Human Angiostatin Kringle 1-3 Biotinylated Antibody

Angiostatin is a 38-45 kDa proteolytic fragment of plasminogen, a 92-100 kDa glycosylated blood zymogen that serves as the precursor for plasmin. Mature human plasminogen is 713 amino acids (aa) in length (aa 98-810). It contains five N-terminal kringle domains (aa 103-561) plus one peptidase S1 domain (aa 581-808). Upon cleavage by tPA between Arg580 and Val581, plasminogen is converted into the disulfide-linked two-subunit enzyme plasmin that dissolves fibrin clots. Plasminogen is also cleaved by MMPs which generate multiple fragments.  Angiostatin has documented antiangiogenic and antitumor activity, likely mediated by a down‑regulation of Bcl2, and an up‑regulation of thrombospondin-1. Over aa 98-358, human angiostatin shares 81% aa identity with mouse angiostatin.