplicate every 24 h. The data shown is the average and is representative of 3 independent samples. (C) IgM fluorescence loss is analyzed in parental and MBD4 Δ/Δ .14, MBD4 Δ/Δ .11, and MBD4 Δ/Δ .12 deletion clones by flow cytometry. Cells were FACS sorted at day 0 for IgM + GFP + cells and re-analyzed after 28 days in culture. Flow cytometry analyses are representative of 24 parental- and 12 subclones from each of the MBD4 Δ/Δ deletion clones. (D) IgM fluorescence loss was quantitated for each parental and MBD4 Δ/Δ deletion subclone after 28 days in culture. Each data point is representative of a single sub-clone. Bars indicate the median in each data set. P -value * p
Techniques Used: Derivative Assay, Reverse Transcription Polymerase Chain Reaction, Sequencing, Quantitative RT-PCR, Clone Assay, Fluorescence, Flow Cytometry, Cytometry, FACS
24) Product Images from "Structural Optimization of 2,3-Dihydro-1H-cyclopenta[b]quinolines Targeting the Noncatalytic RVxF Site of Protein Phosphatase 1 for HIV-1 Inhibition"
Article Title: Structural Optimization of 2,3-Dihydro-1H-cyclopenta[b]quinolines Targeting the Noncatalytic RVxF Site of Protein Phosphatase 1 for HIV-1 Inhibition
Journal: ACS infectious diseases
doi: 10.1021/acsinfecdis.0c00511
Figure Legend Snippet: Inhibition of HIV-1 IIIB infection and metabolic stability of 1E7-03 analogues. (A and B) HIV-1 gag for details). RNA was extracted from the infected cells treated with DMSO, 10 μ M 1E7-03, 10 μ M HU-1a, 10 μ M HU-1c, 10 μ M HU-1d, or 25 μ M AZT for 72 h. RNA expression was analyzed by RT-PCR using 18S mRNA for normalization. The means ± SD are shown ( n = 3 for all panels). * p
Techniques Used: Inhibition, Infection, RNA Expression, Reverse Transcription Polymerase Chain Reaction
25) Product Images from "Tissue-Specific Transgenic Knockdown of Fos-Related Antigen 2 (Fra-2) Expression Mediated by Dominant Negative Fra-2"
Article Title: Tissue-Specific Transgenic Knockdown of Fos-Related Antigen 2 (Fra-2) Expression Mediated by Dominant Negative Fra-2
Journal: Molecular and Cellular Biology
doi: 10.1128/MCB.21.11.3704-3713.2001
Figure Legend Snippet: DII is a candidate target gene for Fra-2 action. (A) Reverse Northern analysis of radiolabeled pineal (midnight) cRNA from WT and NATDNF2 rats. The immobilized plasmid vectors were as follows: 1, pUC18; 2, Fra-2; 3, c-Fos; 4, AANAT; 5, β1-adrenergic receptor; 6, c-Jun; 7, γ-phosphodiesterase; 8, α1A-adrenergic receptor; 9, α1B-adrenergic receptor; 10, preproenkephalin; 11, DII; 12, S antigen; 13, ICER; 14, RZRβ. All expression vectors contain rat genes. (B) Northern blot analysis of total pineal RNA (∼7 μg) extracted from WT and NATDNF2 animals that were sacrificed at the indicated clock times (CT) throughout the dark phase of a 24-h cycle. Blots were exposed to rat DII and 18S ribosomal probes. (C) Quantitation of the relative abundance of the DII/18S steady-state transcript levels at 22 ( n = 3 pairs of rats) and 24 ( n = 4 pairs of rats) h. Open bars, WT; closed bars, NATDNF2.
Techniques Used: Northern Blot, Plasmid Preparation, Expressing, Quantitation Assay
![Tissue survey of DNF2 expression and effects of pineal expression on the Fra-2 response in the night pineal gland. (A) Northern blot analysis performed with total RNA (∼5 μg) extracted from the indicated tissues that were harvested in the middle of the night from transgenic animals designated H17 and carrying a high copy number (estimated at 45 per haploid genome) of the NATDNF2 transgene. The membrane was probed with Fra-2 and GAPDH radiolabeled probes. Blots were exposed to X-ray film for 24 h. No DNF2 signal was observed in WT animals (not shown). (B) Northern blot analysis of total pineal RNA (∼7 μg) was used to investigate the nocturnal Fra-2 response in WT animals and in a high-copy-number transgenic line (H17). Levels of fra-2 and DNF2 mRNAs were assessed at three different time points during the night along with the levels of the 18S rRNA. Downregulation of nocturnal fra-2 mRNA expression was also observed in an independent experiment using samples derived from H16 transgenic rats. CT, clock time (hours). (C) Western blot analysis of pineal proteins prepared from WT mice or animals carrying a range of DNF2 transgene copy numbers (2 [H4], 5 [H13], 20 [H16], and 45 [H17] copies per haploid genome). Animals were sacrificed at the indicated clock times, and SDS-PAGE was run with total pineal protein samples. After electrophoretic transfer, the membrane was exposed to a pan-Fos rabbit antibody directed against the invariant M peptide between aa 129 to 153 in the mouse c-Fos sequence (SC253x). For both panels, the light-dark cycle was 12:12 with lights off at 7 p.m. Selective downregulation of Fra-2 protein was observed in two independent experiments using samples derived from additional H17 transgenic rats.](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC87005/bin/mb1112121002.jpg "... the night along with the levels of the 18S rRNA. Downregulation of nocturnal fra-2 mRNA expression was ...")
Figure Legend Snippet: Tissue survey of DNF2 expression and effects of pineal expression on the Fra-2 response in the night pineal gland. (A) Northern blot analysis performed with total RNA (∼5 μg) extracted from the indicated tissues that were harvested in the middle of the night from transgenic animals designated H17 and carrying a high copy number (estimated at 45 per haploid genome) of the NATDNF2 transgene. The membrane was probed with Fra-2 and GAPDH radiolabeled probes. Blots were exposed to X-ray film for 24 h. No DNF2 signal was observed in WT animals (not shown). (B) Northern blot analysis of total pineal RNA (∼7 μg) was used to investigate the nocturnal Fra-2 response in WT animals and in a high-copy-number transgenic line (H17). Levels of fra-2 and DNF2 mRNAs were assessed at three different time points during the night along with the levels of the 18S rRNA. Downregulation of nocturnal fra-2 mRNA expression was also observed in an independent experiment using samples derived from H16 transgenic rats. CT, clock time (hours). (C) Western blot analysis of pineal proteins prepared from WT mice or animals carrying a range of DNF2 transgene copy numbers (2 [H4], 5 [H13], 20 [H16], and 45 [H17] copies per haploid genome). Animals were sacrificed at the indicated clock times, and SDS-PAGE was run with total pineal protein samples. After electrophoretic transfer, the membrane was exposed to a pan-Fos rabbit antibody directed against the invariant M peptide between aa 129 to 153 in the mouse c-Fos sequence (SC253x). For both panels, the light-dark cycle was 12:12 with lights off at 7 p.m. Selective downregulation of Fra-2 protein was observed in two independent experiments using samples derived from additional H17 transgenic rats.
Techniques Used: Expressing, Northern Blot, Transgenic Assay, Derivative Assay, Western Blot, Mouse Assay, SDS Page, Sequencing
Figure Legend Snippet: cDNA array-based identification of nectadrin as a candidate Fra-2 target gene. (A) Representative details of duplicate rat expression arrays (Clontech's Atlas rat 1.2) probed with cDNAs derived from either transgenic (H17) or control (C17) littermate pineal glands sampled at 24 h. The nectadrin gene is located at position 1A. Following hybridization and washing, arrays were exposed to a storage phosphor screen (Kodak-K) for 3 days and visualized using a model FX molecular imager (Bio-Rad). Images were downloaded as TIFFs and montaged using Adobe Photoshop, version 4.0. The level of nectadrin mRNA is significantly reduced at midnight in the pineal gland of NATDNF2 rats. (B) Nectadrin expression displays a robust day/night rhythm in the rat pineal gland, as determined by Northern blot analysis of total pineal RNA (∼7 μg) extracted from WT and NATDNF2 animals that were sacrificed at the indicated clock times (CT) throughout the dark phase of a 24-h cycle. Blots were exposed to rat nectadrin and 18S probes. (C) Quantitation of the relative abundance of the nectadrin/18S steady-state transcript levels at 22 and 24 h ( n = 3 pairs of rats in each group). Open bars, WT; closed bars, NATDNF2. Statistical analysis for both DII and nectadrin levels of expression was performed by an unpaired t test, using corrected percentages as input values. The DII level is different from control at both 22 and 24 h, while the nectadrin is different from control at only 24 h, at a significance level of P
Techniques Used: Expressing, Derivative Assay, Transgenic Assay, Hybridization, Northern Blot, Quantitation Assay
Figure Legend Snippet: Expression of DNF2 protein has no effect on pineal AANAT expression or melatonin production. (A) Northern blot analysis of total pineal RNA (∼7 μg) extracted from WT and NATDNF2 animals that were sacrificed at the indicated clock times throughout a 24-h cycle. Blots were exposed to rat AANAT, DNF2, and 18S probes. The absence of transgene-associated changes in nocturnal AANAT mRNA level was confirmed in an independent experiment using samples derived from additional H17 transgenic rats. There were six rats in each group. (B) WT and H17 NATDNF2 rats were maintained in individual metabolic cages on a 12:12 light-dark cycle (lights off at clock time 19). Urine was collected every 6 h, starting at clock time 12, and urinary 6-sulfatoxymelatonin (expressed as total nanograms produced/period) was assessed for each group.
Techniques Used: Expressing, Northern Blot, Derivative Assay, Transgenic Assay, Produced
26) Product Images from "Altered Patterns of Cellular Gene Expression in Dermal Microvascular Endothelial Cells Infected with Kaposi's Sarcoma-Associated Herpesvirus"
Article Title: Altered Patterns of Cellular Gene Expression in Dermal Microvascular Endothelial Cells Infected with Kaposi's Sarcoma-Associated Herpesvirus
Journal: Journal of Virology
doi: 10.1128/JVI.76.7.3395-3420.2002
Figure Legend Snippet: Demonstration of virus-encoded latent and lytic cycle gene expression in KSHV-infected DMVEC cultures. (A) Standard nonquantitative RT-PCR products obtained for selected ORF-K1, ORF-K8, and ORF-K8.1 lytic cycle viral genes in the same set of four DMVEC RNA samples used to generate the probes for the Clontech gene array hybridization experiments (RNA batch 1). Each viral primer pair chosen encompassed known intron loci to confirm that the PCR products were derived from spliced mRNA. Primers for 18S rRNA were used as the loading control. Lane 1, control uninfected DMVEC RNA; lane 2, KSHV-infected DMVEC RNA; lane 3, uninfected DMVEC +TPA RNA; lane 4, KSHV-infected DMVEC +TPA RNA. (B) Western immunoblot comparing the expression of KSHV-encoded LANA1 (latent) and ZMP-A (K5, lytic) proteins in uninfected and infected DMVEC cultures. Lane 1, control uninfected DMVEC extract; lane 2, KSHV-infected DMVEC extract; lane 3, uninfected DMVEC +TPA extract; lane 4, KSHV-infected DMVEC +TPA extract. A β-actin loading control on the same samples is also shown in the lower panel.
Techniques Used: Expressing, Infection, Reverse Transcription Polymerase Chain Reaction, Hybridization, Polymerase Chain Reaction, Derivative Assay, Western Blot
27) Product Images from "Transforming Growth Factor-β1 Selectively Recruits microRNAs to the RNA-Induced Silencing Complex and Degrades CFTR mRNA under Permissive Conditions in Human Bronchial Epithelial Cells"
Article Title: Transforming Growth Factor-β1 Selectively Recruits microRNAs to the RNA-Induced Silencing Complex and Degrades CFTR mRNA under Permissive Conditions in Human Bronchial Epithelial Cells
Journal: International Journal of Molecular Sciences
doi: 10.3390/ijms20194933
Figure Legend Snippet: TGF-β1 did not affect CFTR promoter activity but reduced the stability of CFTR mRNA. ( A ). Summary of the CFTR gene promoter reporter assays showing that luciferase activity was increased by expression of the vector containing 1 kb promoter pCFTR-pLuc, compared to vector control. Forskolin increased the luciferase activity of pCFTR-pLuc and TGF-β1 had no effect. Human embryonic kidney (HEK) cells were transfected with pCFTR-pLuc or vector control and 24 h later cells were treated with forskolin (10 µM), TGF-β1 (15 ng/mL), or vehicle control for 6 h. ( B ). The CFTR mRNA half-life measurements showing that TGF-β1 decreased CFTR mRNA stability in F508del HBE cells. The transcriptional inhibitor ActD (5 μg/mL) and either TGF-β1 or vehicle control were added to F508del HBE cells for 4, 8 or 24 h. Total RNA was isolated and the CFTR mRNA level at each time point was calculated by real-time quantitative reverse transcriptase PCR (qRT-PCR), using the relative quantitation method, with 18S as a reference gene. The amount of CFTR mRNA at 4 h was set to 100% ( t = 0) and mRNA half-lives were calculated from the exponential decay model, based on trend line equation C/C 0 = e −kdt (where C and C 0 are mRNA amounts at the time t and t 0 , respectively, and k d is the mRNA decay constant). The resulting curve equations were y (vehicle) = 123 −0.01x and y (TGF-β1) = 112 −0.007x . The calculated half-life of CFTR mRNA was 21.1 h and 13.7 h for the vehicle and TGF-β1-treated cells, respectively. N = 9–12 /group from 3–4 different HEK cell cultures ( A ) and N = 3 in triplicates in F508del HBE cells from three different donors ( B ). Error bars, S.E.M. **** p
Techniques Used: Activity Assay, Luciferase, Expressing, Plasmid Preparation, Transfection, Isolation, Polymerase Chain Reaction, Quantitative RT-PCR, Quantitation Assay
28) Product Images from "Constitutive Nuclear Factor-?B Activity Is Crucial for Human Retinoblastoma Cell Viability"
Article Title: Constitutive Nuclear Factor-?B Activity Is Crucial for Human Retinoblastoma Cell Viability
Journal: The American Journal of Pathology
doi:
Figure Legend Snippet: A: Immunoblotting analysis for the apoptosis inhibitors Bcl-2, BclxL, A1, cIAP-1, cIAP-2, XIAP, and survivin, as well as the proapoptotic molecule Bax, in the Y79 cell line treated with the NF-κB inhibitor SN50 (20 μmol/L) for 3 or 6 hours. NF-κB inhibition down-regulated the protein levels of Bcl-2, A1, and cIAP-2, and up-regulated Bax expression. B and C: Quantitative RT-PCR for Bcl-2 ( B ), Bax ( C ) and 18S RNA in Y79 cells treated with or without SN50 (20 μmol/L for 3 hours). NF-κB inhibition down-regulates Bcl-2 and up-regulates Bax mRNA levels.
Techniques Used: Inhibition, Expressing, Quantitative RT-PCR
29) Product Images from "Broad anti-coronaviral activity of FDA approved drugs against SARS-CoV-2 in vitro and SARS-CoV in vivo"
Article Title: Broad anti-coronaviral activity of FDA approved drugs against SARS-CoV-2 in vitro and SARS-CoV in vivo
Journal: bioRxiv
doi: 10.1101/2020.03.25.008482
Figure Legend Snippet: Hydroxychloroquine and chloroquine inhibit production of SARS-CoV-2 N and RdRp mRNA. Vero cells were pre-treated with hydroxychloroquine sulfate (A, C and E) or chloroquine phosphate (B, D and F) at the indicated concentration (or 0.1% water as vehicle control) for 2 h prior to infection with SARS-CoV-2 (WA-1 strain) at MOI 0.1. 24 h post-infection cells were collected in TRIzol. RNA was extracted from TRIzol sample and qRT-PCR was performed for viral RdRp (A and B) or N (C and D) mRNA using WHO primers. RNA levels were normalized with 18S RNA and fold change for drug treated to vehicle control was calculated (dotted line to denote a fold change of 1 which is no change over control). Data are from 3 independent infections performed on triplicate wells, the fold change was calculated in each independent experiment and the mean fold change is plotted with error bars displaying standard deviation. Along with TRIzol samples for RNA supernatant was collected from cells and used for TCID 50 assays to determine infectious virus production following treatment with HCQ (E) or CQ (F) Data are from 3 independent infections performed on triplicate wells with the TCID 50 /ml being averaged across all wells. Error bars are the standard deviation. G) Cells were treated with 50 μM HCQ or 0.1% water as control. Drug was either added 2 h prior to infection, at the time of infection or 2 h after infection with MOI 0.1 SARS-CoV-2. After 24 h infection, supernatant was collected and used for TCID 50 assays to determine infectious virus production. Data are from 3 independent infections performed on triplicate wells with the TCID 50 /ml being averaged across all wells. Error bars are the standard deviation. H) SARS-CoV spike psuedoviruses (PV) were used for infection of BSC1 cells. The cells were treated with 10 μM of CQ or CPZ for 1 h prior to infection with PV for 3 h. The PV carry BlaM and cells were loaded with CCF2 to monitor cleavage and shift in fluorescence output for evidence of S-mediated entry into cells. Data are normalised to PV alone and are from 3 independent experiments with error bars representing standard deviation.
Techniques Used: Concentration Assay, Infection, Quantitative RT-PCR, Standard Deviation, Fluorescence
30) Product Images from "The extracellular matrix component WIF-1 is expressed during, and can modulate, retinal development"
Article Title: The extracellular matrix component WIF-1 is expressed during, and can modulate, retinal development
Journal: Molecular and cellular neurosciences
doi: 10.1016/j.mcn.2004.08.003
Figure Legend Snippet: RNA encoding WIF-1 is expressed in the retina during retinal differentiation. (A) RT–PCR demonstrates WIF-1 RNA in extracts of retinae from embryonic day (E) 19, postnatal day (P) 5, and adult (Ad) mice. Equal amounts of RNA were loaded in each lane as shown by RT–PCR for 18S ribosomal RNA. (B) Sections of E16 and adult retinae were hybridized with antisense RNA probes for WIF-1. WIF-1 RNA is present in the ganglion cell layer (GCL), inner nuclear layer (INL), and outer nuclear layer (ONL), with little in the neuroblast layer (NBL).
Techniques Used: Reverse Transcription Polymerase Chain Reaction, Mouse Assay
31) Product Images from "Targeted DNA oxidation by LSD1–SMAD2/3 primes TGF-β1/ EMT genes for activation or repression"
Article Title: Targeted DNA oxidation by LSD1–SMAD2/3 primes TGF-β1/ EMT genes for activation or repression
Journal: Nucleic Acids Research
doi: 10.1093/nar/gkaa599
Figure Legend Snippet: Nuclear G oxidation induced by TGF-β1 through the histone demethylase, LSD1. (A) Immunofluorescence detection of 8-oxo-dG by fluorescein-tagged anti-8-oxo-dG antibody in cells pretreated with 5 mM NAC or 5 μM DPI for 1 h before stimulation with 10 ng/ml TGF-β1 for 30 min. Nuclei were stained with TO-PRO-3 Iodide in red while 8-oxo-dG foci were stained in green, as described in the ‘Materials and Methods’ section. Fluorescence quantization and statistical analysis are shown in Supplementary Figures S1C and S1-Stat3–6 . (B) Immunofluorescence detection of 8-oxo-dG by fluorescein-tagged anti-8-oxo-dG antibody in cells transfected with scrambled short hairpin (shCTRL) and shLSD1 RNAs for 24 h before stimulation with 10 ng/ml TGF-β1 for 30 min. Nuclei were stained with TO-PRO-3 Iodide in red while 8-oxo-dG foci were stained in green. Colocalization was measured using ImageJ (Coloc_2 plugin) as described in the ‘Materials and Methods’ section. Fluorescence quantization and statistical analysis are shown in Supplementary Figures S1D and S1-Stat3–6 . (C) Immunofluorescence microscopy of phalloidin in red and E-cadherin in green in control or LSD1-depleted cells exposed to 10 ng/ml TGF-β1 for 72 h. (D–G) mRNA levels of genes regulated by TGF-β1 in cells treated with shLSD1 or with TCP. Results are the mean of at least three experiments performed three times ( n = 9). MANOVA was used to examine the association between the mRNA levels after TGF-β1 and LSD1 depletion; the interaction was significant (see Supplementary Figure 2-Stat.2 for panel D and Supplementary Figure 2-Stat.4 for panel E). Differences between the means of three or more groups were determined by MANOVA. Differences between three or more samples were determined by one-way ANOVA test. Pairwise comparison was performed with Student’s t -test (see Supplementary Figures -Stat). (D) mRNA levels of SNAI1, CDH2, VIM and PAI genes in cells induced for 90 min with TGF-β1 determined by qPCR. Total RNA was isolated, reverse transcribed and amplified by qPCR with specific primers ( Supplementary Table S1 ). The values were normalized to 18S RNA. RNA was isolated as described in the ‘Materials and Methods’ section. * P
Techniques Used: Immunofluorescence, Staining, Fluorescence, Transfection, Microscopy, Real-time Polymerase Chain Reaction, Isolation, Amplification
32) Product Images from "Lytic Reactivation of the Kaposi’s sarcoma-associated herpesvirus (KSHV) is Accompanied by Major Nucleolar Alterations"
Article Title: Lytic Reactivation of the Kaposi’s sarcoma-associated herpesvirus (KSHV) is Accompanied by Major Nucleolar Alterations
Journal: bioRxiv
doi: 10.1101/2020.05.15.097808
Figure Legend Snippet: Northern blot analysis of rRNA during viral lytic reactivation. Total RNA was extracted from uninfected SLK and BAC16-mCherry-ORF45-infected iSLK cells that were either left untreated or treated with Dox and n-Butyrate for 48-hr. Lytic reactivation was confirmed by expression of mCherry-ORF45 in ∼80% of cells. 20 µg RNA from each sample was resolved on denaturing 1.2% agarose gel, transferred to nylon membranes, and hybridized with probes representing 5.8S, 18S and 28S rRNA. No accumulation of pre-rRNA processing products was evident upon lytic reactivation.
Techniques Used: Northern Blot, Infection, Expressing, Agarose Gel Electrophoresis
33) Product Images from "Diterpenoids from Plectranthus spp. as Potential Chemotherapeutic Agents via Apoptosis"
Article Title: Diterpenoids from Plectranthus spp. as Potential Chemotherapeutic Agents via Apoptosis
Journal: Pharmaceuticals
doi: 10.3390/ph13060123
Figure Legend Snippet: ( A ) Gene expression ( Bax, Bcl-2 , Cas-3 , and TP53 ) in A549 and ( B ) CCRF-CEM cell lines after 24 h treatment with all the compounds: Roy (3 µg/mL), Deroy (6.25 µg/mL), Diroy (25 µg/mL), and Parv (1.15 µg/mL) in A549 cells and Roy (0.7 µg/mL), Deroy (4.5 µg/mL), Diroy (25 µg/mL), and Parv (1.15 µg/mL) in CCRF-CEM cells. The transcript level of each gene was normalized to the expression of a reference gene ( 18S RNA ). Data are presented as a fold change in cells treated with tested compounds vs. untreated, control cells, in which expression levels of the genes were set as 1. The mean values ± SD were calculated in triplicates. The same letter (a, b, c and d) at the same genes is not significantly different at the level of p > 0.05.
Techniques Used: Expressing
Related Articles
Polymerase Chain Reaction:Article Title: Autophagy Plays a Role in Chloroplast Degradation during Senescence in Individually Darkened Leaves 1Autophagy Plays a Role in Chloroplast Degradation during Senescence in Individually Darkened Leaves 1 [W]Autophagy Plays a Role in Chloroplast Degradation during Senescence in Individually Darkened Leaves 1 [W] [OA] Article Snippet: .. Gene-specific primers used for autophagy gene PCR were 5′-ATGAAGGCTTTATGTGATAGATTTGTTC-3′ and 5′-TCAGAGCATTTGCCAGTCATCTTCA-3′ for ATG4a ; 5′-ATGAAGGCTTTATGTGATAGATTTGTTC-3′ and 5′-GTCACACAATGAAAAGAATGGCTAGGAG-3′ for ATG4b ( ); 5′-ATGGCGAAGGAAGCGGTCA-3′ and 5′-CACAAAGGAGATCGAAAAGAACAC-3′ for ATG5 ( ); 5′-AGCTCTTGAAGACCCTTCTGTG-3′ and 5′-AATCTGAGTCGCGCCAATC-3′ for ATG7 ; 5′-GTCCTCGACCCAGTAGGAACTATG-3′ and 5′-AGAAACTGCTTCCCAAGAGAATCTG-3′ for ATG9 ; and QuantumRNA 18s internal standards for 18s Article Title: ALDEHYDES POTENTIATE α2(I) COLLAGEN GENE ACTIVITY BY JNK IN HEPATIC STELLATE CELLS Article Snippet: .. PCR products were quantified by Amplification:Article Title: Expression of Stretch-Activated Two-Pore Potassium Channels in Human Myometrium in Pregnancy and Labor Article Snippet: .. Amplification was performed with the |
