The prescribing and dispensing of medication is currently a one-size fits all process and by association, the average pharmacy will contain an anthology of one-size fits all packets of 28 oral dose forms, which will be in turn labelled according to a pile of one-size-fits all prescriptions detailing rigidly indicated dosage regimens.The trouble is, unlike pharmaceutical dose forms, patients are not rigidly quality controlled by the pharmaceutical industry to ensure consistency. With evidence-based medicine, there has been a standardisation of patient care to a certain extent. When it comes to medicines however, we have to consider whether the clinical trials upon which we base our evidence and therefore compile the often strict prescribing guidelines in use by the National Health Service in the UK and other health systems internationally, are inherently flawed when they too are based upon the assumption that patients are homogenous in their response to medication.Despite the media hype which promised instant cures for cancer, heart disease and AIDS, the mapping of the human genome and the emerging science of "genomics" arguably represented nothing more than a complex and highly comprehensive DNA sequence. Accordingly, the tide of excitement very soon ebbed, leaving scientists on the shoreline to get on with unravelling its significance and applying emerging concepts to health and disease. As a result, genomics now has a rapidly growing family with which to apply functional analysis to the genome.As a consequence, we are now firmly embedded in the "omic" revolution. One of the new "omics" that has come to prominence is proteomics, which examines the downstream consequences of our genome, our proteins. Under the proteomics umbrella comes the subgroup of phosphoproteomics and secretomics.The secretome is the diverse type and number of proteins that are secreted or released from our cells and these are the types of proteins that are usually involved in cell migration, communication and signalling.Changes in the expression level and dysfunction in these types of proteins are often found in cancer. Many cellular proteins are switched on and off by kinase enzymes, for example, the tyrosine kinases (TKs), by the addition of phosphate groups. In disease, the pattern of phosphorylation is often found to be abnormal.Studying the phosphoproteome can help us to identify and establish which TK pathways are active in which particular cancers. As well as identifying novel therapeutic targets, knowledge of the TK signalling pathways