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QRET TECHNOLOGIES

QRET TECHNOLOGIES are experts in protein labelling and TR-FRET chelates.

QRET Technologies specializes in developing advanced Förster Resonance Energy Transfer (FRET)-based biosensors, designed to monitor molecular interactions in real-time with high sensitivity and precision. Their products are tailored for researchers in fields like drug discovery, protein-protein interaction studies, and cellular signaling pathways.

Qret Technologies

is a leading company specializing in innovative solutions for preclinical and clinical research. Their cutting-edge products and technologies empower scientists and researchers to advance their studies in protein analysis, stability monitoring, protease activity testing, and virus particle counting. With a focus on sensitivity, simplicity, and high throughput compatibility, Qret Technologies revolutionizes the field of assay development and analysis.

Protein-Probe™

Qret Technologies' flagship technology, Protein-Probe™, enables ultra-sensitive detection of proteins and variations in protein stability. Through carefully designed peptide-probes and modulator buffer systems, their Protein-Probe assays deliver nanomolar sensitivity for antibody aggregates while reducing material consumption compared to traditional methods. This versatile approach extends beyond protein analysis and can be applied to protease activity testing and virus particle counting, providing researchers with valuable tools for exploring a wide range of biological processes.

The company also offers solutions for protein stability, aggregation, and storage formulation monitoring based on the Protein-Probe™ technology. Their time-resolved fluorescence (TRF) readout method, coupled with proprietary assay buffers, allows researchers to define optimal storage formulations for proteins and screen compounds that influence protein aggregation or thermal stability. This high-throughput compatible assay format simplifies workflows and delivers robust results.

mTR-FRET™ and TR-FRET

Qret Technologies' mTR-FRET™ and TR-FRET technologies provide additional versatility for protein detection and protein-ligand interactions. The mTR-FRET™ approach allows researchers to develop assays using single-label ligand-labeled strategies, eliminating the need to label target proteins. This user-friendly format, combined with their lanthanide chelates and proprietary assay modulation solutions, offers cost-effective and efficient solutions for studying a wide range of target proteins.

Lanthanide chelates

In the realm of lanthanide chelate label technologies, Qret Technologies offers a diverse range of products based on 5-9 dentate chelate structures. These chelates, including Eu-chelate W8044, Eu-chelate W1024, and Eu-chelate DTPA, are specifically designed for Time-Resolved Fluorescence (TRF) assays. With reactive groups like ITC, DTA, and IA, these chelates provide versatile options for labeling proteins, peptides, aptamers, and small molecules, accommodating various labeling chemistries. Qret Technologies' labeling kits come with comprehensive instructions and technical support, ensuring efficient and reliable labeling processes.

Committed to driving groundbreaking discoveries and advancements in preclinical and clinical research, Qret Technologies empowers researchers with state-of-the-art tools and technologies. Their products open new avenues for protein analysis, stability monitoring, and binding assays, facilitating a deeper understanding of biological processes and contributing to scientific progress.

 

References

  1. Ecke, Thorsten H.; Scislowski, Mikolaj; Hassan, Nazia; Saura, Mari; Hallmann, Steffen; Koch, Stefan et al. (2022): Luminophore Chemistry for Detection of Urinary Bladder Cancer - Comparison to Cytology and Urinary Rapid Tests (BTA stat®, NMP22® BladderChek® and UBC®Rapid Test). In Anticancer research 42 (11), pp. 5249–5256. DOI: 10.21873/anticanres.16031.
  2. Kopra, Kari; Hassan, Nazia; Vuorinen, Emmiliisa; Valtonen, Salla; Mahran, Randa; Habib, Huda et al. (2022): Rapid high-throughput compatible label-free virus particle quantification method based on time-resolved luminescence. In Analytical and bioanalytical chemistry 414 (15), pp. 4509–4518. DOI: 10.1007/s00216-022-04104-5.
  3. Kopra, Kari; Kainulainen, Markus; Mikkonen, Piia; Rozwandowicz-Jansen, Anita; Hänninen, Pekka; Härmä, Harri (2013): Multiparametric homogeneous method for identification of ligand binding to G protein-coupled receptors: receptor-ligand binding and β-arrestin assay. In Analytical chemistry 85 (4), pp. 2276–2281. DOI: 10.1021/ac303215r.
  4. Kopra, Kari; Ligabue, Alessio; Wang, Qi; Syrjänpää, Markku; Blaževitš, Olga; Veltel, Stefan et al. (2014): A homogeneous quenching resonance energy transfer assay for the kinetic analysis of the GTPase nucleotide exchange reaction. In Analytical and bioanalytical chemistry 406 (17), pp. 4147–4156. DOI: 10.1007/s00216-014-7795-7.
  5. Kopra, Kari; Sharina, Iraida; Martin, Emil; Härmä, Harri (2020): Homogeneous single-label cGMP detection platform for the functional study of nitric oxide-sensitive (soluble) guanylyl cyclases and cGMP-specific phosphodiesterases. In Scientific reports 10 (1), p. 17469. DOI: 10.1038/s41598-020-74611-x.
  6. Kopra, Kari; Syrjänpää, Markku; Hänninen, Pekka; Härmä, Harri (2014): Non-competitive aptamer-based quenching resonance energy transfer assay for homogeneous growth factor quantification. In The Analyst 139 (8), pp. 2016–2023. DOI: 10.1039/C3AN01814H.
  7. Kopra, Kari; Valtonen, Salla; Mahran, Randa; Kapp, Jonas N.; Hassan, Nazia; Gillette, William et al. (2022): Thermal Shift Assay for Small GTPase Stability Screening: Evaluation and Suitability. In International journal of molecular sciences 23 (13). DOI: 10.3390/ijms23137095.
  8. Kopra, Kari; van Adrichem, Arjan J.; Salo-Ahen, Outi M.H.; Peltonen, Juha; Wennerberg, Krister; Härmä, Harri (2017): High-Throughput Dual Screening Method for Ras Activities and Inhibitors. In Analytical chemistry 89 (8), pp. 4508–4516. DOI: 10.1021/acs.analchem.6b04904.
  9. Kopra, Kari; Vuorinen, Emmiliisa; Abreu-Blanco, Maria; Wang, Qi; Eskonen, Ville; Gillette, William et al. (2020): Homogeneous Dual-Parametric-Coupled Assay for Simultaneous Nucleotide Exchange and KRAS/RAF-RBD Interaction Monitoring. In Analytical chemistry 92 (7), pp. 4971–4979. DOI: 10.1021/acs.analchem.9b05126.
  10. Latva, Martti et al., (1997): Correlation between the lowest triplet state energy level of the ligand and lanthanide(III) luminescence quantum yield. In Journal of Luminescence 75(2), pp149–169.
  11. Manoharan GB et al., (2019): High-throughput amenable fluorescence-assays to screen for calmodulin-inhibitors. In Analytical biochemistry 572:25–32.
  12. Syrjänpää M et al., (2019): QTR-FRET: Efficient background reduction technology in time-resolved Förster resonance energy transfer assays. In Analytica chimica acta1092:93–10
  13. Tong-Ochoa N et al.,(2015):Homogeneous single-label tyrosine kinase activity assay for high throughput screening.In Analytica chimica acta
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