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Progress report on Homogeneous Assay project
July 24, 2006International medical diagnostics company Panbio Limited today announced that it has achieved some encouraging results in the development of its Homogeneous Assay Technology.
The company's Advanced Technologies Division has developed a pair of pre-prototype assays for HSV-1 and HSV-2 antibody detection.* The key achievements of this development are:
- The results obtained were based on real samples whereas, earlier in the project, results were based on a model assay; and
- The results obtained were consistent with those obtained when using the current ELISA technology.
The company was also pleased that, at this early stage in the project, the results were obtained in less than 50% of the time taken on current ELISA technology.
The development of the assays has also enabled the project team to demonstrate that the design of the antigen used in the assay can have a positive impact on its performance despite the presence of potentially interfering substances in the sera used for testing.
Paul Nitz, Panbio Chief Executive Officer said, "We are pleased with the progress the project team has made. While a number of technical challenges remain, these results increase our confidence of reaching our next goal which is to produce a prototype assay for pre-clinical evaluation by the end of 2006."
Panbio will be presenting a poster at the American Association of Clinical Chemistry (AACC) meeting in Chicago on July 27 outlining the development of the Homogeneous Assay technology to date. The AACC meeting is one of the premier meetings in the world for the medical diagnostics industry. The company will be discussing the progress of the project with a number of potential licensees of the technology.
Research Australia
- The results obtained were consistent with those obtained when using the current ELISA technology.
The company was also pleased that, at this early stage in the project, the results were obtained in less than 50% of the time taken on current ELISA technology.
The development of the assays has also enabled the project team to demonstrate that the design of the antigen used in the assay can have a positive impact on its performance despite the presence of potentially interfering substances in the sera used for testing.
Paul Nitz, Panbio Chief Executive Officer said, "We are pleased with the progress the project team has made. While a number of technical challenges remain, these results increase our confidence of reaching our next goal which is to produce a prototype assay for pre-clinical evaluation by the end of 2006."
Panbio will be presenting a poster at the American Association of Clinical Chemistry (AACC) meeting in Chicago on July 27 outlining the development of the Homogeneous Assay technology to date. The AACC meeting is one of the premier meetings in the world for the medical diagnostics industry. The company will be discussing the progress of the project with a number of potential licensees of the technology.
Research Australia
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Homogeneous non-competitive bioaffinity assay based on fluorescence resonance energy transfer [An article from: Analytica Chimica Acta] by T. Kokko (Author), L. Kokko (Author), T. Soukka (Author), T. Lovgren (Author) This digital document is a journal article from Analytica Chimica Acta, published by Elsevier in 2007. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser. Description: A homogeneous non-competitive assay principle for measurement of small analytes based on quenching of fluorescence is described. Fluorescence resonance energy transfer (FRET) occurs between the donor, intrinsically fluorescent europium(III)-chelate conjugated to streptavidin, and the acceptor, quencher dye conjugated to biotin derivative when the biotin-quencher is bound to Eu-streptavidin. Fluorescence can be measured only from those streptavidins that are bound to biotin of the sample, while the fluorescence... |
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A novel homogeneous assay format utilising proximity dependent fluorescence energy transfer between particulate labels [An article from: Analytica Chimica Acta] by A. Valanne (Author), H. Lindroos (Author), T. Lovgren (Author), T. Soukka (Author) This digital document is a journal article from Analytica Chimica Acta, published by Elsevier in 2005. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser. Description: Particle labels feature considerably higher specific activity than small molecule labels due to high number of label molecules incorporated in one unit. We developed a novel homogeneous assay relying on time-resolved detection of fluorescence energy transfer between particulate labels. The long-lifetime fluorescent Eu(III)-chelate-doped donor nanoparticles and the prompt near-infrared fluorescent TransFluoSphere(TM) acceptor particles possess high specific activity, resulting in great sensitivity potential. The... |
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Homogeneous assay based on low quantum yield Sm(III)-donor and anti-Stokes' shift time-resolved fluorescence resonance energy-transfer measurement [An article from: Analytica Chimica Acta] by V. Laitala (Author), I. Hemmila (Author) This digital document is a journal article from Analytica Chimica Acta, published by Elsevier in . The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser. Description: Non-overlapping fluorescence resonance energy-transfer (nFRET) is a highly sensitive, time-resolved, assay technology. It utilizes lanthanide chelates as donors together with non-overlapping acceptor fluorophores, which have their absorption maximum energetically at a higher level than the emittive transitions of the donor. In this report the nFRET was studied using a low quantum yield Sm(III)-chelate as the donor in a homogeneous dF508-DNA hybridization assay. Despite the low quantum yield, Sm(III) could function... |
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Homogeneous chemiluminescent assays for free choline in human plasma and whole blood [An article from: Analytica Chimica Acta] by M. Adamczyk (Author), R.J. Brashear (Author), P.G. Mattingly (Author), Tsatso (Author) This digital document is a journal article from Analytica Chimica Acta, published by Elsevier in 2006. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser. Description: Choline was oxidized in the presence of choline oxidase and the hydrogen peroxide generated was detected using a chemiluminescent acridinium-9-carboxamide. The dose response for choline (0-150@mM) was established in buffer and was validated for the quantification of choline in human plasma and whole blood. This homogeneous assay was performed in a 96-well microplate format and required minimal sample volume (4@mL) and short analysis time (0.98, plasma; R>0.97, whole blood) with LC-MS/MS.... |
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Homogeneous, unmodified gold nanoparticle-based colorimetric assay of hydrogen peroxide [An article from: Analytica Chimica Acta] by Z.S. Wu (Author), S.B. Zhang (Author), M.M. Guo (Author), C.R. Chen (Author), G. Shen (Author) This digital document is a journal article from Analytica Chimica Acta, published by Elsevier in 2007. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser. Description: An unmodified gold nanoparticle-based colorimetric assay system in homogeneous format has been developed using hydrogen peroxide (H"2O"2) as a model analyte. H"2O"2 is added to o-phenylenediamine/horseradish peroxidase solution, and allowed to react for 10min. Then, unmodified gold nanoparticles that serve as ''reaction indicators'' are added to the reaction solution. The resulting mixture color changes dramatically from red to blue. The reason is that azoaniline, a horseradish peroxidase-catalyzed oxidation... |
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Homogeneous time-resolved fluorescence assays for the detection of activity and inhibition of phosphatase enzymes employing phosphorescently labeled peptide ... [An article from: Analytica Chimica Acta] by D.J. O'Shea (Author), T.C. O'Riordan (Author), P.J. O'Sullivan (Author), Papk (Author) This digital document is a journal article from Analytica Chimica Acta, published by Elsevier in 2007. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser. Description: A rapid, homogenous, antibody-free assay for phosphatase enzymes was developed using the phosphorescent platinum (II)-coproporphyrin label (PtCP) and time-resolved fluorescent detection. An internally quenched decameric peptide substrate containing a phospho-tyrosine residue, labeled with PtCP-maleimide and dabcyl-NHS at its termini was designed. Phosphatase catalysed dephosphorylation of the substrate resulted in a minor increase in PtCP signal, while subsequent cleavage by chymotrypsin at the dephosphorylated... |
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