As research efforts shift from the gene to the protein, scientists are actively engaged in studying protein functions and interactions with other biomolecules to learn more about cellular processes. This report evaluates the cutting-edge technologies that life scientists use to study biomolecular interactions and complexes in vitro. This critical information will help marketing professionals and product developers better understand the users' level of satisfaction with the technologies available, the definition of quality from the users' perspective and the unmet needs of the customers and clients. Two predominant methods for identifying biomolecular interactions and complexes in vitro are protein microarrays and microfluidics lab-on-a-chip. These technologies allow scientists to study the specificity of binding between two biomolecules, the concentration of a biomolecule present, the rate of association/dissociation and the affinity for binding. Features sought after in this array-based technology include low non-specific binding, reproducibility, high chemical stability, stable baselines and flexibility. In the field of microfluidics, scientists look for systems that require low sample consumption, the capability for simultaneous experimental runs, increased temperature stability and the ability to analyze surface ligand concentrations and contact times. Proteomics has created the demand for new experimental designs that allow for the evolution of conventional, hands-on and multi-apparatus lab investigations into micro-scale, automated and integrated analyses. Array-based and microfluidic technologies meet this demand by accelerating laboratory experiments in an efficient and cost-saving manner. Although these are relatively new technologies, improvements to protein microarray and microfluidics lab-on-a-chip are already being developed. These advances have allowed for increased experimental efficiency and higher quality results. The final report is based on the opinions of a worldwide panel of research scientists. It provides you with the answers needed to better serve the protein science market and is available at a fraction of what it would cost to conduct a custom study similar in size and scope. Biomolecular Interactions (In Vitro Methods) is designed as the eighth installment in our series-which details all aspects of protein research-and specifically focuses on the well-established in vitro methods for identifying biomolecular interactions and complexes. As companies strive to meet the demand for high-throughput protein identification, characterization and screening, they must have access to the latest information about the science being conducted at the forefront of technology. Report Highlights More than 330 researchers studying biomolecular interactions using in vitro methods participated in this survey between November 26 and December 5, 2001. The report details findings for each and every question in the survey. Below is a glimpse of some of the findings derived from different questions: Currently only a small percentage of protein scientists employ protein chip technology, although 41% have plans to use it within 12 months. Protein microarrays will permit researchers to scan thousands of proteins in a variety of proteomic experiments, including "comparing protein expression patterns" and "assessing protein-protein interactions." Half of the protein researchers surveyed report that a "faster analysis time" is the major factor influencing their decision to embrace microarrays in their protein research. "High resolution acquisition" is the factor that is most important in a lab's decision to select one type of scanner over another. One quarter of the survey participants use protein microarray technology on a daily basis. Few protein scientists use microfluidics technology for protein research, but 20% have plans to use it within the next 12 months. "Increased precision and accuracy" is the most important factor in the decision to use microfluidics lab-on-a-chip technology. (Electronic copy also includes 1 print copy) |