Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.

ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.

The ANGPTL3 Human Recombinant is produced with N-terminal fusion of His-Tag. The Angiopoietin-like protein 3 His Tagged Fusion Protein is 26kDa containing 207 amino acid residues of the ANGPTL3 Human (26-233 a.a.) and 16 additional amino acid residues – His-Tag (underlined).

Escherichia Coli.

ANGPTL3 Human filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

Angiopoietin 5 purity is greater than 95% as determined by SDS-PAGE.

Add 0.2 ml of 0.1M Acetate buffer pH-4 and let the lyophilized pellet of ANGPTL3 Human dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of Angiopoietin 5 is limited.

Store lyophilized ANGPTL3 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Angiopoietin 5 can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

MRGSHHHHHH GMASHMSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL LQLGHGLKDF VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR RTTYKLQVKN EEVKNMSLEL NSKLESLLEE KILLQQKVKY LEEQLTNLIQ NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ TVEDQYKQLN QQHSQIKEIE NQLRRTSIQE PTEISLSSKP RAP.

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