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Genomic Solutions Inc biorobotics microgrid ii microarray
Serum samples collected from C57BL/6NCrl mice (n = 12–16 per group) immunized with either saline, CDN Nanovaccine, Nanovaccine, or Combination Nanovaccine at 14, 79, and 178 DPI was analyzed for total anti-F1-V IgG antibodies against twenty-seven 14- to 17-mer linear peptides (11 amino acid overlaps) from the F1 antigen and fifty-three 15- to 17-mer linear peptides (11 or 12 amino acid overlaps) from the V antigen. The peptides were covalently bound to <t>microarray</t> slides as described in Materials and Methods. Each row corresponds to a specific peptide, the top row representing peptide F1 and the proceeding downward rows corresponding to each following linear peptide incrementally through peptide V53. Each column represents responses from a single mouse. The mean fluorescence intensity of serum responses to each peptide is represented by a range of color from white (no response) to purple (maximum response). The full-length F1-V fusion protein was used as a positive control, and Bacillus anthracis protective antigen (PA) and chicken egg ovalbumin (OVA) were used as negative controls. Black arrows indicate significance (p ≤ 0.05) of Combination Nanovaccine and CDN Vaccine serum compared to naïve serum at all time points evaluated. Blue arrows indicate significance (p < –0.05) of Combination Nanovaccine and CDN Vaccine serum compared to naïve serum at 179 DPI. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
Biorobotics Microgrid Ii Microarray, supplied by Genomic Solutions Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Single-dose combination nanovaccine induces both rapid and long-lived protection against pneumonic plague"

Article Title: Single-dose combination nanovaccine induces both rapid and long-lived protection against pneumonic plague

Journal: Acta biomaterialia

doi: 10.1016/j.actbio.2019.10.016

Serum samples collected from C57BL/6NCrl mice (n = 12–16 per group) immunized with either saline, CDN Nanovaccine, Nanovaccine, or Combination Nanovaccine at 14, 79, and 178 DPI was analyzed for total anti-F1-V IgG antibodies against twenty-seven 14- to 17-mer linear peptides (11 amino acid overlaps) from the F1 antigen and fifty-three 15- to 17-mer linear peptides (11 or 12 amino acid overlaps) from the V antigen. The peptides were covalently bound to microarray slides as described in Materials and Methods. Each row corresponds to a specific peptide, the top row representing peptide F1 and the proceeding downward rows corresponding to each following linear peptide incrementally through peptide V53. Each column represents responses from a single mouse. The mean fluorescence intensity of serum responses to each peptide is represented by a range of color from white (no response) to purple (maximum response). The full-length F1-V fusion protein was used as a positive control, and Bacillus anthracis protective antigen (PA) and chicken egg ovalbumin (OVA) were used as negative controls. Black arrows indicate significance (p ≤ 0.05) of Combination Nanovaccine and CDN Vaccine serum compared to naïve serum at all time points evaluated. Blue arrows indicate significance (p < –0.05) of Combination Nanovaccine and CDN Vaccine serum compared to naïve serum at 179 DPI. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
Figure Legend Snippet: Serum samples collected from C57BL/6NCrl mice (n = 12–16 per group) immunized with either saline, CDN Nanovaccine, Nanovaccine, or Combination Nanovaccine at 14, 79, and 178 DPI was analyzed for total anti-F1-V IgG antibodies against twenty-seven 14- to 17-mer linear peptides (11 amino acid overlaps) from the F1 antigen and fifty-three 15- to 17-mer linear peptides (11 or 12 amino acid overlaps) from the V antigen. The peptides were covalently bound to microarray slides as described in Materials and Methods. Each row corresponds to a specific peptide, the top row representing peptide F1 and the proceeding downward rows corresponding to each following linear peptide incrementally through peptide V53. Each column represents responses from a single mouse. The mean fluorescence intensity of serum responses to each peptide is represented by a range of color from white (no response) to purple (maximum response). The full-length F1-V fusion protein was used as a positive control, and Bacillus anthracis protective antigen (PA) and chicken egg ovalbumin (OVA) were used as negative controls. Black arrows indicate significance (p ≤ 0.05) of Combination Nanovaccine and CDN Vaccine serum compared to naïve serum at all time points evaluated. Blue arrows indicate significance (p < –0.05) of Combination Nanovaccine and CDN Vaccine serum compared to naïve serum at 179 DPI. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Techniques Used: Microarray, Fluorescence, Positive Control

Related Articles

Microarray:

Article Title: Analysis of swine antigen-specific antibody responses to Mycoplasma hyopneumoniae infection determined by protein microarray.
Article Snippet: Accepted Manuscript Title: Analysis of swine antigen-specific antibody responses to Mycoplasma hyopneumoniae infection determined by protein microarray Authors: Andrew C. Petersen, Jeannett M. Clampitt, F. Chris Minion PII: S0378-1135(18)31028-9 DOI: https://doi.org/10.1016/j.vetmic.2019.02.010 Reference: VETMIC 8214 To appear in: VETMIC Received date: 31 August 2018 Revised date: 9 January 2019 Accepted date: 5 February 2019 Please cite this article as: Petersen AC, Clampitt JM, Minion FC, Analysis of swine antigen-specific antibody responses to Mycoplasma hyopneumoniae infection determined by protein microarray, Veterinary Microbiology (2019), https://doi.org/10.1016/j.vetmic.2019.02.010 This is a PDF file of an unedited manuscript that has been accepted for publication.. As a service to our customers we are providing this early version of the manuscript.. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form.

other:

Article Title: DNA polymerase-α regulates type I interferon activation through cytosolic RNA:DNA synthesis
Article Snippet: The antigens were printed in duplicate onto nitrocellulose-coated 16-pad FASTTM slides (Whatman, Sanford, ME, USA) by MicroGrid II 610 bio-robotics array printer (Genomic Solutions Inc., Ann Arbor, MI, USA).

Article Title: DNA polymerase-α regulates the activation of type I interferons through cytosolic RNA:DNA synthesis.
Article Snippet: The antigens were printed in duplicate onto nitrocellulose-coated 16-pad FASTTM slides (Whatman, Sanford, ME, USA) by MicroGrid II 610 bio-robotics array printer (Genomic Solutions Inc., Ann Arbor, MI, USA).

Article Title: Skeletal muscle alterations and exercise performance decrease in erythropoietin-deficient mice: a comparative study
Article Snippet: The microarrays were spotted (LEFG, CEA, Evry, France) by printing the probes (suspended in a spotting buffer composed of 1:1 v/v dimethyl sulfoxide (DMSO) and Tris EDTA buffer) on hydrogel slides (Nexterion, Schott) with a Microgrid-II robot (Genomic Solutions Inc., Ann Arbor, MI).

Article Title: Single-dose combination nanovaccine induces both rapid and long-lived protection against pneumonic plague
Article Snippet: Peptide microarray printing and analysis Twenty-seven 14- to 17-mer linear peptides (11 amino acid overlaps) spanning the full length of F1 antigen and fifty-three 15-to 17-mer linear peptides (11 or 12 amino acid overlaps) spanning the full length of V antigen, as well as full length proteins F1-V, Bacillus anthracis protective antigen (PA), and chicken egg ovalbumin (OVA) were printed onto Nexterion Slide AL (Schott, Louisville, KY) using a BioRobotics MicroGRID II microarray printer (Genomic Solutions, Inc. Ann Arbor, MI).

Hybridization:

Article Title: Isolation of putative pepper defense-related genes against the pathogen Phytophthora capsici using suppression subtractive hybridization/macroarray and RNA-sequencing analyses
Article Snippet: The oomycete Phytophthora capsici Leonian is one of the most economically important pathogens limiting pepper (Capsicum annuum) production in many regions around the world.. Insights into the defense mechanisms of pepper against P. capsici would be helpful in the breeding of resistant cultivars.. However, little is still known about the defense system in pepper against P. capsici.



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Glycan Array Analysis of AgRP Binding to Heparan Sulfate Oligosaccharides (A) Fluorescent image of the glass slide glycan arrays showing fluorescence signals (green dots) of AgRP binding to 52 immobilized heparan sulfate oligosaccharides (low-molecular-weight heparan sulfate, LMHS). (B) Bar graph showing the relative fluorescence intensity of AgRP binding to the heparan sulfate oligosaccharides arrays. Heparan sulfate oligosaccharides 22 and 41 show the highest intensity. (C) The structures of the different heparan sulfate oligosaccharides on the slide <t>microarray</t> in A. Data are represented as mean ± SEM.
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Testing the limits of NRF2 binding. Systematic multivariate ARE results by protein binding <t>microarray</t> for NRF2-MAFG heterodimer are shown. Tolerance for sequence variation was studied for positions 1–3 (white), 6–8 (grey) and 9–11 (dark grey) ( A ) and positions 1, 5 and 11 (seed sequences are shown in grey) ( B ). Results are depicted as measured binding relative to NQO1.ARE binding (black) (mean ± S.E.M., n = 45).
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Image Search Results


Glycan Array Analysis of AgRP Binding to Heparan Sulfate Oligosaccharides (A) Fluorescent image of the glass slide glycan arrays showing fluorescence signals (green dots) of AgRP binding to 52 immobilized heparan sulfate oligosaccharides (low-molecular-weight heparan sulfate, LMHS). (B) Bar graph showing the relative fluorescence intensity of AgRP binding to the heparan sulfate oligosaccharides arrays. Heparan sulfate oligosaccharides 22 and 41 show the highest intensity. (C) The structures of the different heparan sulfate oligosaccharides on the slide microarray in A. Data are represented as mean ± SEM.

Journal: iScience

Article Title: Charge Characteristics of Agouti-Related Protein Implicate Potent Involvement of Heparan Sulfate Proteoglycans in Metabolic Function

doi: 10.1016/j.isci.2019.10.061

Figure Lengend Snippet: Glycan Array Analysis of AgRP Binding to Heparan Sulfate Oligosaccharides (A) Fluorescent image of the glass slide glycan arrays showing fluorescence signals (green dots) of AgRP binding to 52 immobilized heparan sulfate oligosaccharides (low-molecular-weight heparan sulfate, LMHS). (B) Bar graph showing the relative fluorescence intensity of AgRP binding to the heparan sulfate oligosaccharides arrays. Heparan sulfate oligosaccharides 22 and 41 show the highest intensity. (C) The structures of the different heparan sulfate oligosaccharides on the slide microarray in A. Data are represented as mean ± SEM.

Article Snippet: Amine(-NH 2 )-linked heparan sulfate glycan compounds (Glycan Therapeutics) were immobilized on NHS-activated surface-coated slides (Nexterion Slide-H, Applied Microarrays) using a robotic microarray printer (Microgrid II, Digilab) that was equipped with StealthSMP4B microarray pins (Telechem) to couple heparan sulfate glycan compounds by covalent binding via (-NH 2 ) reactive chemistry.

Techniques: Glycoproteomics, Binding Assay, Fluorescence, Molecular Weight, Microarray

Testing the limits of NRF2 binding. Systematic multivariate ARE results by protein binding microarray for NRF2-MAFG heterodimer are shown. Tolerance for sequence variation was studied for positions 1–3 (white), 6–8 (grey) and 9–11 (dark grey) ( A ) and positions 1, 5 and 11 (seed sequences are shown in grey) ( B ). Results are depicted as measured binding relative to NQO1.ARE binding (black) (mean ± S.E.M., n = 45).

Journal: Nucleic Acids Research

Article Title: The Effects of Sequence Variation on Genome-wide NRF2 Binding—New Target Genes and Regulatory SNPs

doi: 10.1093/nar/gkw052

Figure Lengend Snippet: Testing the limits of NRF2 binding. Systematic multivariate ARE results by protein binding microarray for NRF2-MAFG heterodimer are shown. Tolerance for sequence variation was studied for positions 1–3 (white), 6–8 (grey) and 9–11 (dark grey) ( A ) and positions 1, 5 and 11 (seed sequences are shown in grey) ( B ). Results are depicted as measured binding relative to NQO1.ARE binding (black) (mean ± S.E.M., n = 45).

Article Snippet: The dilutions were dispensed in a 384-well plate (polypropylene plate No 267462, Nunc, N.Y, USA) and printed onto the avidin-coated glass slides with a microarray printer (BioRobotics MicroGrid II, BioRobotics Ltd, Cambridge, UK).

Techniques: Binding Assay, Protein Binding, Microarray, Sequencing

A SNP in FTL promoter has drastic effects of NRF2 binding and transcriptional activation. ( A ) A promoter analysis of the FTL gene at chr19 showing the location of experimentally verified NRF2 binding ARE together with dbSNP (v138) and ENCODE ChIP-seq data. ChIP-seq track displays combined MAFF and MAFK binding signals in H1-hESC (MAFK), K562 (MAFF, MAFK), HeLa-S3 (MAFK), HepG (MAFF, MAFK) and IMR90 (MAFK) cell lines. ( B ) Detailed view showing FTL ARE sequence and the SNP (rs113067944, A→C) position. ( C ) Protein binding microarray results for FTL.ARE.A and the SNP bearing FTL.ARE.C. Results are calculated as measured binding relative to NQO1.ARE binding (mean ± S.E.M, n = 39.). Scramble oligonucleotides served as negative control. ( D ) HEK-293T cells were transfected with NQO1-ARE and FTL-ARE bearing either allele A or allele C with and without NRF2 -expressing plasmids. Twenty-four h after transfection cells were treated with NRF2 inducer (L-SFN) for 16 h followed by luciferase activity measurements. An empty pGL3 promoter vector served as control and activities were normalized to β-galactosidase activity. Results are shown relative to control (mean± S.E.M, n = 4).

Journal: Nucleic Acids Research

Article Title: The Effects of Sequence Variation on Genome-wide NRF2 Binding—New Target Genes and Regulatory SNPs

doi: 10.1093/nar/gkw052

Figure Lengend Snippet: A SNP in FTL promoter has drastic effects of NRF2 binding and transcriptional activation. ( A ) A promoter analysis of the FTL gene at chr19 showing the location of experimentally verified NRF2 binding ARE together with dbSNP (v138) and ENCODE ChIP-seq data. ChIP-seq track displays combined MAFF and MAFK binding signals in H1-hESC (MAFK), K562 (MAFF, MAFK), HeLa-S3 (MAFK), HepG (MAFF, MAFK) and IMR90 (MAFK) cell lines. ( B ) Detailed view showing FTL ARE sequence and the SNP (rs113067944, A→C) position. ( C ) Protein binding microarray results for FTL.ARE.A and the SNP bearing FTL.ARE.C. Results are calculated as measured binding relative to NQO1.ARE binding (mean ± S.E.M, n = 39.). Scramble oligonucleotides served as negative control. ( D ) HEK-293T cells were transfected with NQO1-ARE and FTL-ARE bearing either allele A or allele C with and without NRF2 -expressing plasmids. Twenty-four h after transfection cells were treated with NRF2 inducer (L-SFN) for 16 h followed by luciferase activity measurements. An empty pGL3 promoter vector served as control and activities were normalized to β-galactosidase activity. Results are shown relative to control (mean± S.E.M, n = 4).

Article Snippet: The dilutions were dispensed in a 384-well plate (polypropylene plate No 267462, Nunc, N.Y, USA) and printed onto the avidin-coated glass slides with a microarray printer (BioRobotics MicroGrid II, BioRobotics Ltd, Cambridge, UK).

Techniques: Binding Assay, Activation Assay, ChIP-sequencing, Sequencing, Protein Binding, Microarray, Negative Control, Transfection, Expressing, Luciferase, Activity Assay, Plasmid Preparation, Control