profiling of sera to discover new disease biomarkers; the monitoring of disease states and responses to therapy in personalized medicine; the monitoring of environment and food. Digital bioassay is an example of using protein microarray for diagnostic purposes. In this technology, an array of microwells on a glass/polymer chip are seeded with magnetic beads (coated with fluorescent tagged antibodies), subjected to targeted antigens and then characterised by a microscope through counting fluorescing wells. A cost-effective fabrication platform (using OSTE polymers) for such microwell arrays has been recently demonstrated and the bio-assay model system has been successfully characterised. Proteomics pertains to protein expression profiling i.e. which proteins are expressed in the lysate of a particular cell. Protein functional analysis is the identification of protein–protein interactions (e.g. identification of members of a protein complex), protein–phospholipid interactions, small molecule targets, enzymatic substrates (particularly the substrates of kinases) and receptor ligands. Antibody characterization is characterizing cross-reactivity, specificity and mapping epitopes. Treatment development involves the development of antigen-specific therapies for autoimmunity, cancer and allergies; the identification of small molecule targets that could potentially be used as new drugs. Challenges Despite the considerable investments made by several companies, proteins chips have yet to flood the market. Manufacturers have found that proteins are actually quite difficult to handle. Production of reliable, consistent, high-throughput proteins that are correctly folded and functional is fraught with difficulties as they often result in low-yield of proteins due to decreased solubility and formation of inclusion bodies. A protein chip requires a lot more steps in its creation than does a DNA chip. There are a number of approaches to this problem which differ fundamentally according to whether the proteins are immobilised through non-specific, poorly defined interactions, or through a specific set of known interactions. The former approach is attractive in its simplicity and is compatible with purified proteins derived from native or recombinant sources but suffers from a number of risks. Most notable amongst these relate to the uncontrolled nature of the interactions between each protein and the surface; at best, this might give rise to a heterogeneous population of proteins in which active sites are sometimes occluded by the surface; at worst, it might destroy activity altogether due to partial or complete surface-mediated unfolding of the immobilised protein. Challenges include: 1) finding a surface and a method of attachment that allows the proteins to maintain their secondary or tertiary structure and