Potent platelet activator that aggregates platelets via both GPIb (GP1BA/GP1BB) and GPVI (GP6). Alboluxin induces a tyrosine phosphorylation profile in platelets that resembles those produced by collagen and convulxin, involving the time dependent tyrosine phosphorylation of Fc receptor gamma chain (FCGR1A), phospholipase Cgamma2 (PLCG2), LAT and p72SYK. Inhibition of alpha-IIb/beta-3 reduces the aggregation response to alboluxin, as well as tyrosine phosphorylation of platelet proteins, showing that activation of alpha-IIb/beta-3 and binding of fibrinogen are involved in alboluxin-induced platelet aggregation and it is not simply agglutination. Trimer of 3 heterodimers of alpha and beta subunits; disulfide-linked. Expressed by the venom gland. The complex may be glycosylated. May not activate platelet via the integrin alpha-2/beta-1, since antibodies against this integrin have no effect. Belongs to the snaclec family. The subunit alpha may be blocked, since it was impossible to sequence.