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microarray processing station intavis slide spotting robot  (INTAVIS Inc)

 
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    INTAVIS Inc microarray processing station intavis slide spotting robot
    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. ).
    Microarray Processing Station Intavis Slide Spotting Robot, supplied by INTAVIS 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/microarray+processing+station+intavis+slide+spotting+robot/pmc05979958-312-7-10
    Average 90 stars, based on 1 article reviews
    microarray processing station intavis slide spotting robot - by Bioz Stars, 2026-10
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    1) Product Images from "Identification of an Arg-Leu-Arg tripeptide that contributes to the binding interface between the cytokine MIF and the chemokine receptor CXCR4"

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

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-23554-5

    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. ).
    Figure Legend 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. ).

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

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    Article Title: Identification of an Arg-Leu-Arg tripeptide that contributes to the binding interface between the cytokine MIF and the chemokine receptor CXCR4
    Article Snippet: .. Analysis of interactions was performed using a microarray processing station (Intavis Slide Spotting Robot). ..



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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 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