Galactose-binding lectin which recognizes specific carbohydrate structures and agglutinates a variety of animal cells by binding to cell-surface glycoproteins and glycolipids. Calcium-dependent lectin. Also binds lactose and raffinose (PubMed:28003128). Shows high hemagglutinating activity on mammalian erythrocytes (Ref.5, PubMed:16309723). It also involved in immunological functions, since it is able of inducing potent neutrophil activation (PubMed:21266049, PubMed:16309723). In vivo, it causes edema and increases vascular permeability after injection into mouse hind paws (10-100 ug/paw). In anesthetized rats, it decreases the blood pressure by approximately 15%, with a rapid return to the resting level (PubMed:16309723). Is an effective inhibitor of cell growth in some cancer cell lines, especially against renal and pancreatic cancer cell lines, human breast and ovarian carcinoma, glioblastoma and a bovine brain microvascular endothelial cell line (PubMed:10628348, PubMed:11478954). Hemagglutination activity is inhibited by lactose (MIC=2.5 mM), galactose (MIC=10 mM), and raffinose (Ref.5, PubMed:16309723, PubMed:28003128). Is very weakly or not inhibited by gentamicin, kanamycin, glucose and sucrose (PubMed:16309723, PubMed:28003128). Homodecamer of disulfide-linked dimers arranged in two 5-fold symmetric pentamers (Ref.5, PubMed:28003128). Binds the gentamicin group of aminoglycoside antibiotics at the dimeric interface near the intermolecular disulfide bond (PubMed:28003128). Expressed by the venom gland. Can be used in the treatment of bovine mastitis, since it is able to both inhibit bacterial biofilm growth, and disrupt existing biofilm, without affecting bacterial cell viability. The lectin (up to 200 microg/ml) does not aggregate human platelet-rich plasma (PRP) or washed platelets (WP), nor does it alter the aggregation induced by ADP in PRP or by thrombin in WP. Belongs to the true venom lectin family. Truncated N-terminus.