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microsys 5100-4sq non-contact robotic microarray spotting system  (Digilab Inc)

 
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    Digilab Inc microsys 5100-4sq non-contact robotic microarray spotting system
    Microsys 5100 4sq Non Contact Robotic Microarray Spotting System, 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/microsys++5100+4sq+microarray+spotter/pmc05106528-168-2-4
    Average 90 stars, based on 1 article reviews
    microsys 5100-4sq non-contact robotic microarray spotting system - by Bioz Stars, 2026-09
    90/100 stars

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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 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