Researchers routinely use GTP binding antibodies for the research of human disease. Thus it is worthwhile to provide a recap of the GTP binding process.
GTPases, a type of heterotrimeric G proteins, are essential to all metabolic functions. They act as molecular switches on the cell membrane, activating in response to various chemical signals. For example hormones, cytokines, physical stresses and cell-to-cell communications all activate downstream pathways. The interactions are complex, each requiring a different GTP protein. These function as molecular switches to activate or deactivate specific cellular responses.
G-proteins work by hydrolyzing GTP (guanosine triphosphate). They switch between active and inactive states, depending on whether they are GTP (guanosine triphosphate) or GDP (guanosine diphosphate) bound. In their active (GTP) state, they interact with effectors to initiate a downstream signal. In their GDP state this signal is non-functional.
G-protein activity is regulated by GEF (guanine-nucleotide exchange factor) activators, and GAP (GTPase-activating protein) ‘inactivators.’ We at Novus Biologicals have a full antibody database covering both activator and deactivator proteins.
GEF proteins translate signals from a variety of stimuli including G-protein-coupled receptors, receptor tyrosine kinases and adhesion molecules, to promote GTP binding and signal activation. The signals are terminated by GAP action, which promotes hydrolysis of GTP to GDP – thus returning the G-proteins to their inactive state. GDI (G-nucleotide dissociation inhibitors) regulators also exist, which are specific to the Rho/Rac and Rab sub-groups of G-proteins and also influence G-protein signaling via a GDP/GTP binding mechanism.
The use of antibodies to study G-proteins and their regulators is an important part of human disease research. We at Novus Biologicals have an enormous antibody database, to which new antibodies are constantly being added.
