| Description | This entry represents Secapin; a nontoxic peptide found in the venom of bees and wasps, a serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities against bacteria and fungi [ ]. It may function in the innate immune response to microbial infection and possibly in the venom, as an antifibrinolytic agent []. Secapin shares a common folding pattern with apamin, mast cell degranulating peptide and tertiapin; it is centred on a β-turn covalently linked to an α-helical segment by one disulphide link (two disulphide links in the other peptides) []. Secapin-2 induces hyperalgesia and edema mediated by leukotrienes when injected into mice and it does not induce hemolytic activity, mast cell degranulation, or chemotactic activity for polymorphonucleated leukocytes (PMNL) []. | Name | Secapin |
| Short Name | Secapin | Type | Family |
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