The ability of Src-family kinases (SFKs) to mediate signaling from cell surface receptors in hematopoietic cells is a function of their catalytic activity, location and binding partners. Kinase activity is regulated in the cell by kinases and phosphatases that alter the state of phosphorylation of key tyrosine residues and by protein binding partners that stabilize the kinase in active or inactive conformations or localize the enzyme to specific subcellular or submembrane domains. Kinase activity and function can be modulated experimentally through the use of small molecule inhibitors designed to directly target catalytic or binding domains or regulate the location of the protein by altering its state of acylation.