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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+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, 2026-08
    90/100 stars

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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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    Figure 2. (A) Layout of the biomarker <t>microarray</t> (BMA) slide, showing the arrangement of capture antibodies and controls within each well. (B) Illustration of the BMA slide design with 16 wells and its alignment within the slide holder for analysis. The numbers along the side correspond to the row numbers of each well, while the numbers along the bottom represent the column positions of the slide.
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    Image Search Results


    Figure 2. (A) Layout of the biomarker microarray (BMA) slide, showing the arrangement of capture antibodies and controls within each well. (B) Illustration of the BMA slide design with 16 wells and its alignment within the slide holder for analysis. The numbers along the side correspond to the row numbers of each well, while the numbers along the bottom represent the column positions of the slide.

    Journal: Micromachines

    Article Title: Portable Fluorescence Microarray Reader-Enabled Biomarker Panel Detection System for Point-of-Care Diagnosis of Lupus Nephritis.

    doi: 10.3390/mi16020156

    Figure Lengend Snippet: Figure 2. (A) Layout of the biomarker microarray (BMA) slide, showing the arrangement of capture antibodies and controls within each well. (B) Illustration of the BMA slide design with 16 wells and its alignment within the slide holder for analysis. The numbers along the side correspond to the row numbers of each well, while the numbers along the bottom represent the column positions of the slide.

    Article Snippet: The slides were prepared using a non-contact microarray printing robot (sciFLEXARRAYER S3; Scienion GmbH, Berlin, Germany), which printed capture antibodies for each biomarker in triplicate at a controlled drop volume of 450 ± 20 pL.

    Techniques: Biomarker Discovery, Microarray