Plexin B1 (C-terminal region) Antibody

Plexins are a family of large integral membrane proteins that complex with neuropilins to form semaphorin co-receptors. The extracellular region of plexins contains a semaphorin domain, multiple glycine-rich motifs, and MET-related sequences. The cytoplasmic region contains a Sex/Plexin domain and putative tyrosine phosphorylation sites that mediate signal transduction after activation. In addition, Plexin B1 and B2 contain cleavage sites for subtilisin-like proprotein convertases. These cleavage sites may be important for regulating assembly of heterodimeric receptors or release of the extracellular domain. Plexin-B1 is expressed as a 300 kDa precursor protein that can be cleaved into a 200 kDa a-subunit and a 100 kDa b-subunit. This plexin is the receptor for the class IV semaphorin, Sema-4D. Sema-4D activation of Plexin B1 recruits and activates c-Met, which can promote cell survival, migration, and angiogenesis

The antibody detects 300, 150, and 100 kDa* bands on SDS-PAGE immunoblots of mouse liver and rat PC12 cells. These bands correspond to the full length and proteolytically processed forms of Plexin B1. In mouse liver, this antibody detects 300 and 100 kDa forms of Plexin B1. This sequence has high homology with similar regions in rat and mouse Plexin B1, and has low homology to other plexin family members.