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• W2091874744 abstract "Altered serum levels of TIMP-1 are an indicator of various pathological states. To quantitate TIMP-1 in biological samples, we have previously isolated TIMP-1 specific single-chain Fv fragments (scFvs) using phage-display. In the work presented here, we have used these scFvs to establish a TIMP-1 ELISA based exclusively on recombinant scFv fusion proteins.Two distinct TIMP-1 specific scFvs were used as the antigen binding components after being genetically fused to the N-termini of two different fusion protein constructs. One fusion protein, comprising a CL domain, serves as a coating reagent, while the second fusion protein with a modified form of bacterial alkaline phosphatase is used as a detection reagent. A double antibody sandwich-ELISA was then established and optimized.An ELISA for the quantitation of tissue inhibitor of metalloproteinase (TIMP)-1, based entirely on recombinant antibody fragments, was developed as an alternative to assays using polyclonal antisera or monoclonal antibodies. Its performance was shown to compare well with a conventional ELISA. Finally, TIMP-1 concentrations in the sera of sixty healthy individuals were determined.The assay described here provides a standardized, reliable and readily available means of quantitation of TIMP-1 in a large number of blood samples." @default.
• W2091874744 created "2016-06-24" @default.
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• W2091874744 date "2003-09-01" @default.
• W2091874744 modified "2023-10-06" @default.
• W2091874744 title "An ELISA for the detection of TIMP-1 based on recombinant single chain Fv fusion proteins" @default.
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• W2091874744 doi "https://doi.org/10.1016/s0009-8981(03)00281-x" @default.
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