real time rt pcr qpcr  (Solis BioDyne)


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    Solis BioDyne real time rt pcr qpcr
    AKH and AKHR isoforms differ in the tissue specificity of their expression. <t>RT-PCR</t> analysis of AKH and AKHR mRNAs was performed using tissues from larvae ( a ) as well as adult moths ( b ). The adult RNA samples other than testes and ovary contained male and female tissues in equal proportions. The mRNA levels were measured relative to BmActin, and BmTubulin mRNAs. The samples contained pooled tissues from several individuals. Values represent means ± SD from three independent experiments. Data were analyzed by Kruskal–Wallis test followed by pairwise comparisons using Wilcoxon rank sum test. The significant differences are indicated by different letters ( p
    Real Time Rt Pcr Qpcr, supplied by Solis BioDyne, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Functional Analysis of Adipokinetic Hormone Signaling in Bombyx mori"

    Article Title: Functional Analysis of Adipokinetic Hormone Signaling in Bombyx mori

    Journal: Cells

    doi: 10.3390/cells9122667

    AKH and AKHR isoforms differ in the tissue specificity of their expression. RT-PCR analysis of AKH and AKHR mRNAs was performed using tissues from larvae ( a ) as well as adult moths ( b ). The adult RNA samples other than testes and ovary contained male and female tissues in equal proportions. The mRNA levels were measured relative to BmActin, and BmTubulin mRNAs. The samples contained pooled tissues from several individuals. Values represent means ± SD from three independent experiments. Data were analyzed by Kruskal–Wallis test followed by pairwise comparisons using Wilcoxon rank sum test. The significant differences are indicated by different letters ( p
    Figure Legend Snippet: AKH and AKHR isoforms differ in the tissue specificity of their expression. RT-PCR analysis of AKH and AKHR mRNAs was performed using tissues from larvae ( a ) as well as adult moths ( b ). The adult RNA samples other than testes and ovary contained male and female tissues in equal proportions. The mRNA levels were measured relative to BmActin, and BmTubulin mRNAs. The samples contained pooled tissues from several individuals. Values represent means ± SD from three independent experiments. Data were analyzed by Kruskal–Wallis test followed by pairwise comparisons using Wilcoxon rank sum test. The significant differences are indicated by different letters ( p

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction

    2) Product Images from "ECM alterations in Fndc3a (Fibronectin Domain Containing Protein 3A) deficient zebrafish cause temporal fin development and regeneration defects"

    Article Title: ECM alterations in Fndc3a (Fibronectin Domain Containing Protein 3A) deficient zebrafish cause temporal fin development and regeneration defects

    Journal: Scientific Reports

    doi: 10.1038/s41598-019-50055-w

    Generation and phenotype of fndc3a wue1/wue1 zebrafish mutants. ( A ) The CRISPR/Cas9 system was used to target exon 13 in the zebrafish fndc3a gene coding for the third fibronectin type III domain (nucleotides marked in light blue indicate sgRNA target sequence and in red the region of mutated sequence). ( B ) fndc3a wue1/wue1 mutants showed straightened tail buds (22 hpf; n = 19/40), kinked tails (48 hpf; n = 27/100), and caudal fin deformations (120 hpf; n = 9/41) during the first days of embryonic development. ( C ) A fraction of adult fndc3a wue1/wue1 mutants displayed weak (n = 15/71) to strong (n = 6/71) caudal fin phenotypes and tail malformations. ( D ) qPCR quantification of relative fndc3a expression levels in genotypic different groups of embryos indicated reduction of fndc3a transcripts in fndc3a wue1/ + and fndc3a wue1/wue1 (ΔΔCt calculation; significance levels of a 2-sided paired student t-test are given). Investigation of protein domains shown in A has been performed via the SMART database (Simple Modular Architecture Research Tool; http://smart.embl-heidelberg.de ) 69 . Black arrows indicate developmental malformations. Scale bars for whole embryos: 250 µm; scale bars for tail magnifications: 100 µm.
    Figure Legend Snippet: Generation and phenotype of fndc3a wue1/wue1 zebrafish mutants. ( A ) The CRISPR/Cas9 system was used to target exon 13 in the zebrafish fndc3a gene coding for the third fibronectin type III domain (nucleotides marked in light blue indicate sgRNA target sequence and in red the region of mutated sequence). ( B ) fndc3a wue1/wue1 mutants showed straightened tail buds (22 hpf; n = 19/40), kinked tails (48 hpf; n = 27/100), and caudal fin deformations (120 hpf; n = 9/41) during the first days of embryonic development. ( C ) A fraction of adult fndc3a wue1/wue1 mutants displayed weak (n = 15/71) to strong (n = 6/71) caudal fin phenotypes and tail malformations. ( D ) qPCR quantification of relative fndc3a expression levels in genotypic different groups of embryos indicated reduction of fndc3a transcripts in fndc3a wue1/ + and fndc3a wue1/wue1 (ΔΔCt calculation; significance levels of a 2-sided paired student t-test are given). Investigation of protein domains shown in A has been performed via the SMART database (Simple Modular Architecture Research Tool; http://smart.embl-heidelberg.de ) 69 . Black arrows indicate developmental malformations. Scale bars for whole embryos: 250 µm; scale bars for tail magnifications: 100 µm.

    Techniques Used: CRISPR, Sequencing, Real-time Polymerase Chain Reaction, Expressing

    Correct ECM structure in the median fin fold and regenerating caudal fins is hampered in fndc3a wue1/wue1 mutants. ( A,B ) F-actin in the median fin fold was visualized by phalloidin staining and localization of β-catenin by immunofluorescence (n = 6 for each group, 22–24 hpf). Cellular organization of ventral median fin fold cells and ECM matrix was symmetrically structured in control embryos and showed nuclear localization of active Wnt signals in apical cells (white arrowheads in B). fndc3a wue1/wue1 mutants depicted cellular alterations and unstructured ECM assembly by showing irregular cell shapes (arrows in A ), cavities within the fin fold (dashed lines in A ) and speckled accumulation of β-catenin between cells (arrows in B ). Nuclear localization of β-catenin in apical cells was maintained (arrowheads in B ). ( C,D ) Fin regenerates of fndc3a wue1/wue1 mutants stained for F-actin showed regenerate abnormalities (arrows in C ), irregular regenerate borders (dashed lines in C ) and cellular cavities (dashed lines in D ; n = 4 for each group). ( E , F ) Fin regenerates of fndc3a wue1/wue1 mutants stained for β-catenin depicted divergent ECM assembly (arrows in E ), appearance of abnormal cells loosely attached to the regenerate (arrows in F ) and cavities (dashed lines in F ; n = 3 for each group). Images either show maximum intensity projections (30 to 40 single z-slices; z-distance: 1.5 µm) or a representative higher resolution single z slice.
    Figure Legend Snippet: Correct ECM structure in the median fin fold and regenerating caudal fins is hampered in fndc3a wue1/wue1 mutants. ( A,B ) F-actin in the median fin fold was visualized by phalloidin staining and localization of β-catenin by immunofluorescence (n = 6 for each group, 22–24 hpf). Cellular organization of ventral median fin fold cells and ECM matrix was symmetrically structured in control embryos and showed nuclear localization of active Wnt signals in apical cells (white arrowheads in B). fndc3a wue1/wue1 mutants depicted cellular alterations and unstructured ECM assembly by showing irregular cell shapes (arrows in A ), cavities within the fin fold (dashed lines in A ) and speckled accumulation of β-catenin between cells (arrows in B ). Nuclear localization of β-catenin in apical cells was maintained (arrowheads in B ). ( C,D ) Fin regenerates of fndc3a wue1/wue1 mutants stained for F-actin showed regenerate abnormalities (arrows in C ), irregular regenerate borders (dashed lines in C ) and cellular cavities (dashed lines in D ; n = 4 for each group). ( E , F ) Fin regenerates of fndc3a wue1/wue1 mutants stained for β-catenin depicted divergent ECM assembly (arrows in E ), appearance of abnormal cells loosely attached to the regenerate (arrows in F ) and cavities (dashed lines in F ; n = 3 for each group). Images either show maximum intensity projections (30 to 40 single z-slices; z-distance: 1.5 µm) or a representative higher resolution single z slice.

    Techniques Used: Staining, Immunofluorescence

    3) Product Images from "Optimization of an O2-balanced bioartificial pancreas for type 1 diabetes using statistical design of experiment"

    Article Title: Optimization of an O2-balanced bioartificial pancreas for type 1 diabetes using statistical design of experiment

    Journal: Scientific Reports

    doi: 10.1038/s41598-022-07887-w

    Hypoxic signature of neonate pig islets (NPIs) in O 2  balanced BAPs. Alginate encapsulated NPIs (3000 IEQ/150 µL) were cultured for 3, 8, and 15 days under 20% O 2  (20% O 2 , positive control, white bar) or 1% O 2  condition without O 2  strategy (1% O 2,  negative control, black bar) or with the innovative strategy of oxygenation (ISO) composed of silicone-CaO 2  disk and 500 µg/mL HEMOXCell by alginate (1% O 2  + ISO, grey bars). Fold change in VEGF secretion by total metabolic activity (AU/RLU) of encapsulated NPIs compared to the control cultured for 3 days under 20% O 2  without O 2  strategy. ( B ) Relative quantitative RT-PCR expression analysis of Heme oxygenase (HO-1) of decapsulated NPIs cultured for 15 days within BAPs (n = 4–7). Results from independent experiments (n = 4–7) are expressed  as mean ± SEM. *p 
    Figure Legend Snippet: Hypoxic signature of neonate pig islets (NPIs) in O 2 balanced BAPs. Alginate encapsulated NPIs (3000 IEQ/150 µL) were cultured for 3, 8, and 15 days under 20% O 2 (20% O 2 , positive control, white bar) or 1% O 2 condition without O 2 strategy (1% O 2, negative control, black bar) or with the innovative strategy of oxygenation (ISO) composed of silicone-CaO 2 disk and 500 µg/mL HEMOXCell by alginate (1% O 2  + ISO, grey bars). Fold change in VEGF secretion by total metabolic activity (AU/RLU) of encapsulated NPIs compared to the control cultured for 3 days under 20% O 2 without O 2 strategy. ( B ) Relative quantitative RT-PCR expression analysis of Heme oxygenase (HO-1) of decapsulated NPIs cultured for 15 days within BAPs (n = 4–7). Results from independent experiments (n = 4–7) are expressed as mean ± SEM. *p 

    Techniques Used: Cell Culture, Positive Control, Negative Control, Activity Assay, Quantitative RT-PCR, Expressing

    Effect of O 2  strategy on the maturation of neonate pig islets (NPIs) embarked in O 2  balanced BAPs. The analyses were performed on pre-encapsulated NPIs 24 h after isolation (day 1) and on encapsulated NPIs cultured for 8 or 15 days within BAPs in 20% O 2  (positive control) and 1% O 2  conditions without the O 2  strategy (1% O 2 , negative control) or with the O 2  strategy composed of silicone-CaO 2  disk and 500 µg/mL HEMOXCell by alginate (1% O 2  + ISO) (n = 4–7 pigs). ( A ) Immunostaining of insulin ß cells (green, Alexa-Fluor 488) and glucagon α cells (red, Alexa-Fluor 555) staining of NPIs in 4 µm thick cross-sections. Views in white light are shown to the lower-left of each photo. The scale is indicated in each picture. ( B ) Percentage of mean insulin-positive area per islet (Insulin) and percentage of mean glucagon-positive area per islet (Glucagon). The percentages of insulin and glucagon were quantified within 150 islets in day 1 (n = 4 pigs) and an average of 30 islets per condition after day 8 of culture (n = 3 pigs). ( C ) Intracellular insulin by ATP content ratio. ( D ) Relative quantitative RT-PCR expression analysis of insulin ( INS ), glucagon ( GCG ), pancreatic progenitor transcription factor ( PDX1 ) and NKX6.1 ( NKX6.1 ). *p 
    Figure Legend Snippet: Effect of O 2 strategy on the maturation of neonate pig islets (NPIs) embarked in O 2 balanced BAPs. The analyses were performed on pre-encapsulated NPIs 24 h after isolation (day 1) and on encapsulated NPIs cultured for 8 or 15 days within BAPs in 20% O 2 (positive control) and 1% O 2 conditions without the O 2 strategy (1% O 2 , negative control) or with the O 2 strategy composed of silicone-CaO 2 disk and 500 µg/mL HEMOXCell by alginate (1% O 2  + ISO) (n = 4–7 pigs). ( A ) Immunostaining of insulin ß cells (green, Alexa-Fluor 488) and glucagon α cells (red, Alexa-Fluor 555) staining of NPIs in 4 µm thick cross-sections. Views in white light are shown to the lower-left of each photo. The scale is indicated in each picture. ( B ) Percentage of mean insulin-positive area per islet (Insulin) and percentage of mean glucagon-positive area per islet (Glucagon). The percentages of insulin and glucagon were quantified within 150 islets in day 1 (n = 4 pigs) and an average of 30 islets per condition after day 8 of culture (n = 3 pigs). ( C ) Intracellular insulin by ATP content ratio. ( D ) Relative quantitative RT-PCR expression analysis of insulin ( INS ), glucagon ( GCG ), pancreatic progenitor transcription factor ( PDX1 ) and NKX6.1 ( NKX6.1 ). *p 

    Techniques Used: Isolation, Cell Culture, Positive Control, Negative Control, Immunostaining, Staining, Quantitative RT-PCR, Expressing

    4) Product Images from "Stem Cell Modeling of Neuroferritinopathy Reveals Iron as a Determinant of Senescence and Ferroptosis during Neuronal Aging"

    Article Title: Stem Cell Modeling of Neuroferritinopathy Reveals Iron as a Determinant of Senescence and Ferroptosis during Neuronal Aging

    Journal: Stem Cell Reports

    doi: 10.1016/j.stemcr.2019.09.002

    Iron-Dependent Senescence Phenotype Involves an NCOA4 Decrease and p53 Activation (A–C) Immunoblotting of NCOA4 expression in soluble fibroblast homogenates, untreated (A), treated with iron (B), or leupeptin (C). The results are presented as the mean ± SD of three independent experiments. (D) NCOA4 mRNA levels of fibroblasts determined by qRT-PCR and normalized to the mRNA expression of GAPDH. The data are presented as the mean ± SD of three independent experiments. (E) Immunoblotting of NCOA4 expression in soluble NPC homogenates, ∗ unspecific band. The results are presented as the mean ± SD of three independent experiments. (F) Immunofluorescence of p53 and NCOA4 in NPCs. The results are presented as the mean ± SD of three independent experiments. Scale bars, 20 μm. (G and H) Immunoblotting of NCOA4 expression (G) and H2A.X (H) in neuron soluble homogenates, ∗ unspecific band. (I) qRT-PCR analysis of SLC7A11 expression. The data are presented as the mean ± SD values of three independent experiments. The data were analyzed by unpaired, two-tailed t test, ∗∗ p
    Figure Legend Snippet: Iron-Dependent Senescence Phenotype Involves an NCOA4 Decrease and p53 Activation (A–C) Immunoblotting of NCOA4 expression in soluble fibroblast homogenates, untreated (A), treated with iron (B), or leupeptin (C). The results are presented as the mean ± SD of three independent experiments. (D) NCOA4 mRNA levels of fibroblasts determined by qRT-PCR and normalized to the mRNA expression of GAPDH. The data are presented as the mean ± SD of three independent experiments. (E) Immunoblotting of NCOA4 expression in soluble NPC homogenates, ∗ unspecific band. The results are presented as the mean ± SD of three independent experiments. (F) Immunofluorescence of p53 and NCOA4 in NPCs. The results are presented as the mean ± SD of three independent experiments. Scale bars, 20 μm. (G and H) Immunoblotting of NCOA4 expression (G) and H2A.X (H) in neuron soluble homogenates, ∗ unspecific band. (I) qRT-PCR analysis of SLC7A11 expression. The data are presented as the mean ± SD values of three independent experiments. The data were analyzed by unpaired, two-tailed t test, ∗∗ p

    Techniques Used: Activation Assay, Expressing, Quantitative RT-PCR, Immunofluorescence, Two Tailed Test

    Scheme of the Proposed Molecular Mechanism Stimulated by Iron in NF and Aging The insertion of the variant L-ferritin peptide into the protein shell causes the enhancement of redox-active iron in the cytosol, inducing iron-dependent ferritin translation that generates the overproduction of protein, facilitating its aggregation. Furthermore, an iron-dependent decrease in NCOA4 occurs that abolishes the physiological degradation of ferritin by the lysosome, further increasing ferritin/iron aggregation. The augmentation of ROS promotes cell oxidative injury with consequent DNA damage and protein and lipid oxidation. DNA instability is also enhanced by the diminished level of NCOA4. The cells seem to respond by triggering a p53-dependent pathway that further promotes senescence. However, the endless ROS-induced lipid peroxidation leads to death by ferroptosis. Although over a much longer time course, this mechanism might also occur physiologically during aging due to the ferritin/iron accumulation mainly in non-dividing cells.
    Figure Legend Snippet: Scheme of the Proposed Molecular Mechanism Stimulated by Iron in NF and Aging The insertion of the variant L-ferritin peptide into the protein shell causes the enhancement of redox-active iron in the cytosol, inducing iron-dependent ferritin translation that generates the overproduction of protein, facilitating its aggregation. Furthermore, an iron-dependent decrease in NCOA4 occurs that abolishes the physiological degradation of ferritin by the lysosome, further increasing ferritin/iron aggregation. The augmentation of ROS promotes cell oxidative injury with consequent DNA damage and protein and lipid oxidation. DNA instability is also enhanced by the diminished level of NCOA4. The cells seem to respond by triggering a p53-dependent pathway that further promotes senescence. However, the endless ROS-induced lipid peroxidation leads to death by ferroptosis. Although over a much longer time course, this mechanism might also occur physiologically during aging due to the ferritin/iron accumulation mainly in non-dividing cells.

    Techniques Used: Variant Assay

    Iron-Induced Senescence in NF Fibroblasts (A and B) (A) Cells morphology (upper panel) and SA-β-Gal activity (lower panel) in bright field. Scale bars, 20 μm. (B) SA-β-Gal activity of NF1 cells treated with iron (Fe) and NAC. Scale bars, 20 μm. Positive stained cells in (A) and (B) were counted and plotted as a percentage of the total cells. The results are presented as the mean ± SD of five fields in three independent experiments. (C) Ultrastructural analysis of fibroblasts examined by EM evidencing vacuoles (white arrows) and mitochondria (black arrows). (D) Immunoblotting of LC3I and II expression in soluble fibroblast homogenates. Results are presented as the mean ± SD of three independent experiments. (E) Levels of IL-1β and IL-6 determined by ELISAs on cell media. The results are presented as the mean ± SD of three independent experiments in octuplicate. The data were analyzed by unpaired, two-tailed t test, except for (B) in which one-way ANOVA were used, ∗ p
    Figure Legend Snippet: Iron-Induced Senescence in NF Fibroblasts (A and B) (A) Cells morphology (upper panel) and SA-β-Gal activity (lower panel) in bright field. Scale bars, 20 μm. (B) SA-β-Gal activity of NF1 cells treated with iron (Fe) and NAC. Scale bars, 20 μm. Positive stained cells in (A) and (B) were counted and plotted as a percentage of the total cells. The results are presented as the mean ± SD of five fields in three independent experiments. (C) Ultrastructural analysis of fibroblasts examined by EM evidencing vacuoles (white arrows) and mitochondria (black arrows). (D) Immunoblotting of LC3I and II expression in soluble fibroblast homogenates. Results are presented as the mean ± SD of three independent experiments. (E) Levels of IL-1β and IL-6 determined by ELISAs on cell media. The results are presented as the mean ± SD of three independent experiments in octuplicate. The data were analyzed by unpaired, two-tailed t test, except for (B) in which one-way ANOVA were used, ∗ p

    Techniques Used: Activity Assay, Staining, Expressing, Two Tailed Test

    Representative Images of NF Fibroblasts and iPSC-Derived Neurons Showed Formation of Ferritin/Iron Aggregates (A) Control and variant fibroblasts untreated (UT) or treated (Fe) with 100 μM FeAC for 14 days and stained with an anti-human H-ferritin antibody (Hoechst staining to detect the nuclei). The arrows show the ferritin aggregates. Scale bars, 20 μm. (B) Ultrastructural analysis of fibroblasts examined under an electron microscope (EM). The arrows indicate the aggregates. Cells untreated (UT) or treated (Fe) as described in (A) were subjected to an ESI analysis. The images showing the ultrastructural organization observed at 250 eV with a superimposed iron map represented by pseudo-colors. The iron granules were counted and are represented as a ratio to the total number in the counted fields (means ± SD of three independent experiments). The data were analyzed by unpaired, two-tailed t test, ∗∗∗ p
    Figure Legend Snippet: Representative Images of NF Fibroblasts and iPSC-Derived Neurons Showed Formation of Ferritin/Iron Aggregates (A) Control and variant fibroblasts untreated (UT) or treated (Fe) with 100 μM FeAC for 14 days and stained with an anti-human H-ferritin antibody (Hoechst staining to detect the nuclei). The arrows show the ferritin aggregates. Scale bars, 20 μm. (B) Ultrastructural analysis of fibroblasts examined under an electron microscope (EM). The arrows indicate the aggregates. Cells untreated (UT) or treated (Fe) as described in (A) were subjected to an ESI analysis. The images showing the ultrastructural organization observed at 250 eV with a superimposed iron map represented by pseudo-colors. The iron granules were counted and are represented as a ratio to the total number in the counted fields (means ± SD of three independent experiments). The data were analyzed by unpaired, two-tailed t test, ∗∗∗ p

    Techniques Used: Derivative Assay, Variant Assay, Staining, Microscopy, Two Tailed Test

    5) Product Images from "DUX4 regulates oocyte to embryo transition in human"

    Article Title: DUX4 regulates oocyte to embryo transition in human

    Journal: bioRxiv

    doi: 10.1101/732289

    Induction of DUX4 in the DUX4 TetOn hESCs leads to expression of intergenic genome. (a) The DUX4-ires-EmGFP piggyBac vector used to establish the doxicycline inducible DUX4 TetOn hESCs in H1 (clones 2 and 8) and H9 (clones 3 and 4). (b) DUX4 TetOn hESC clones (as above) +/- 1 μg/ml doxicycline for 3 h and live imaged for EmGFP. (c) mRNA expression kinetics of DUX4, ZSCAN4, and TRIM48 after 1 h, 2 h, and 3 h doxicycline induction measured using qRT-PCR. The data for the DUX4 TetOn H1 clone 2 is shown. Similar expression patterns were also found for the H1 clone 8, and H9 clones 3 and 4. (d) DUX4 TetOn hESCs treated with 1 μg/ml doxicycline for 4 h, fixed, and immunostained for DUX4. Representative images for nuclear DUX4 staining are shown for the H1 clone 2. Similar staining pattern were seen for the H1 clone 8 and H9 clones 3 and 4. Scale bar 50 μm. (e) Enrichment analysis of the DUX4-induced TFEs with 816 publicly available ChIP-seq datasets. A total of 7,216 ChIP-seq data for transcription factors are shown. ChIP-seq data for DUX4 are shown in red. Dots on the left side of the dashed line are underrepresented, whereas dots on the right side are overrepresented. (f) ATAC-seq intensity of human early embryo around the gained, non-significant (NS), and lost ATAC-seq peaks after DUX4 induction which overlap with ERVL-MaLR elements.
    Figure Legend Snippet: Induction of DUX4 in the DUX4 TetOn hESCs leads to expression of intergenic genome. (a) The DUX4-ires-EmGFP piggyBac vector used to establish the doxicycline inducible DUX4 TetOn hESCs in H1 (clones 2 and 8) and H9 (clones 3 and 4). (b) DUX4 TetOn hESC clones (as above) +/- 1 μg/ml doxicycline for 3 h and live imaged for EmGFP. (c) mRNA expression kinetics of DUX4, ZSCAN4, and TRIM48 after 1 h, 2 h, and 3 h doxicycline induction measured using qRT-PCR. The data for the DUX4 TetOn H1 clone 2 is shown. Similar expression patterns were also found for the H1 clone 8, and H9 clones 3 and 4. (d) DUX4 TetOn hESCs treated with 1 μg/ml doxicycline for 4 h, fixed, and immunostained for DUX4. Representative images for nuclear DUX4 staining are shown for the H1 clone 2. Similar staining pattern were seen for the H1 clone 8 and H9 clones 3 and 4. Scale bar 50 μm. (e) Enrichment analysis of the DUX4-induced TFEs with 816 publicly available ChIP-seq datasets. A total of 7,216 ChIP-seq data for transcription factors are shown. ChIP-seq data for DUX4 are shown in red. Dots on the left side of the dashed line are underrepresented, whereas dots on the right side are overrepresented. (f) ATAC-seq intensity of human early embryo around the gained, non-significant (NS), and lost ATAC-seq peaks after DUX4 induction which overlap with ERVL-MaLR elements.

    Techniques Used: Expressing, Plasmid Preparation, Clone Assay, Quantitative RT-PCR, Staining, Chromatin Immunoprecipitation

    6) Product Images from "Fndc3a (Fibronectin Domain Containing Protein 3A) influences median fin fold development and caudal fin regeneration in zebrafish by ECM alteration"

    Article Title: Fndc3a (Fibronectin Domain Containing Protein 3A) influences median fin fold development and caudal fin regeneration in zebrafish by ECM alteration

    Journal: bioRxiv

    doi: 10.1101/386813

    Correct ECM structure in the median fin fold and regenerating caudal fins is hampered in fndc3a wue1/wue1 mutants. (A) F-actin in the median fin fold 22hpf was visualized by phalloidin staining, (B) localization of β-catenin during fin development was visualized by immunofluorescence of 24hpf embryos (n=6 for each group). Both colorations mark cell membranes and ECM structures. Cellular organization of ventral median fin fold cells and ECM matrix is symmetrically structured in control embryos and shows nuclear localization of active Wnt signals in cells at the fin fold tip (white arrowheads in B). fndc3a wue1/wue1 mutants depict cellular alterations and unstructured ECM assembly by showing irregular cell shapes (white arrows in A), cavities within the fin fold (white arrowheads in A2) and speckled accumulation of β-catenin between cells (white arrows in B). Nuclear localization of β-catenin in cells at the fin fold tip was maintained (grey arrowheads in B). (C and D; n=4 for each group) Fin regenerates of fndc3a wue1/wue1 mutants incubated at 32°C and stained for F-actin showed regenerate abnormalities (white arrows in C), irregular regenerate borders (white dashed lines in C) and cellular cavities (white arrowheads in D) (E and F; n=3 for each group) Fin regenerates of fndc3a wue1/wue1 mutants also depicted intracellular accumulation of β-catenin, divergent ECM assembly (white arrows) in addition to appearance of abnormal cells loosely attached to the regenerate (white arrowheads). Images either show maximum intensity projections (30 to 40 single z-slices; z-distance: 1.5µm) or a representative higher resolution single z slice.
    Figure Legend Snippet: Correct ECM structure in the median fin fold and regenerating caudal fins is hampered in fndc3a wue1/wue1 mutants. (A) F-actin in the median fin fold 22hpf was visualized by phalloidin staining, (B) localization of β-catenin during fin development was visualized by immunofluorescence of 24hpf embryos (n=6 for each group). Both colorations mark cell membranes and ECM structures. Cellular organization of ventral median fin fold cells and ECM matrix is symmetrically structured in control embryos and shows nuclear localization of active Wnt signals in cells at the fin fold tip (white arrowheads in B). fndc3a wue1/wue1 mutants depict cellular alterations and unstructured ECM assembly by showing irregular cell shapes (white arrows in A), cavities within the fin fold (white arrowheads in A2) and speckled accumulation of β-catenin between cells (white arrows in B). Nuclear localization of β-catenin in cells at the fin fold tip was maintained (grey arrowheads in B). (C and D; n=4 for each group) Fin regenerates of fndc3a wue1/wue1 mutants incubated at 32°C and stained for F-actin showed regenerate abnormalities (white arrows in C), irregular regenerate borders (white dashed lines in C) and cellular cavities (white arrowheads in D) (E and F; n=3 for each group) Fin regenerates of fndc3a wue1/wue1 mutants also depicted intracellular accumulation of β-catenin, divergent ECM assembly (white arrows) in addition to appearance of abnormal cells loosely attached to the regenerate (white arrowheads). Images either show maximum intensity projections (30 to 40 single z-slices; z-distance: 1.5µm) or a representative higher resolution single z slice.

    Techniques Used: Staining, Immunofluorescence, Incubation

    Generation and phenotype of fndc3a wue1,wue1 zebrafish mutants. (A) The CRISPR/Cas9 system was used to target exon 13 in the zebrafish fndc3a gene coding for the third fibronectin type III domain (nucleotides marked in blue indicate sgRNA target sequence; nucleotides marked in red indicate the region of mutated sequence). (B-D) fndc3a wue1/wue1 mutants show straightened tail buds (n=19/40), kinked tails (n= 27/100), and actinotrichia fiber aggregation during the first days of embryonic development (n= 9/41; indicated by arrows). (E) A fraction of adult fndc3a wue1/wue1 mutants display weak (n= 15/71) to strong (n= 6/71) caudal fin phenotypes and tail malformations. (F) qPCR quantification of relative fndc3a expression levels in genotypic different groups of embryos indicated reduction of fndc3a transcripts in fndc3a wue1/+ and fndc3a Nue1/Nue1 (ΔΔCt calculation; comparison of biological triplicates for each genotype with twelve 24hpf embryos each; two independent fndc3a primer pairs; normalized against AB controls; gapdh and ef1a1l1 expression were used as endogenous/housekeeping controls; significance levels and p-values of a 2-sided paired student t-test are given). Scale bars for embryo overview: 250pm; scale bars for tail magnifications: 100µm.
    Figure Legend Snippet: Generation and phenotype of fndc3a wue1,wue1 zebrafish mutants. (A) The CRISPR/Cas9 system was used to target exon 13 in the zebrafish fndc3a gene coding for the third fibronectin type III domain (nucleotides marked in blue indicate sgRNA target sequence; nucleotides marked in red indicate the region of mutated sequence). (B-D) fndc3a wue1/wue1 mutants show straightened tail buds (n=19/40), kinked tails (n= 27/100), and actinotrichia fiber aggregation during the first days of embryonic development (n= 9/41; indicated by arrows). (E) A fraction of adult fndc3a wue1/wue1 mutants display weak (n= 15/71) to strong (n= 6/71) caudal fin phenotypes and tail malformations. (F) qPCR quantification of relative fndc3a expression levels in genotypic different groups of embryos indicated reduction of fndc3a transcripts in fndc3a wue1/+ and fndc3a Nue1/Nue1 (ΔΔCt calculation; comparison of biological triplicates for each genotype with twelve 24hpf embryos each; two independent fndc3a primer pairs; normalized against AB controls; gapdh and ef1a1l1 expression were used as endogenous/housekeeping controls; significance levels and p-values of a 2-sided paired student t-test are given). Scale bars for embryo overview: 250pm; scale bars for tail magnifications: 100µm.

    Techniques Used: CRISPR, Sequencing, Real-time Polymerase Chain Reaction, Expressing

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    Solis BioDyne real time rt pcr qpcr
    AKH and AKHR isoforms differ in the tissue specificity of their expression. <t>RT-PCR</t> analysis of AKH and AKHR mRNAs was performed using tissues from larvae ( a ) as well as adult moths ( b ). The adult RNA samples other than testes and ovary contained male and female tissues in equal proportions. The mRNA levels were measured relative to BmActin, and BmTubulin mRNAs. The samples contained pooled tissues from several individuals. Values represent means ± SD from three independent experiments. Data were analyzed by Kruskal–Wallis test followed by pairwise comparisons using Wilcoxon rank sum test. The significant differences are indicated by different letters ( p
    Real Time Rt Pcr Qpcr, supplied by Solis BioDyne, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    real time rt pcr qpcr - by Bioz Stars, 2022-05
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    92
    Solis BioDyne hot firepol multiplex mix ready
    Sensitivity of the newly described <t>multiplex</t> PCR method compared to the corresponding simplex PCR for each of the targeted bacterial taxon. Every reaction was performed with six samples of corresponding control bacteria at different concentrations. Lane 1: 1 ng/μl, lane 2: 0.5 ng/μl, lane 3: 0.1 ng/μl, lane 4: 0.05 ng/μl and lane 5: 0.01ng/μl, lane 6: water control. a-b: P . fuscovaginae strain UBP735, c-d: B . glumae strain NCPPB 3923, e-f: Sphingomonas strain V1-2, g-h: X . oryzae pv. oryzae strain BAI10, i-j: Pantoea strain ARC10. a, c, e, g, i: simplex PCR with only one primer pair in each case. b, d, f, h, j: multiplex PCR including the five primer pairs.
    Hot Firepol Multiplex Mix Ready, supplied by Solis BioDyne, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hot firepol multiplex mix ready/product/Solis BioDyne
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hot firepol multiplex mix ready - by Bioz Stars, 2022-05
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    AKH and AKHR isoforms differ in the tissue specificity of their expression. RT-PCR analysis of AKH and AKHR mRNAs was performed using tissues from larvae ( a ) as well as adult moths ( b ). The adult RNA samples other than testes and ovary contained male and female tissues in equal proportions. The mRNA levels were measured relative to BmActin, and BmTubulin mRNAs. The samples contained pooled tissues from several individuals. Values represent means ± SD from three independent experiments. Data were analyzed by Kruskal–Wallis test followed by pairwise comparisons using Wilcoxon rank sum test. The significant differences are indicated by different letters ( p

    Journal: Cells

    Article Title: Functional Analysis of Adipokinetic Hormone Signaling in Bombyx mori

    doi: 10.3390/cells9122667

    Figure Lengend Snippet: AKH and AKHR isoforms differ in the tissue specificity of their expression. RT-PCR analysis of AKH and AKHR mRNAs was performed using tissues from larvae ( a ) as well as adult moths ( b ). The adult RNA samples other than testes and ovary contained male and female tissues in equal proportions. The mRNA levels were measured relative to BmActin, and BmTubulin mRNAs. The samples contained pooled tissues from several individuals. Values represent means ± SD from three independent experiments. Data were analyzed by Kruskal–Wallis test followed by pairwise comparisons using Wilcoxon rank sum test. The significant differences are indicated by different letters ( p

    Article Snippet: Relative gene expression was quantified by real-time-RT-PCR (qPCR) using HOT FIREPol EvaGreen qPCR Mix Plus (ROX, Solis BioDyne, Tartu, Estonia).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction

    Generation and phenotype of fndc3a wue1/wue1 zebrafish mutants. ( A ) The CRISPR/Cas9 system was used to target exon 13 in the zebrafish fndc3a gene coding for the third fibronectin type III domain (nucleotides marked in light blue indicate sgRNA target sequence and in red the region of mutated sequence). ( B ) fndc3a wue1/wue1 mutants showed straightened tail buds (22 hpf; n = 19/40), kinked tails (48 hpf; n = 27/100), and caudal fin deformations (120 hpf; n = 9/41) during the first days of embryonic development. ( C ) A fraction of adult fndc3a wue1/wue1 mutants displayed weak (n = 15/71) to strong (n = 6/71) caudal fin phenotypes and tail malformations. ( D ) qPCR quantification of relative fndc3a expression levels in genotypic different groups of embryos indicated reduction of fndc3a transcripts in fndc3a wue1/ + and fndc3a wue1/wue1 (ΔΔCt calculation; significance levels of a 2-sided paired student t-test are given). Investigation of protein domains shown in A has been performed via the SMART database (Simple Modular Architecture Research Tool; http://smart.embl-heidelberg.de ) 69 . Black arrows indicate developmental malformations. Scale bars for whole embryos: 250 µm; scale bars for tail magnifications: 100 µm.

    Journal: Scientific Reports

    Article Title: ECM alterations in Fndc3a (Fibronectin Domain Containing Protein 3A) deficient zebrafish cause temporal fin development and regeneration defects

    doi: 10.1038/s41598-019-50055-w

    Figure Lengend Snippet: Generation and phenotype of fndc3a wue1/wue1 zebrafish mutants. ( A ) The CRISPR/Cas9 system was used to target exon 13 in the zebrafish fndc3a gene coding for the third fibronectin type III domain (nucleotides marked in light blue indicate sgRNA target sequence and in red the region of mutated sequence). ( B ) fndc3a wue1/wue1 mutants showed straightened tail buds (22 hpf; n = 19/40), kinked tails (48 hpf; n = 27/100), and caudal fin deformations (120 hpf; n = 9/41) during the first days of embryonic development. ( C ) A fraction of adult fndc3a wue1/wue1 mutants displayed weak (n = 15/71) to strong (n = 6/71) caudal fin phenotypes and tail malformations. ( D ) qPCR quantification of relative fndc3a expression levels in genotypic different groups of embryos indicated reduction of fndc3a transcripts in fndc3a wue1/ + and fndc3a wue1/wue1 (ΔΔCt calculation; significance levels of a 2-sided paired student t-test are given). Investigation of protein domains shown in A has been performed via the SMART database (Simple Modular Architecture Research Tool; http://smart.embl-heidelberg.de ) 69 . Black arrows indicate developmental malformations. Scale bars for whole embryos: 250 µm; scale bars for tail magnifications: 100 µm.

    Article Snippet: Each group and primer sample was analyzed in triplicates on a single qPCR plate utilizing HOT FIREPol Eva Green Mix Plus (Solis BioDyne).

    Techniques: CRISPR, Sequencing, Real-time Polymerase Chain Reaction, Expressing

    Correct ECM structure in the median fin fold and regenerating caudal fins is hampered in fndc3a wue1/wue1 mutants. ( A,B ) F-actin in the median fin fold was visualized by phalloidin staining and localization of β-catenin by immunofluorescence (n = 6 for each group, 22–24 hpf). Cellular organization of ventral median fin fold cells and ECM matrix was symmetrically structured in control embryos and showed nuclear localization of active Wnt signals in apical cells (white arrowheads in B). fndc3a wue1/wue1 mutants depicted cellular alterations and unstructured ECM assembly by showing irregular cell shapes (arrows in A ), cavities within the fin fold (dashed lines in A ) and speckled accumulation of β-catenin between cells (arrows in B ). Nuclear localization of β-catenin in apical cells was maintained (arrowheads in B ). ( C,D ) Fin regenerates of fndc3a wue1/wue1 mutants stained for F-actin showed regenerate abnormalities (arrows in C ), irregular regenerate borders (dashed lines in C ) and cellular cavities (dashed lines in D ; n = 4 for each group). ( E , F ) Fin regenerates of fndc3a wue1/wue1 mutants stained for β-catenin depicted divergent ECM assembly (arrows in E ), appearance of abnormal cells loosely attached to the regenerate (arrows in F ) and cavities (dashed lines in F ; n = 3 for each group). Images either show maximum intensity projections (30 to 40 single z-slices; z-distance: 1.5 µm) or a representative higher resolution single z slice.

    Journal: Scientific Reports

    Article Title: ECM alterations in Fndc3a (Fibronectin Domain Containing Protein 3A) deficient zebrafish cause temporal fin development and regeneration defects

    doi: 10.1038/s41598-019-50055-w

    Figure Lengend Snippet: Correct ECM structure in the median fin fold and regenerating caudal fins is hampered in fndc3a wue1/wue1 mutants. ( A,B ) F-actin in the median fin fold was visualized by phalloidin staining and localization of β-catenin by immunofluorescence (n = 6 for each group, 22–24 hpf). Cellular organization of ventral median fin fold cells and ECM matrix was symmetrically structured in control embryos and showed nuclear localization of active Wnt signals in apical cells (white arrowheads in B). fndc3a wue1/wue1 mutants depicted cellular alterations and unstructured ECM assembly by showing irregular cell shapes (arrows in A ), cavities within the fin fold (dashed lines in A ) and speckled accumulation of β-catenin between cells (arrows in B ). Nuclear localization of β-catenin in apical cells was maintained (arrowheads in B ). ( C,D ) Fin regenerates of fndc3a wue1/wue1 mutants stained for F-actin showed regenerate abnormalities (arrows in C ), irregular regenerate borders (dashed lines in C ) and cellular cavities (dashed lines in D ; n = 4 for each group). ( E , F ) Fin regenerates of fndc3a wue1/wue1 mutants stained for β-catenin depicted divergent ECM assembly (arrows in E ), appearance of abnormal cells loosely attached to the regenerate (arrows in F ) and cavities (dashed lines in F ; n = 3 for each group). Images either show maximum intensity projections (30 to 40 single z-slices; z-distance: 1.5 µm) or a representative higher resolution single z slice.

    Article Snippet: Each group and primer sample was analyzed in triplicates on a single qPCR plate utilizing HOT FIREPol Eva Green Mix Plus (Solis BioDyne).

    Techniques: Staining, Immunofluorescence

    Hypoxic signature of neonate pig islets (NPIs) in O 2  balanced BAPs. Alginate encapsulated NPIs (3000 IEQ/150 µL) were cultured for 3, 8, and 15 days under 20% O 2  (20% O 2 , positive control, white bar) or 1% O 2  condition without O 2  strategy (1% O 2,  negative control, black bar) or with the innovative strategy of oxygenation (ISO) composed of silicone-CaO 2  disk and 500 µg/mL HEMOXCell by alginate (1% O 2  + ISO, grey bars). Fold change in VEGF secretion by total metabolic activity (AU/RLU) of encapsulated NPIs compared to the control cultured for 3 days under 20% O 2  without O 2  strategy. ( B ) Relative quantitative RT-PCR expression analysis of Heme oxygenase (HO-1) of decapsulated NPIs cultured for 15 days within BAPs (n = 4–7). Results from independent experiments (n = 4–7) are expressed  as mean ± SEM. *p 

    Journal: Scientific Reports

    Article Title: Optimization of an O2-balanced bioartificial pancreas for type 1 diabetes using statistical design of experiment

    doi: 10.1038/s41598-022-07887-w

    Figure Lengend Snippet: Hypoxic signature of neonate pig islets (NPIs) in O 2 balanced BAPs. Alginate encapsulated NPIs (3000 IEQ/150 µL) were cultured for 3, 8, and 15 days under 20% O 2 (20% O 2 , positive control, white bar) or 1% O 2 condition without O 2 strategy (1% O 2, negative control, black bar) or with the innovative strategy of oxygenation (ISO) composed of silicone-CaO 2 disk and 500 µg/mL HEMOXCell by alginate (1% O 2  + ISO, grey bars). Fold change in VEGF secretion by total metabolic activity (AU/RLU) of encapsulated NPIs compared to the control cultured for 3 days under 20% O 2 without O 2 strategy. ( B ) Relative quantitative RT-PCR expression analysis of Heme oxygenase (HO-1) of decapsulated NPIs cultured for 15 days within BAPs (n = 4–7). Results from independent experiments (n = 4–7) are expressed as mean ± SEM. *p 

    Article Snippet: Real-time quantitative polymerase chain reaction (RT-qPCR) was performed on a CFX 96 Touch instrument (Bio-Rad, Hercules, CA, USA) using Hot FirePol qPCR reagents (Solis BioDyne, Tartu, Estonia).

    Techniques: Cell Culture, Positive Control, Negative Control, Activity Assay, Quantitative RT-PCR, Expressing

    Effect of O 2  strategy on the maturation of neonate pig islets (NPIs) embarked in O 2  balanced BAPs. The analyses were performed on pre-encapsulated NPIs 24 h after isolation (day 1) and on encapsulated NPIs cultured for 8 or 15 days within BAPs in 20% O 2  (positive control) and 1% O 2  conditions without the O 2  strategy (1% O 2 , negative control) or with the O 2  strategy composed of silicone-CaO 2  disk and 500 µg/mL HEMOXCell by alginate (1% O 2  + ISO) (n = 4–7 pigs). ( A ) Immunostaining of insulin ß cells (green, Alexa-Fluor 488) and glucagon α cells (red, Alexa-Fluor 555) staining of NPIs in 4 µm thick cross-sections. Views in white light are shown to the lower-left of each photo. The scale is indicated in each picture. ( B ) Percentage of mean insulin-positive area per islet (Insulin) and percentage of mean glucagon-positive area per islet (Glucagon). The percentages of insulin and glucagon were quantified within 150 islets in day 1 (n = 4 pigs) and an average of 30 islets per condition after day 8 of culture (n = 3 pigs). ( C ) Intracellular insulin by ATP content ratio. ( D ) Relative quantitative RT-PCR expression analysis of insulin ( INS ), glucagon ( GCG ), pancreatic progenitor transcription factor ( PDX1 ) and NKX6.1 ( NKX6.1 ). *p 

    Journal: Scientific Reports

    Article Title: Optimization of an O2-balanced bioartificial pancreas for type 1 diabetes using statistical design of experiment

    doi: 10.1038/s41598-022-07887-w

    Figure Lengend Snippet: Effect of O 2 strategy on the maturation of neonate pig islets (NPIs) embarked in O 2 balanced BAPs. The analyses were performed on pre-encapsulated NPIs 24 h after isolation (day 1) and on encapsulated NPIs cultured for 8 or 15 days within BAPs in 20% O 2 (positive control) and 1% O 2 conditions without the O 2 strategy (1% O 2 , negative control) or with the O 2 strategy composed of silicone-CaO 2 disk and 500 µg/mL HEMOXCell by alginate (1% O 2  + ISO) (n = 4–7 pigs). ( A ) Immunostaining of insulin ß cells (green, Alexa-Fluor 488) and glucagon α cells (red, Alexa-Fluor 555) staining of NPIs in 4 µm thick cross-sections. Views in white light are shown to the lower-left of each photo. The scale is indicated in each picture. ( B ) Percentage of mean insulin-positive area per islet (Insulin) and percentage of mean glucagon-positive area per islet (Glucagon). The percentages of insulin and glucagon were quantified within 150 islets in day 1 (n = 4 pigs) and an average of 30 islets per condition after day 8 of culture (n = 3 pigs). ( C ) Intracellular insulin by ATP content ratio. ( D ) Relative quantitative RT-PCR expression analysis of insulin ( INS ), glucagon ( GCG ), pancreatic progenitor transcription factor ( PDX1 ) and NKX6.1 ( NKX6.1 ). *p 

    Article Snippet: Real-time quantitative polymerase chain reaction (RT-qPCR) was performed on a CFX 96 Touch instrument (Bio-Rad, Hercules, CA, USA) using Hot FirePol qPCR reagents (Solis BioDyne, Tartu, Estonia).

    Techniques: Isolation, Cell Culture, Positive Control, Negative Control, Immunostaining, Staining, Quantitative RT-PCR, Expressing

    Sensitivity of the newly described multiplex PCR method compared to the corresponding simplex PCR for each of the targeted bacterial taxon. Every reaction was performed with six samples of corresponding control bacteria at different concentrations. Lane 1: 1 ng/μl, lane 2: 0.5 ng/μl, lane 3: 0.1 ng/μl, lane 4: 0.05 ng/μl and lane 5: 0.01ng/μl, lane 6: water control. a-b: P . fuscovaginae strain UBP735, c-d: B . glumae strain NCPPB 3923, e-f: Sphingomonas strain V1-2, g-h: X . oryzae pv. oryzae strain BAI10, i-j: Pantoea strain ARC10. a, c, e, g, i: simplex PCR with only one primer pair in each case. b, d, f, h, j: multiplex PCR including the five primer pairs.

    Journal: PLoS ONE

    Article Title: Design of a new multiplex PCR assay for rice pathogenic bacteria detection and its application to infer disease incidence and detect co-infection in rice fields in Burkina Faso

    doi: 10.1371/journal.pone.0232115

    Figure Lengend Snippet: Sensitivity of the newly described multiplex PCR method compared to the corresponding simplex PCR for each of the targeted bacterial taxon. Every reaction was performed with six samples of corresponding control bacteria at different concentrations. Lane 1: 1 ng/μl, lane 2: 0.5 ng/μl, lane 3: 0.1 ng/μl, lane 4: 0.05 ng/μl and lane 5: 0.01ng/μl, lane 6: water control. a-b: P . fuscovaginae strain UBP735, c-d: B . glumae strain NCPPB 3923, e-f: Sphingomonas strain V1-2, g-h: X . oryzae pv. oryzae strain BAI10, i-j: Pantoea strain ARC10. a, c, e, g, i: simplex PCR with only one primer pair in each case. b, d, f, h, j: multiplex PCR including the five primer pairs.

    Article Snippet: Following the optimization, the final conditions for the multiplex PCR protocol were: 2 μl of DNA added to 23 μl master mix comprising 5 μl Hot Firepol Multiplex Mix ready to load 5X (Solis BioDyne,Tartu, Estonia), 1.25 μl (NH4 )2 SO4 (160 mM), 0.2 μl of each primers specific of P . fuscovaginae at 5 μM, 0.2 μl of each primers specific of B . gluma e and B . gladioli at 100 μM, 0.3 μl of each primers specific of Pantoea spp. at 100 μM and 0.3 μl of each primers specific of X . oryzae at 10 μM and finally 0.1 μl of each primers specific of Sphingomonas spp. at 10 μM.

    Techniques: Multiplex Assay, Polymerase Chain Reaction

    Detection of the five bacterial taxa using the newly described multiplex PCR protocol. L: molecular size marker, 100 bp DNA ladder ready to load, Solis Biodyne, Pfs : P . fuscovaginae strain UBP735, Bg : B . glumae strain NCPPB 3923, Sph : Sphingomonas strain V1-2, Xoc : X . oryzae pv. oryzicola strain BAI10, Pan : Pantoea strain ARC10, Mix: Equal amounts of all five DNA samples.

    Journal: PLoS ONE

    Article Title: Design of a new multiplex PCR assay for rice pathogenic bacteria detection and its application to infer disease incidence and detect co-infection in rice fields in Burkina Faso

    doi: 10.1371/journal.pone.0232115

    Figure Lengend Snippet: Detection of the five bacterial taxa using the newly described multiplex PCR protocol. L: molecular size marker, 100 bp DNA ladder ready to load, Solis Biodyne, Pfs : P . fuscovaginae strain UBP735, Bg : B . glumae strain NCPPB 3923, Sph : Sphingomonas strain V1-2, Xoc : X . oryzae pv. oryzicola strain BAI10, Pan : Pantoea strain ARC10, Mix: Equal amounts of all five DNA samples.

    Article Snippet: Following the optimization, the final conditions for the multiplex PCR protocol were: 2 μl of DNA added to 23 μl master mix comprising 5 μl Hot Firepol Multiplex Mix ready to load 5X (Solis BioDyne,Tartu, Estonia), 1.25 μl (NH4 )2 SO4 (160 mM), 0.2 μl of each primers specific of P . fuscovaginae at 5 μM, 0.2 μl of each primers specific of B . gluma e and B . gladioli at 100 μM, 0.3 μl of each primers specific of Pantoea spp. at 100 μM and 0.3 μl of each primers specific of X . oryzae at 10 μM and finally 0.1 μl of each primers specific of Sphingomonas spp. at 10 μM.

    Techniques: Multiplex Assay, Polymerase Chain Reaction, Marker