Recombinant Mouse Lipoprotein Lipase (LPL) Protein (His&Myc)

Name: Recombinant Mouse Lipoprotein Lipase (LPL) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-05038P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Lipoprotein Lipase (LPL) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P11152
Target Symbol	LPL
Synonyms	Lpl; Lipoprotein lipase; LPL; EC 3.1.1.34
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	ADAGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSG
Expression Range	28-474aa
Protein Length	Full Length of Mature Protein
Mol. Weight	57.3 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.
Subcellular Location	Cell membrane; Peripheral membrane protein; Extracellular side. Secreted. Secreted, extracellular space, extracellular matrix.
Protein Families	AB hydrolase superfamily, Lipase family
Database References	KEGG: mmu:16956 STRING: 10090.ENSMUSP00000015712 UniGene: PMID: 29615667 the negatively charged IDR of GPIHBP1 traverses a vast space, facilitating capture of LPL by capillary endothelial cells and simultaneously contributing to GPIHBP1's ability to preserve LPL structure and activity. PMID: 29899144 LPL in the hypothalamus is an important regulator of body weight and glucose homeostasis PMID: 28456865 These results identify LPL as an important regulator of fatty acid transport to skeletal compartments and demonstrate an intricate functional link between systemic and skeletal fatty acid and glucose metabolism. PMID: 28608812 mutation of a conserved cysteine in GPIHBP1 abolishes the ability of GPIHBP1 to bind LPL PMID: 28476858 The data suggests that ANGPTL3 is part of the machinery causing dyslipidemia majorily via LPL inhibition in mastitis mice. PMID: 29104012 Using in vitro ketosis model by glucose starvation, studied inhibition of ketosis by momilactone B. Found momilactone B could regulate the angiopoietin-like-3 (ANGPTL3)-lipoprotein lipase (LPL)pathway, and suppressed the expression of HMGCS2 through the increased expression of STAT5b. PMID: 27874312 physiological changes in adipose tissue ANGPTL4 expression during fasting and cold resulted in inverse changes in the amount of mature-glycosylated LPL in wild-type mice, but not Angptl4(-/-) mice. We conclude that ANGPTL4 promotes loss of intracellular LPL by stimulating LPL degradation after LPL processing in the endoplasmic reticulum (ER). PMID: 27034464 LPL moved quickly from heparan sulfate proteoglycans (HSPGs) on adipocytes to GPIHBP1-coated beads, thereby depleting LPL stores on the surface of adipocytes. We conclude that HSPG-bound LPL in the interstitial spaces of tissues is mobile, allowing the LPL to move to GPIHBP1 on endothelial cells PMID: 27811232 our study reveals that hepatic LPL is involved in the regulation of plasma LPL activity and lipid homeostasis. PMID: 27234787 The induction of LPL activity by fasting in core transgenic mice activated PPARalpha downstream target genes that are involved in fatty acid beta-oxidation. PMID: 27665576 This study shows that TNF-alpha, by a Foxo1 dependent pathway, increases the transcription of ANGPTL4 which is secreted by the cells and causes inactivation of LPL. PMID: 28215713 Our findings suggest that neuronal LPL is involved in the regulation of body weight and composition in response to either the change in quantity (HF feeding) or quality (n-3 PUFA-enriched) of dietary fat PMID: 27282869 An LPL structural model suggests that the LPL S447X truncation exposes residues implicated in LPL binding to lipoprotein binding uptake receptors, such as GPIHBP1. PMID: 27984852 feeding induces lipasin, activating the lipasin-Angptl3 pathway, which inhibits LPL in cardiac and skeletal muscles to direct circulating TAG to WAT for storage PMID: 26687026 MiR-590 agomir down-regulates LPL mRNA and protein expression in a mouse model of atherosclerosis. PMID: 26397958 Deficiency of Lipoprotein Lipase in Neurons Decreases AMPA Receptor Phosphorylation and Leads to Neurobehavioral Abnormalities in Mice PMID: 26263173 Systemic LPL deletion results in impaired glucose tolerance, whole-body and tissue-specific insulin resistance, which is associated with tissue lipid deposition in various insulin target tissues PMID: 25635326 Results indicated that aggregation of alpha-syn and reduction of UCHL1 expression in LPL-deficient mice may affect synaptic function. PMID: 25595992 the amount of LPL expressed in muscle and heart governed both the binding of chylomicron particles and the assimilation of chylomicron lipids in the tissue. PMID: 25589507 Maternal overnutrition induces LPL expression in trophoblasts by reducing the inhibitory effect of SIRT1 on PPARgamma. PMID: 25948680 Lipoprotein lipase is an important modulator of lipid uptake and storage in hypothalamic neurons. PMID: 26265042 Results suggest that impaired synaptic vesicle recycling results from deficient docosahexaenoic acid and arachidonic acid and contributes to the presynaptic dysfunction and plasticity impairment in LPL-deficient neurons PMID: 25194787 Adipocyte-specific Sel1L-deficient (AKO) mice are resistant to diet-induced obesity. Sel1L stabilizes and prevents LPL dimers from aggregation in the endoplasmic reticulum. PMID: 25066055 This study showed that phloridzin improved plasma lipoprotein lipase activity via a decrease of ANGPTL4 mRNA expression and an increase of AMP-activated protein kinase phosphorylation. PMID: 24932810 TRL margination depends on LPL bound to GPIHBP1. PMID: 24726386 LpL hydrolysis of circulating lipoproteins is required for the accumulation of lipids in the heart of fasting mice. PMID: 24493834 The expression levels of miR-27a and miR-29a inversely correlate with the mRNA levels of lipoprotein lipase and its key transcriptional regulator peroxisome proliferator-activated receptor gamma during 3T3-L1 adipocyte differentiation. PMID: 24457907 Leu452His mutation in lipoprotein lipase gene transfer associated with hypertriglyceridemia in mice in vivo. PMID: 24086538 PPARgamma1 was intimately involved in LPL gene expression in skeletal muscle and the AMPK-PPARgamma1 pathway may play a role in exercise-induced LPL expression. PMID: 24644240 Activated cyclin-dependent kinase 5 promotes microglial phagocytosis of fibrillar beta-amyloid by up-regulating lipoprotein lipase expression. PMID: 23816988 inactivation of LPL by Angptl4 appears to occur after both proteins have traveled along the secretory pathway and arrived at the cell surface. PMID: 24220340 The present study showed that miR-467b protects apoE(-/-) mice from atherosclerosis by reducing lipid accumulation and inflammatory cytokine secretion via downregulation of LPL expression. PMID: 24309104 Lipoprotein lipase activity decreases in adipose tissue during fasting. PMID: 23176178 Macrophage LpL plays an important role in the development of atherosclerosis but not adiposity. PMID: 23378601 LpL has a role as the "gatekeeper" for tissue lipid distribution and its deficiency more profoundly affects brown than white fat biology PMID: 23542081 Neither a high fat diet nor fasting/re-feeding markedly altered the distribution pattern of LPL or GPIHBP1 in mouse pancreas. PMID: 23186339 Findings indicate that miR-467b may regulate lipid accumulation and proinflammatory cytokine secretion in oxLDL-stimulated macrophages by targeting the LPL gene. PMID: 22963823 ABCG1 controls LPL activity and promotes lipid accumulation in human macrophages in the presence of triglyceride-rich lipoproteins. PMID: 22772754 variation in Lmf1 expression is a posttranslational determinant of LPL activity. PMID: 22345169 lipoprotein retention in Bruch's membrane is mediated by lipoprotein lipase PMID: 21801873 Hematopoietic cell-derived LPL could efficiently ameliorate severe hypertriglyceridemia and hypo-alpha-cholesterolemia at the compensation of increased triglyceride content of liver PMID: 21980507 These results suggest that downregulation of miR-467b is involved in the development of hepatic steatosis by modulating the expression of its target, LPL. PMID: 21986524 Uptake of dietary retinoids at the maternal-fetal barrier: in vivo evidence for the role of lipoprotein lipase and alternative pathways. PMID: 21795711 LPL gene expression appears to be under dietary control: supplementation with cyanidin-3-O-beta-glucoside appears to up-regulate LPL in plasma and skeletal muscle but down-regulate LPL in visceral adipose tissue in the KK-Ay mouse model of diabetes PMID: 21360538 the cleavage of ANGPTL4 by these PCs modulates its inhibitory effect on LPL activity. PMID: 21398697 LPL is a novel Abeta-binding protein promoting cellular uptake and subsequent degradation of Abeta. PMID: 21177248 Data show that apoC-II and LPL mRNAs correlate temporally and geographically with surfactant lipid synthesis in preparation for birth and suggest that fatty acid recruitment from the circulation by apoC-II-activated LPL is modulated by apoC-II secretion. PMID: 21059267 PPAR-alpha response is generated by unbound fatty acids released locally by lipase activity and not by circulating plasma fatty acids. PMID: 20421589 Results show that cotransfection of LPL with wild-type Lmf1 restores its ability to support normal lipase maturation. PMID: 19471043

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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