real time rt pcr qpcr  (Solis BioDyne)


Bioz Verified Symbol Solis BioDyne is a verified supplier
Bioz Manufacturer Symbol Solis BioDyne manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    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
    https://www.bioz.com/result/real time rt pcr qpcr/product/Solis BioDyne
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    real time rt pcr qpcr - by Bioz Stars, 2022-07
    94/100 stars

    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 "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

    4) 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

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    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
    https://www.bioz.com/result/real time rt pcr qpcr/product/Solis BioDyne
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    real time rt pcr qpcr - by Bioz Stars, 2022-07
    94/100 stars
      Buy from Supplier

    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, 2022-07
    92/100 stars
      Buy from Supplier

    Image Search Results


    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

    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

    Journal: Stem Cell Reports

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

    doi: 10.1016/j.stemcr.2019.09.002

    Figure Lengend 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

    Article Snippet: For the real-time qPCR analysis, HOT FIREPol EvaGreen qPCR Mix Plus (Solis Biodyne) was used, and the expression levels were normalized to GAPDH expression.

    Techniques: 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.

    Journal: Stem Cell Reports

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

    doi: 10.1016/j.stemcr.2019.09.002

    Figure Lengend 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.

    Article Snippet: For the real-time qPCR analysis, HOT FIREPol EvaGreen qPCR Mix Plus (Solis Biodyne) was used, and the expression levels were normalized to GAPDH expression.

    Techniques: 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

    Journal: Stem Cell Reports

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

    doi: 10.1016/j.stemcr.2019.09.002

    Figure Lengend 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

    Article Snippet: For the real-time qPCR analysis, HOT FIREPol EvaGreen qPCR Mix Plus (Solis Biodyne) was used, and the expression levels were normalized to GAPDH expression.

    Techniques: 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

    Journal: Stem Cell Reports

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

    doi: 10.1016/j.stemcr.2019.09.002

    Figure Lengend 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

    Article Snippet: For the real-time qPCR analysis, HOT FIREPol EvaGreen qPCR Mix Plus (Solis Biodyne) was used, and the expression levels were normalized to GAPDH expression.

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

    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