Picture of wind turbine against blue sky

Open Access research with a real impact...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

The Energy Systems Research Unit (ESRU) within Strathclyde's Department of Mechanical and Aerospace Engineering is producing Open Access research that can help society deploy and optimise renewable energy systems, such as wind turbine technology.

Explore wind turbine research in Strathprints

Explore all of Strathclyde's Open Access research content

Immunoassay for P38 MAPK using surface enhanced resonance Raman spectroscopy (SERRS)

Douglas, P. and Stokes, R.J. and Graham, D. and Smith, W.E. (2008) Immunoassay for P38 MAPK using surface enhanced resonance Raman spectroscopy (SERRS). Analyst, 133 (6). pp. 791-796. ISSN 0003-2654

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

A micro-bead sandwich assay for P38 mitogen-activated protein kinase using surface enhanced resonance Raman spectroscopy (SERRS) detection is reported. Monoclonal capture antibodies were immobilised on a solid phase of magnetic micro-beads with secondary detection using a rhodamine-labelled antibody. Quantitative SERRS detection of the secondary antibody was possible with a limit of detection of 9.5 × 10−12 mol dm−3. The sandwich assay was quantitative and sensitive to 6 ng ml−1. The mechanism of the SERRS detection in the immunoassay was investigated. The addition of SERRS aggregating agents causes the dissociation of the immuno-complex from the magnetic beads. Scanning electron microscopy images indicate that the colloidal suspension rather than adsorbed silver nanoparticles on the beads provide the SERRS signals, that the aggregate size is partially controlled and that there is some inhomogeneity in the distribution of organic matter on the nanoscale. (Abstract from: http://www.swetswise.com/eAccess/viewAbstract.do?articleID=36962529)