Monoclonal antibodies (MAbs) were raised in mice against a bacterial f
usion protein composed of the intracellular serine/threonine kinase do
main of the type-2 activin receptor, ACTR2, fused to glutathione S-tra
nsferase. Three MAbs with high affinity toward the ACTR2 kinase domain
were isolated, one of which recognized specifically ACTR2 expressed t
ransiently in vascular endothelial cells. These reagents should be of
use in the elucidation of mechanisms of transmembrane signaling by thi
s member of the emerging receptor serine threonine kinase family.