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microarray spotting robot digilab omnigrid  (Digilab Inc)

 
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    Digilab Inc microarray spotting robot digilab omnigrid
    Microarray Spotting Robot Digilab Omnigrid, supplied by Digilab Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/microarray-spotting+robot/microarraying+robot+microgrid+610/pm26549580-241-7-6
    Average 90 stars, based on 1 article reviews
    microarray spotting robot digilab omnigrid - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Microarray:

    Article Title: The role of indoleamine 2,3-dioxygenase-aryl hydrocarbon receptor pathway in the TLR4-induced tolerogenic phenotype in human DCs.
    Article Snippet: .. After denaturation, samples were spotted onto nitrocellulose-coated glass slides (Grace Bio-labs) with a microarray robot (MicroGrid 610, Digilab). .. Then, slides were incubated overnight in blocking solution (0.2% I-Block (Thermo Fisher Scientific), Tween-20 (0.1%) in PBS (Sigma-Aldrich) at 4 °C.

    Article Title: Clinical utility of reverse phase protein array for molecular classification of breast cancer.
    Article Snippet: Reverse Phase Protein Array (RPPA) represents a sensitive and high-throughput technique allowing simultaneous quantitation of protein expression levels in biological samples.. This study aimed to confirm the ability of RPPA to classify archival formalin-fixed paraffin-embedded (FFPE) breast cancer tissues into molecular classes used in the Nottingham prognostic index plus (NPI?) determined by immunohistochemistry (IHC).. Proteins were extracted from FFPE breast cancer tissues using three extraction protocols: the Q-proteome FFPE Tissue Kit (Qiagen, Hilden, Germany) and two in-house methods using Laemmli buffer with either incubation for 20 min or 2 h at 105 C. Two preparation methods, full-face sections and macrodissection, were used to assess the yield and quality of protein extracts.

    Article Title: The mannose receptor negatively modulates the Toll-like receptor 4-aryl hydrocarbon receptor-indoleamine 2,3-dioxygenase axis in dendritic cells affecting T helper cell polarization.
    Article Snippet: .. After denaturation, samples were spotted onto nitrocellulose-coated glass slides (Grace Bio-Labs, Bend, Ore) with a microarray robot (MicroGrid 610; Digilab, Marlborough, Mass). .. Then slides were incubated overnight in blocking solution (0.2% IBlock [Thermo Fisher Scientific] and 0.1% Tween-20 in PBS [SigmaAldrich]) at 48C.

    Article Title: A Pro-Inflammatory Signature Constitutively Activated in Monogenic Autoinflammatory Diseases
    Article Snippet: .. Briefly, samples were spotted in duplicates onto a nitrocellulose-coated glass slide (Grace Bio-labs, Bend, OR, USA) using a microarray robot (MicroGrid 610, Digilab, Marlborough, MA, USA). .. The printed slides were blocked and incubated with specific primary antibodies listed in (Cell Signalling) overnight at 4 °C, with shaking.

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

    Article Title: The role of indoleamine 2,3-dioxygenase-aryl hydrocarbon receptor pathway in the TLR4-induced tolerogenic phenotype in human DCs
    Article Snippet: .. After denaturation, samples were spotted onto nitrocellulose-coated glass slides (Grace Bio-labs) with a microarray robot (MicroGrid 610, Digilab). .. Then, slides were incubated overnight in blocking solution (0.2% I-Block (Thermo Fisher Scientific), Tween-20 (0.1%) in PBS (Sigma-Aldrich) at 4 °C.

    other:

    Article Title: New and Improved Techniques for the Study of Pathogenic Fungi.
    Article Snippet: Fungal pathogens pose serious threats to human, plant, and ecosystem health.. Improved diagnostics and antifungal strategies are therefore urgently required.. Here, we review recent developments in online bioinformatic tools and associated interactive data archives, which enable sophisticated comparative genomics and functional analysis of fungal pathogens in silico.

    Glycoproteomics:

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

    Binding Assay:

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



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    Identification of the RLR sequence as a potential MIF binding region to the N-terminal peptide of CXCR4. ( a , b ) The peptide spot <t>microarray</t> method suggests that the RLR tripeptide at sequence position 87–89 may contribute to MIF/CXCR4 binding. A peptide spot array containing 15-mer spotted MIF peptides positionally shifted by three amino acids were probed with biotin-CXCR4(1–27). Graphs are plots of spotted MIF peptides over the intensity of the binding signal to biotin-CXCR4(1–27) as read-out by streptavidin Cy5.5 fluorescence. ( a ) Of five positionally shifted 15-mer peptides of the region 79–105 only peptides containing RLR interact with CXCR4(1–27). ( b ) Binding of RLR-containing MIF peptides is modulated by N-terminal extension, but residues N-terminal of RLR do not exhibit binding activity per se . ( c ) Structural model of MIF (as monomer and trimer) and position of the N-like loop (green) and the RLR sequence (red). Note: in the three-dimensional conformation of the monomer, RLR is located in the vicinity of the N-like loop of MIF. The trimeric structure shows that both the N-like loop and RLR are surface-exposed on the trimer (see also Fig. ).
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    Identification of the RLR sequence as a potential MIF binding region to the N-terminal peptide of CXCR4. ( a , b ) The peptide spot <t>microarray</t> method suggests that the RLR tripeptide at sequence position 87–89 may contribute to MIF/CXCR4 binding. A peptide spot array containing 15-mer spotted MIF peptides positionally shifted by three amino acids were probed with biotin-CXCR4(1–27). Graphs are plots of spotted MIF peptides over the intensity of the binding signal to biotin-CXCR4(1–27) as read-out by streptavidin Cy5.5 fluorescence. ( a ) Of five positionally shifted 15-mer peptides of the region 79–105 only peptides containing RLR interact with CXCR4(1–27). ( b ) Binding of RLR-containing MIF peptides is modulated by N-terminal extension, but residues N-terminal of RLR do not exhibit binding activity per se . ( c ) Structural model of MIF (as monomer and trimer) and position of the N-like loop (green) and the RLR sequence (red). Note: in the three-dimensional conformation of the monomer, RLR is located in the vicinity of the N-like loop of MIF. The trimeric structure shows that both the N-like loop and RLR are surface-exposed on the trimer (see also Fig. ).
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    Image Search Results


    Identification of the RLR sequence as a potential MIF binding region to the N-terminal peptide of CXCR4. ( a , b ) The peptide spot microarray method suggests that the RLR tripeptide at sequence position 87–89 may contribute to MIF/CXCR4 binding. A peptide spot array containing 15-mer spotted MIF peptides positionally shifted by three amino acids were probed with biotin-CXCR4(1–27). Graphs are plots of spotted MIF peptides over the intensity of the binding signal to biotin-CXCR4(1–27) as read-out by streptavidin Cy5.5 fluorescence. ( a ) Of five positionally shifted 15-mer peptides of the region 79–105 only peptides containing RLR interact with CXCR4(1–27). ( b ) Binding of RLR-containing MIF peptides is modulated by N-terminal extension, but residues N-terminal of RLR do not exhibit binding activity per se . ( c ) Structural model of MIF (as monomer and trimer) and position of the N-like loop (green) and the RLR sequence (red). Note: in the three-dimensional conformation of the monomer, RLR is located in the vicinity of the N-like loop of MIF. The trimeric structure shows that both the N-like loop and RLR are surface-exposed on the trimer (see also Fig. ).

    Journal: Scientific Reports

    Article Title: Identification of an Arg-Leu-Arg tripeptide that contributes to the binding interface between the cytokine MIF and the chemokine receptor CXCR4

    doi: 10.1038/s41598-018-23554-5

    Figure Lengend Snippet: Identification of the RLR sequence as a potential MIF binding region to the N-terminal peptide of CXCR4. ( a , b ) The peptide spot microarray method suggests that the RLR tripeptide at sequence position 87–89 may contribute to MIF/CXCR4 binding. A peptide spot array containing 15-mer spotted MIF peptides positionally shifted by three amino acids were probed with biotin-CXCR4(1–27). Graphs are plots of spotted MIF peptides over the intensity of the binding signal to biotin-CXCR4(1–27) as read-out by streptavidin Cy5.5 fluorescence. ( a ) Of five positionally shifted 15-mer peptides of the region 79–105 only peptides containing RLR interact with CXCR4(1–27). ( b ) Binding of RLR-containing MIF peptides is modulated by N-terminal extension, but residues N-terminal of RLR do not exhibit binding activity per se . ( c ) Structural model of MIF (as monomer and trimer) and position of the N-like loop (green) and the RLR sequence (red). Note: in the three-dimensional conformation of the monomer, RLR is located in the vicinity of the N-like loop of MIF. The trimeric structure shows that both the N-like loop and RLR are surface-exposed on the trimer (see also Fig. ).

    Article Snippet: Analysis of interactions was performed using a microarray processing station (Intavis Slide Spotting Robot).

    Techniques: Sequencing, Binding Assay, Microarray, Fluorescence, Activity Assay