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Related Experiment Video

Updated: Jun 15, 2026

Identifying PD-1/PD-L1 Inhibitors with Surface Plasmon Resonance Technology
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Identifying PD-1/PD-L1 Inhibitors with Surface Plasmon Resonance Technology

Published on: May 2, 2025

High-throughput kinase assay based on surface plasmon resonance.

Hiroyuki Takeda1, Naoki Goshima, Nobuo Nomura

  • 1Protein Expression Team, Japan Biological Information Research Center, Japan Biological Informatics Consortium, Tokyo, Japan.

Methods in Molecular Biology (Clifton, N.J.)
|March 11, 2010
PubMed
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We developed a novel high-throughput kinase assay using surface plasmon resonance (SPR). This method enables efficient detection of tyrosine phosphorylation in over 1,000 samples daily, enhancing drug discovery research.

Area of Science:

  • Biochemistry
  • Assay Development
  • Biotechnology

Background:

  • Kinase assays are crucial for understanding cellular signaling and drug discovery.
  • Existing methods can be limited in throughput, flexibility, and real-time monitoring capabilities.

Purpose of the Study:

  • To design and validate a novel high-throughput kinase assay.
  • To enable flexible detection of tyrosine phosphorylation using native substrates.
  • To achieve high sample processing capacity for kinase activity screening.

Main Methods:

  • Utilized an array-based surface plasmon resonance (SPR) apparatus.
  • Developed a two-part assay: in vitro phosphorylation and phospho-detection on a sensor chip.
  • Employed immobilized capture antibodies for substrate immobilization and anti-phosphotyrosine (pTyr) antibodies for detection.

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Identification of Kinase-substrate Pairs Using High Throughput Screening
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Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

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Last Updated: Jun 15, 2026

Identifying PD-1/PD-L1 Inhibitors with Surface Plasmon Resonance Technology
07:04

Identifying PD-1/PD-L1 Inhibitors with Surface Plasmon Resonance Technology

Published on: May 2, 2025

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Main Results:

  • Successfully detected tyrosine phosphorylation using both biotinylated peptides and recombinant proteins as substrates.
  • Achieved a wide dynamic range and real-time monitoring of phosphorylation events via SPR.
  • Optimized the assay for array-based processing, enabling up to 1,000 samples per day.

Conclusions:

  • The novel HTP kinase assay offers high flexibility and performance for tyrosine phosphorylation detection.
  • The SPR-based approach provides reliable, real-time data and significantly increases sample throughput.
  • This assay is a valuable tool for accelerating kinase inhibitor screening and drug discovery.