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scientific openplex spr imaging (spri) instruments  (HORIBA Ltd)

 
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    HORIBA Ltd scientific openplex spr imaging (spri) instruments
    a Image of the SPOC sensor surface (10 k pattern) as viewed from the flowcell of the <t>OpenPleX.</t> The hockey-stick shaped orientation mark is visible in the center of the array. b Difference image showing the pattern of binding observed on the SPOC biosensor surface after injection of mouse anti-HaloTag antibody (133 nM). c Difference image showing the pattern of binding observed after the Mouse anti-Jun antibody injection (200 nM) which specifically detects two spots (yellow marks) where Jun-HaloTag was capture-purified as expected. d 1:1 fit (orange line) OpenPleX data of the anti-Jun antibody binding to Jun Spots #1 and #2 from c show similar binding profiles and equilibrium dissociation constants. e Difference image shows the pattern of binding observed after the mouse anti-p53 antibody injection (17.8 nM) which specifically detects four spots (yellow marks) where p53-HaloTag was capture-purified as expected. f 1:1 fit (orange lines) OpenPleX data of the anti-p53 antibody binding to the four p53 spots detected in e show similar binding profiles and equilibrium dissociation constants. g Iso-affinity plot of the kinetics measured for the Mouse anti-p53 and anti-Jun injections (p53 = 10 spots across 3 sensors; Jun = 4 spots across 2 sensors). The numerical source dataset for this iso-affinity plot is on Table .
    Scientific Openplex Spr Imaging (Spri) Instruments, supplied by HORIBA Ltd, 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/result/scientific openplex spr imaging (spri) instruments/product/HORIBA Ltd
    Average 90 stars, based on 1 article reviews
    scientific openplex spr imaging (spri) instruments - by Bioz Stars, 2026-04
    90/100 stars

    Images

    1) Product Images from "Multiplexed proteomic biosensor platform for label-free real-time simultaneous kinetic screening of thousands of protein interactions"

    Article Title: Multiplexed proteomic biosensor platform for label-free real-time simultaneous kinetic screening of thousands of protein interactions

    Journal: Communications Biology

    doi: 10.1038/s42003-025-07844-z

    a Image of the SPOC sensor surface (10 k pattern) as viewed from the flowcell of the OpenPleX. The hockey-stick shaped orientation mark is visible in the center of the array. b Difference image showing the pattern of binding observed on the SPOC biosensor surface after injection of mouse anti-HaloTag antibody (133 nM). c Difference image showing the pattern of binding observed after the Mouse anti-Jun antibody injection (200 nM) which specifically detects two spots (yellow marks) where Jun-HaloTag was capture-purified as expected. d 1:1 fit (orange line) OpenPleX data of the anti-Jun antibody binding to Jun Spots #1 and #2 from c show similar binding profiles and equilibrium dissociation constants. e Difference image shows the pattern of binding observed after the mouse anti-p53 antibody injection (17.8 nM) which specifically detects four spots (yellow marks) where p53-HaloTag was capture-purified as expected. f 1:1 fit (orange lines) OpenPleX data of the anti-p53 antibody binding to the four p53 spots detected in e show similar binding profiles and equilibrium dissociation constants. g Iso-affinity plot of the kinetics measured for the Mouse anti-p53 and anti-Jun injections (p53 = 10 spots across 3 sensors; Jun = 4 spots across 2 sensors). The numerical source dataset for this iso-affinity plot is on Table .
    Figure Legend Snippet: a Image of the SPOC sensor surface (10 k pattern) as viewed from the flowcell of the OpenPleX. The hockey-stick shaped orientation mark is visible in the center of the array. b Difference image showing the pattern of binding observed on the SPOC biosensor surface after injection of mouse anti-HaloTag antibody (133 nM). c Difference image showing the pattern of binding observed after the Mouse anti-Jun antibody injection (200 nM) which specifically detects two spots (yellow marks) where Jun-HaloTag was capture-purified as expected. d 1:1 fit (orange line) OpenPleX data of the anti-Jun antibody binding to Jun Spots #1 and #2 from c show similar binding profiles and equilibrium dissociation constants. e Difference image shows the pattern of binding observed after the mouse anti-p53 antibody injection (17.8 nM) which specifically detects four spots (yellow marks) where p53-HaloTag was capture-purified as expected. f 1:1 fit (orange lines) OpenPleX data of the anti-p53 antibody binding to the four p53 spots detected in e show similar binding profiles and equilibrium dissociation constants. g Iso-affinity plot of the kinetics measured for the Mouse anti-p53 and anti-Jun injections (p53 = 10 spots across 3 sensors; Jun = 4 spots across 2 sensors). The numerical source dataset for this iso-affinity plot is on Table .

    Techniques Used: Binding Assay, Injection, Purification

    10 k SPOC array kinetic parameters derived from two protein specific antibody analytes binding to their respective target protein-ligands as measured on the OpenPleX instrument
    Figure Legend Snippet: 10 k SPOC array kinetic parameters derived from two protein specific antibody analytes binding to their respective target protein-ligands as measured on the OpenPleX instrument

    Techniques Used: Derivative Assay, Binding Assay



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    a Image of the SPOC sensor surface (10 k pattern) as viewed from the flowcell of the <t>OpenPleX.</t> The hockey-stick shaped orientation mark is visible in the center of the array. b Difference image showing the pattern of binding observed on the SPOC biosensor surface after injection of mouse anti-HaloTag antibody (133 nM). c Difference image showing the pattern of binding observed after the Mouse anti-Jun antibody injection (200 nM) which specifically detects two spots (yellow marks) where Jun-HaloTag was capture-purified as expected. d 1:1 fit (orange line) OpenPleX data of the anti-Jun antibody binding to Jun Spots #1 and #2 from c show similar binding profiles and equilibrium dissociation constants. e Difference image shows the pattern of binding observed after the mouse anti-p53 antibody injection (17.8 nM) which specifically detects four spots (yellow marks) where p53-HaloTag was capture-purified as expected. f 1:1 fit (orange lines) OpenPleX data of the anti-p53 antibody binding to the four p53 spots detected in e show similar binding profiles and equilibrium dissociation constants. g Iso-affinity plot of the kinetics measured for the Mouse anti-p53 and anti-Jun injections (p53 = 10 spots across 3 sensors; Jun = 4 spots across 2 sensors). The numerical source dataset for this iso-affinity plot is on Table .
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    a Image of the SPOC sensor surface (10 k pattern) as viewed from the flowcell of the <t>OpenPleX.</t> The hockey-stick shaped orientation mark is visible in the center of the array. b Difference image showing the pattern of binding observed on the SPOC biosensor surface after injection of mouse anti-HaloTag antibody (133 nM). c Difference image showing the pattern of binding observed after the Mouse anti-Jun antibody injection (200 nM) which specifically detects two spots (yellow marks) where Jun-HaloTag was capture-purified as expected. d 1:1 fit (orange line) OpenPleX data of the anti-Jun antibody binding to Jun Spots #1 and #2 from c show similar binding profiles and equilibrium dissociation constants. e Difference image shows the pattern of binding observed after the mouse anti-p53 antibody injection (17.8 nM) which specifically detects four spots (yellow marks) where p53-HaloTag was capture-purified as expected. f 1:1 fit (orange lines) OpenPleX data of the anti-p53 antibody binding to the four p53 spots detected in e show similar binding profiles and equilibrium dissociation constants. g Iso-affinity plot of the kinetics measured for the Mouse anti-p53 and anti-Jun injections (p53 = 10 spots across 3 sensors; Jun = 4 spots across 2 sensors). The numerical source dataset for this iso-affinity plot is on Table .
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    Image Search Results


    a Image of the SPOC sensor surface (10 k pattern) as viewed from the flowcell of the OpenPleX. The hockey-stick shaped orientation mark is visible in the center of the array. b Difference image showing the pattern of binding observed on the SPOC biosensor surface after injection of mouse anti-HaloTag antibody (133 nM). c Difference image showing the pattern of binding observed after the Mouse anti-Jun antibody injection (200 nM) which specifically detects two spots (yellow marks) where Jun-HaloTag was capture-purified as expected. d 1:1 fit (orange line) OpenPleX data of the anti-Jun antibody binding to Jun Spots #1 and #2 from c show similar binding profiles and equilibrium dissociation constants. e Difference image shows the pattern of binding observed after the mouse anti-p53 antibody injection (17.8 nM) which specifically detects four spots (yellow marks) where p53-HaloTag was capture-purified as expected. f 1:1 fit (orange lines) OpenPleX data of the anti-p53 antibody binding to the four p53 spots detected in e show similar binding profiles and equilibrium dissociation constants. g Iso-affinity plot of the kinetics measured for the Mouse anti-p53 and anti-Jun injections (p53 = 10 spots across 3 sensors; Jun = 4 spots across 2 sensors). The numerical source dataset for this iso-affinity plot is on Table .

    Journal: Communications Biology

    Article Title: Multiplexed proteomic biosensor platform for label-free real-time simultaneous kinetic screening of thousands of protein interactions

    doi: 10.1038/s42003-025-07844-z

    Figure Lengend Snippet: a Image of the SPOC sensor surface (10 k pattern) as viewed from the flowcell of the OpenPleX. The hockey-stick shaped orientation mark is visible in the center of the array. b Difference image showing the pattern of binding observed on the SPOC biosensor surface after injection of mouse anti-HaloTag antibody (133 nM). c Difference image showing the pattern of binding observed after the Mouse anti-Jun antibody injection (200 nM) which specifically detects two spots (yellow marks) where Jun-HaloTag was capture-purified as expected. d 1:1 fit (orange line) OpenPleX data of the anti-Jun antibody binding to Jun Spots #1 and #2 from c show similar binding profiles and equilibrium dissociation constants. e Difference image shows the pattern of binding observed after the mouse anti-p53 antibody injection (17.8 nM) which specifically detects four spots (yellow marks) where p53-HaloTag was capture-purified as expected. f 1:1 fit (orange lines) OpenPleX data of the anti-p53 antibody binding to the four p53 spots detected in e show similar binding profiles and equilibrium dissociation constants. g Iso-affinity plot of the kinetics measured for the Mouse anti-p53 and anti-Jun injections (p53 = 10 spots across 3 sensors; Jun = 4 spots across 2 sensors). The numerical source dataset for this iso-affinity plot is on Table .

    Article Snippet: The SPOC technology is adaptable to any SPR instrument; however, for this publication, the custom Carterra LSA XT SPR and Horiba Scientific OpenPleX SPR imaging (SPRi) instruments were used for validation because both instruments are amenable to HTP screening and require minimal effort to integrate with our SPOC protein biosensor platform.

    Techniques: Binding Assay, Injection, Purification

    10 k SPOC array kinetic parameters derived from two protein specific antibody analytes binding to their respective target protein-ligands as measured on the OpenPleX instrument

    Journal: Communications Biology

    Article Title: Multiplexed proteomic biosensor platform for label-free real-time simultaneous kinetic screening of thousands of protein interactions

    doi: 10.1038/s42003-025-07844-z

    Figure Lengend Snippet: 10 k SPOC array kinetic parameters derived from two protein specific antibody analytes binding to their respective target protein-ligands as measured on the OpenPleX instrument

    Article Snippet: The SPOC technology is adaptable to any SPR instrument; however, for this publication, the custom Carterra LSA XT SPR and Horiba Scientific OpenPleX SPR imaging (SPRi) instruments were used for validation because both instruments are amenable to HTP screening and require minimal effort to integrate with our SPOC protein biosensor platform.

    Techniques: Derivative Assay, Binding Assay