ANGPTL-3 (Angiopoietin like protein 3) is a member of the angiopoietin family of structurally related proteins, characterized by a coiled N-terminal domain and a C-terminal fibrinogen like domain. It is primarily expressed in the liver and can exert activities related to both angiogenesis and lipid metabolism. ANGPTL-3 inhibits lipoprotein lipase (LPL) and endothelial lipase (EL), which has the effect of increasing plasma levels of triglycerides and HDL associated cholesterol. The fibrinogen like portion of the ANGPTL-3 protein can bind alpha-5/beta-3 integrins leading to endothelial cell adhesion and migration. Recombinant human ANGPTL-3 is a glycoprotein that migrates by SDS-PAGE analysis at an apparent molecular weight of 62 kDa, and contains 452 amino acid residues including a C-terminal His tag.
Angiopoietin-like protein 3, ANG-5, ANGPT5
SRIDQDNSSF DSLSPEPKSR FAMLDDVKIL ANGLLQLGHG LKDFVHKTKG QINDIFQKLN IFDQSFYDLS LQTSEIKEEE KELRRTTYKL QVKNEEVKNM SLELNSKLES LLEEKILLQQ KVKYLEEQLT NLIQNQPETP EHPEVTSLKT FVEKQDNSIK DLLQTVEDQY KQLNQQHSQI KEIENQLRRT SIQEPTEISL SSKPRAPRTT PFLQLNEIRN VKHDGIPAEC TTIYNRGEHT SGMYAIRPSN SQVFHVYCDV ISGSPWTLIQ HRIDGSQNFN ETWENYKYGF GRLDGEFWLG LEKIYSIVKQ SNYVLRIELE DWKDNKHYIE YSFYLGNHET NYTLHLVAIT GNVPNAIPEN KDLVFSTWDH KAKGHFNCPE GYSGGWWWHD ECGENNLNGK YNKPRAKSKP ERRRGLSWKS QNGRLYSIKS TKMLIHPTDS ESFEHHHHHH HH
Greater than 98% by SDS-PAGE gel and HPLC analyses.
Measured by its binding ability to recombinant αvβ3 integrin in a functional ELISA.