Laboratory Robotics and Automation最新文献

Homogeneous time-resolved fluorescence (HTRF®) assays are ideal for miniaturization in high-throughput screening. HTRF assays can be scaled down from 200 μL reactions to 25 to 70 μL reactions without loss of sensitivity. Three assay formats using proprietary europium cryptate, (Eu)K, and XL665 are described. An HTRF tyrosine kinase assay illustrates the indirect assay format. Inhibition can be detected with enzyme concentrations as low as 20 pM. An HTRF receptor-ligand binding assay is used to show a direct assay format. Reproducibility and stability are shown by a comparison of competitive binding curves under varying assay conditions. An HTRF reverse transcriptase assay is described to show the semidirect assay format. Enzyme concentrations were varied and compared with a typical [³²P]-labeled assay. All three assay formats have been optimized using HTRF reagents. Results, measured in the highly sensitive Discovery® HTRF microplate analyzer, show that the sensitivity of HTRF is maintained when converting from 96-well format to 384-well format, despite the decrease in volume of reagents. © 1999 John Wiley & Sons, Inc. Lab Robotics and Automation 11: 324–329, 1999

Laboratório Fleury is a reference clinical laboratory performing more than 1,200 different laboratory tests, with a workload of 3.5 million tests in 1998. With 60% of this workload directed to our clinical chemistry section, we started a project three years ago to evaluate the possibility of an automation system to fulfill our needs of quality, increased productivity, and as a base for further increases in workload. A workforce was assembled, and after detailed studies of our necessities and possibilities as well as an extensive program of visits and contacts in the U.S., Europe, and Japan, a final solution was settled.The system is being manufactured by IDS, Japan, and will be delivered by April 1999. It includes an inlet unit, an error lane, a decapper, a waiting line, a retrieve unit, a sorting table, a recapper unit, and an outlet unit. One of the main characteristics of our system is that it can be easily upgraded in order to receive more machines and/or more samples. © 1999 John Wiley & Sons, Inc. Lab Robotics and Automation 11: 335–337, 1999

In the manufacturing sector, computer simulation has been used for many years to support complex decisions such as automation of processes or planning new factories. Clinical laboratories and diagnostic manufacturers are also faced with the challenges of automation and process redesign that will fundamentally change the way work is performed and the net economic impact of those changes. The question arises as to how we can minimize the risks, explore options, and make the right decisions. In this report, we present an overview of how simulation modeling can assist with laboratory decision making. © 1999 John Wiley & Sons, Inc. Lab Robotics and Automation 11: 312–315, 1999

Knowing how and when to implement new technology is an ongoing challenge in highly competitive, innovation-driven industries such as chemicals and electronics. Using the emerging field of combinatorial materials science as the primary example, this discussion enumerates, describes, and illustrates the seven specific stages a company must go through in the successful adoption and assimilation of innovation. These stages, as depicted over a single S curve, include: awareness, acquisition, application, acceptance, communication, assimilation, and incremental iteration. The competitive advantages of early technology adoption are described, as are the issues involved in implementing a combinatorial, or high-speed, approach to new materials discovery. © 1999 John Wiley & Sons, Inc. Lab Robotics and Automation 11: 330–334, 1999

Determining the complete DNA sequence of an organism is a complex and time-consuming project. Automation, especially of front-end procedures, has been used to reduce the time and costs of genome projects. The BioRobot™ 96OO is a multipurpose robotic system that facilitates high-throughput genome sequencing by reducing sample handling and integrating multiple steps on the same workstation. © 1999 John Wiley & Sons, Inc. Lab Robotics and Automation 11: 316–319, 1999

This article describes a new design of a urea biosensor developed by covalent immobilization of the enzyme urease on the top of a nickel-hexacyanoferrate-modified nickel electrode. The behavior of the electrode was described with respect to several experimental parameters in flow injection mode. Detection of urease-produced NH ion from parent urea at a working potential of 100 mV vs. a Ag/AgCl/2 M NaCl electrode showed linearity in the concentration range of urea in aqueous solutions from 10 μM to 10 mM. The influence of carrier electrolyte concentration, flow rate, and pH on the properties of the transducer were also examined. The selectivity recognition of the transducer was studied with respect to the influence of potentially interfering sodium and potassium ions. The electrode was tested over a period of 45 days. After this period, the biosensor lost only 20% of its sensitivity. © 1999 John Wiley & Sons, Inc. Lab Robotics and Automation 11: 266–271, 1999