| Description : |
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. |
| Source : |
E.coli |
| Species : |
Human |
| Tag : |
His |
| Form : |
ANGPTL3 Human filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4. |
| Molecular Mass : |
26 kDa |
| Protein length : |
26-233 a.a. |
| AA Sequence : |
MRGSHHHHHH GMASHMSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL LQLGHGLKDF VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR RTTYKLQVKN EEVKNMSLEL NSKLESLLEE KILLQQKVKY LEEQLTNLIQ NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ TVEDQYKQLN QQHSQIKEIE NQLRRTSIQE PTEISLSSKP RAP. |
| Purity : |
> 95% as determined by SDS-PAGE. |
| Notes : |
Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. |
| Storage : |
Stored at -20 centigrade. |
| Reconstitution : |
Soubility: 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. |
