Agglucetin specifically causes platelet aggregation and surface exposure of integrin alpha-IIb/beta-3 with a GPIb-(GP1BA-) dependent manner in washed platelets. It binds to human platelets in a saturable manner, and its binding is specifically blocked by anti-GP Ib mAb. It regulates endothelial cell survival and promotes angiogenesis by activating integrin alpha-v/beta-3 signaling through FAK/phosphatidylinositol 3-kinase (PI3K)/Akt pathway. Heterotetramer of the subunits alpha-1, alpha-2, beta-1 and beta-2; disulfide-linked. Expressed by the venom gland. Belongs to the snaclec family. PubMed:22447656 describes a heterodimeric snaclec (named agkisacucetin) that is presented as being another protein than agglucetin, despite the very high sequence similarity. Agkisacucetin is described as an inhibitor of platelet aggregation, but no experimental data or cited references support this description. In addition, according to PubMed:22447656, agkisacucetin cannot be tetrameric, because cysteine residues are missing. However, non-covalently linked tetramers are found in snaclecs, as exemplified by rhodocetin.