Recombinant Mouse Lipoprotein lipase(Lpl)

Code CSB-YP013065MO
Size Pls inquire
Source Yeast
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Code CSB-EP013065MO-B
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-MP013065MO
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity >85% (SDS-PAGE)
Target Names Lpl
Uniprot No. P11152
Alternative Names Lpl; Lipoprotein lipase; LPL; EC 3.1.1.34
Species Mus musculus (Mouse)
Expression Region 28-474
Target Protein Sequence ADA GRDFSDIESK FALRTPEDTA EDTCHLIPGL ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLYRAQQH YPVSAGYTKL VGNDVARFIN WMEEEFNYPL DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ PGCNIGEAIR VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTEDGKQHNQ AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG ELLMMKLKWI SDSYFSWPDW WSSPSFVIER IRVKAGETQK KVIFCAREKV SHLQKGKDSA VFVKCHDKSL KKSG
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Data

Function The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium.
Gene References into Functions
  1. LPL-mediated release of essential fatty acid DHA regulates hematopoietic stem progenitor cell expansion and definitive hematopoiesis PMID: 29615667
  2. 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
  3. LPL in the hypothalamus is an important regulator of body weight and glucose homeostasis PMID: 28456865
  4. 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
  5. mutation of a conserved cysteine in GPIHBP1 abolishes the ability of GPIHBP1 to bind LPL PMID: 28476858
  6. The data suggests that ANGPTL3 is part of the machinery causing dyslipidemia majorily via LPL inhibition in mastitis mice. PMID: 29104012
  7. 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
  8. 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
  9. 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
  10. our study reveals that hepatic LPL is involved in the regulation of plasma LPL activity and lipid homeostasis. PMID: 27234787
  11. 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
  12. 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
  13. 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
  14. 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
  15. 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
  16. MiR-590 agomir down-regulates LPL mRNA and protein expression in a mouse model of atherosclerosis. PMID: 26397958
  17. Deficiency of Lipoprotein Lipase in Neurons Decreases AMPA Receptor Phosphorylation and Leads to Neurobehavioral Abnormalities in Mice PMID: 26263173
  18. 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
  19. Results indicated that aggregation of alpha-syn and reduction of UCHL1 expression in LPL-deficient mice may affect synaptic function. PMID: 25595992
  20. 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
  21. Maternal overnutrition induces LPL expression in trophoblasts by reducing the inhibitory effect of SIRT1 on PPARgamma. PMID: 25948680
  22. Lipoprotein lipase is an important modulator of lipid uptake and storage in hypothalamic neurons. PMID: 26265042
  23. 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
  24. 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
  25. 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
  26. TRL margination depends on LPL bound to GPIHBP1. PMID: 24726386
  27. LpL hydrolysis of circulating lipoproteins is required for the accumulation of lipids in the heart of fasting mice. PMID: 24493834
  28. 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
  29. Leu452His mutation in lipoprotein lipase gene transfer associated with hypertriglyceridemia in mice in vivo. PMID: 24086538
  30. 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
  31. Activated cyclin-dependent kinase 5 promotes microglial phagocytosis of fibrillar beta-amyloid by up-regulating lipoprotein lipase expression. PMID: 23816988
  32. 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
  33. 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
  34. Lipoprotein lipase activity decreases in adipose tissue during fasting. PMID: 23176178
  35. Macrophage LpL plays an important role in the development of atherosclerosis but not adiposity. PMID: 23378601
  36. LpL has a role as the "gatekeeper" for tissue lipid distribution and its deficiency more profoundly affects brown than white fat biology PMID: 23542081
  37. Neither a high fat diet nor fasting/re-feeding markedly altered the distribution pattern of LPL or GPIHBP1 in mouse pancreas. PMID: 23186339
  38. Findings indicate that miR-467b may regulate lipid accumulation and proinflammatory cytokine secretion in oxLDL-stimulated macrophages by targeting the LPL gene. PMID: 22963823
  39. ABCG1 controls LPL activity and promotes lipid accumulation in human macrophages in the presence of triglyceride-rich lipoproteins. PMID: 22772754
  40. variation in Lmf1 expression is a posttranslational determinant of LPL activity. PMID: 22345169
  41. lipoprotein retention in Bruch's membrane is mediated by lipoprotein lipase PMID: 21801873
  42. Hematopoietic cell-derived LPL could efficiently ameliorate severe hypertriglyceridemia and hypo-alpha-cholesterolemia at the compensation of increased triglyceride content of liver PMID: 21980507
  43. 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
  44. Uptake of dietary retinoids at the maternal-fetal barrier: in vivo evidence for the role of lipoprotein lipase and alternative pathways. PMID: 21795711
  45. 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
  46. the cleavage of ANGPTL4 by these PCs modulates its inhibitory effect on LPL activity. PMID: 21398697
  47. LPL is a novel Abeta-binding protein promoting cellular uptake and subsequent degradation of Abeta. PMID: 21177248
  48. 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
  49. PPAR-alpha response is generated by unbound fatty acids released locally by lipase activity and not by circulating plasma fatty acids. PMID: 20421589
  50. Results show that cotransfection of LPL with wild-type Lmf1 restores its ability to support normal lipase maturation. PMID: 19471043

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Subcellular Location Cell membrane, Lipid-anchor, GPI-anchor, Secreted
Protein Families AB hydrolase superfamily, Lipase family
Tissue Specificity Expressed in liver, epididymal fat, heart, psoas muscle, lactating mammary gland, adrenal, lung, and ovary. Highest levels in heart and adrenal gland.
Database Links

KEGG: mmu:16956

STRING: 10090.ENSMUSP00000015712

UniGene: Mm.1514

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