Mouse ANGPTL3 Recombinant Protein (C-His) (MV176011)
概述
图片
参考文献
产品说明书
概述
货号
MV176011
品牌
abinScience
描述
Recombinant Mouse ANGPTL3 Protein, C-His (MV176011) expressed in Mammalian Cells, spanning Ser17-Thr206. Purity: >90% by SDS-PAGE.
Highlights
●His-Tagged — N-terminal 6×His tag for IMAC purification.
●Mammalian Expression — Proper folding and native glycosylation.
●High Purity — >90% purity verified by SDS-PAGE.
表达系统
Mammalian cells
Accession号
Q9R182
蛋白长度
Ser17-Thr206
应用
ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
种属
Mus musculus (Mouse)
性质
Recombinant
内毒素水平
Please contact with the lab for this information.
纯度
>90% as determined by SDS-PAGE.
预测分子量
24.81 kDa
状态
Lyophilized
保存溶液
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.
重悬
Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
运输
In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
稳定性和存储
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.
别名
ANG-5, ANGPT5, ANGPTL3, ANGPTL3(17-221), ANGPTL3(17-224), Angiopoietin-5, Angiopoietin-like protein 3, Angiopoietin-related protein 3
背景
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
