Protein Interaction and Dynamics Facility
The Protein Interaction and Dynamics facility is equipped to discover and analyze protein biomarkers from biological samples and to measure protein-protein and protein-ligand interactions in a multiplex format.
A Ciphergen Protein Chip System with PBS II series Reader separates, detects and analyzes proteins at the femtomole level directly from biological samples.
Facility Director: William Morgan, Ph.D. Email: MorganWT@umkc.edu Phone: (816)235-2596 Research profile Description of services with pricing information (pdf file)
The Ciphergen ProteinChip® System with PBS II series Reader separates, detects and analyzes proteins at the femtomole level directly from biological samples. The proteins are captured and analyzed on ProteinChip Arrays using the ProteinChip Reader and dedicated software for data analysis. Chip surfaces are designed to bind hydrophobic, hydrophilic (cation or anion) or specific ligands. The system enables "on-chip" biomarker discovery, expression profiling, purification, characterization and functional analysis of proteins and protein-biomolecule interactions.
The signal amplification produced by the protein capture and micropurification is analogous to searching for "a needle in a haystack" by capturing the needles and washing away the hay. Detection of the purified proteins is performed by Laser Desorption / Ionization Time-Of-Flight mass analysis (MALDI-TOF). Chemical and biochemical processing can be included at any step throughout the SELDI (Surface-Enhanced Laser Desorption/Ionization) process to greatly enhance the detailed knowledge gained from a set of experiments.
Qiagen LiquiChip System Workstation (Reader, Microplate Handler, and Fluid Module carries out high-throughput, multiplex, homogeneous assays of analytes in a bead-based protein interaction format. LiquiChip beads are used to immobilize capture molecules, and immobilization technology for 6xHis-tagged proteins using metal chelates or penta·his antibodies, for biotinylated capture molecules using avidin, and for capture molecules amenable to carbodiimide coupling chemistry.
LiquiChip assays are based on xMAP technology and involve the interaction of immobilized, bead-bound capture molecules with a reaction partner (analyte) in solution. A reporter molecule, specific for the analyte, is used to quantify the interaction. Analytes free in solution interact with bead-bound capture molecules and are detected using reporter molecules specific for the analyte. Assays of all types of molecular recognition and multi-molecular interactions are feasible (e.g. antigen-antibody, protein-protein interactions, enzyme assays, receptor-ligand assays, protein-nucleic acid assays) making the system very versatile. Using competitive assay techniques, even unlabeled interaction partners can be screened by measuring the decrease of signal. Moreover, the system can rapidly assay up to 100 different analytes in a single sample.
