This LPL protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
LPL is a crucial enzyme involved in lipid metabolism. It is abundantly expressed and plays a significant role in various physiological processes. LPL is involved in the metabolism and transport of lipids, particularly triglycerides [1]. LPL regulates the hydrolysis of triglyceride-rich lipoproteins in the circulation, generating fatty acids for storage or energy utilization [2].
Moreover, LPL has been implicated in atherosclerosis. Studies have shown that LPL deficiency can lead to dysregulation of lipid homeostasis, resulting in conditions like hyperlipoproteinemia [3]. Additionally, LPL deficiency has been associated with the down-regulation of endothelial GPIHBP1 expression, impacting LPL metabolism and function [4].
Furthermore, LPL is regulated by phosphorylation, with non-phosphorylatable forms exhibiting distinct phenotypes during processes like podosome formation and phagocytosis [5]. It is also subject to translational regulation by factors like protein kinase C [6].
References:
[1] L. Gan, J. Xu, D. Liu, Q. Ding, M. Liu, R. Chenet al., Regulation of plasma lipid homeostasis by hepatic lipoprotein lipase in adult mice, The Journal of Lipid Research, vol. 57, no. 7, p. 1155-1161, 2016. https://doi.org/10.1194/jlr.m065011
[2] R. Unal, I. Pokrovskaya, P. Tripathi, B. Monia, P. Kern, & G. Ranganathan, Translational regulation of lipoprotein lipase in adipocytes: depletion of cellular protein kinase cα activates binding of the c subunit of protein kinase a to the 3′-untranslated region of the lipoprotein lipase mrna, Biochemical Journal, vol. 413, no. 2, p. 315-322, 2008. https://doi.org/10.1042/bj20071559
[3] S. Kaser, A. Sandhofer, B. Hölzl, R. Gander, C. Ebenbichler, B. Paulweberet al., Phospholipid and cholesteryl ester transfer are increased in lipoprotein lipase deficiency, Journal of Internal Medicine, vol. 253, no. 2, p. 208-216, 2003. https://doi.org/10.1046/j.1365-2796.2003.01091.x
[4] N. Vaziri, J. Yuan, Z. Ni, S. Nicholas, & K. Norris, Lipoprotein lipase deficiency in chronic kidney disease is accompanied by down-regulation of endothelial gpihbp1 expression, Clinical and Experimental Nephrology, vol. 16, no. 2, p. 238-243, 2011. https://doi.org/10.1007/s10157-011-0549-3
[5] X. Lin, P. Krishnamoorthy, E. Walker, H. Joshi, & S. Morley, Expression of non-phosphorylatable s5a-l-plastin exerts phenotypes distinct from l-plastin deficiency during podosome formation and phagocytosis, Frontiers in Cell and Developmental Biology, vol. 11, 2023. https://doi.org/10.3389/fcell.2023.1020091
[6] G. Ranganathan, R. Kaakaji, & P. Kern, Role of protein kinase c in the translational regulation of lipoprotein lipase in adipocytes, Journal of Biological Chemistry, vol. 274, no. 13, p. 9122-9127, 1999. https://doi.org/10.1074/jbc.274.13.9122
