To develop and validate a reliable, robust and efficient assay to detect and quantify biologic compounds and during early stage of a biotherapeutic agent discovery. An enrichment-free immunoassay method was developed to quantify a polyhistidine N- and FLAG C-terminally-tagged recombinant protein of ∼55 kDa. The target proteins were purified by a nickel-based matrix via tag affinity, followed by probing with biotinylated antitag antibody and subsequently detected by streptavidin-horseradish peroxidase conjugate using an automated capillary-based western system. A simple, highly sensitive and efficient immunoassay protocol was established to assess the stability and pharmacokinetic properties of propitious recombinant proteins in mouse to support early stage development of a biotherapeutic lead.
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