

| Catalog No. | MV176011 |
|---|---|
| Description |
Recombinant Mouse ANGPTL3 Protein, C-His (MV176011) expressed in Mammalian Cells, spanning Ser17-Thr206. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | Mammalian cells |
| Accession | Q9R182 |
| Protein length | Ser17-Thr206 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Mus musculus (Mouse) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Predicted molecular weight | 24.81 kDa |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Alternate Names | ANG-5, ANGPT5, ANGPTL3, ANGPTL3(17-221), ANGPTL3(17-224), Angiopoietin-5, Angiopoietin-like protein 3, Angiopoietin-related protein 3 |
| Background | Angiopoietin-related protein 3 is a ~52 kDa protein. Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake. Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity; the function seems to be specific for the feeding conditions. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1. Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids; the cleaved N-terminal domain is more efficient than the uncleaved proprotein. 1. Koishi, R. et al. (2002) Nature genetics 30, 151-7. PMID: 11788823 2. Ando, Y. et al. (2003) Journal of lipid research 44, 1216-23. PMID: 12671033 3. Wang, Y. et al. (2015) Proceedings of the National Academy of Sciences of the United States of America 112, 11630-5. PMID: 26305978 4. Ono, M. et al. (2003) The Journal of biological chemistry 278, 41804-9. PMID: 12909640 5. Köster, A. et al. (2005) Endocrinology 146, 4943-50. PMID: 16081640 6. Liu, J. et al. (2010) The Journal of biological chemistry 285, 27561-70. PMID: 20581395 7. Jin, W. et al. (2007) Cell metabolism 6, 129-36. PMID: 17681148 8. Wang, Y. et al. (2015) Journal of lipid research 56, 1296-307. PMID: 25954050 9. Kim, HK. et al. (2015) Diabetes 64, 1142-53. PMID: 25338813 |
| Note | For research use only |
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