The DOCK-C (also called Zir) subfamily of the dedicator of cytokinesis (DOCK) family of guanine nucleotide exchange factors function as activators of small GTPases. Dock7 was originally identified based on high sequence similarity to Dock180, the archetypal member of the DOCK family. It is also known as dedicator of cytokinesis protein 7, ZIR2, and KIAA1771. Like other DOCK proteins, Dock7 has a DHR1 domain that binds phospholipids, and a DHR2 domain containing the guanine nucleotide exchange activity. Dock7 expression has been reported in neurons and in HEK 293 cells. It binds the small GTPases Rac1 and Rac3, but does not bind Cdc42. Dock7 is required for proliferation and differentiation of neurocytes and glial cells. Dock7 has also been reported to interact with the hamartin-tuberin complex, which is disrupted in patients with of tuberous sclerosis.
These products are affinity-purified IgG antibodies that recognize human Dock7. The antibodies were raised in rabbit using synthetic peptides, and can be used for Western blot (WB) detection (Cat.# 28057, 28079), immunocytochemical (ICC) detection (Cat.# 28057), or immunoprecipitation (IP) (Cat.# 28057) of human Dock7.