Lipoprotein Lipase Proteins (LPL)

LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. Additionally we are shipping Lipoprotein Lipase Antibodies (142) and Lipoprotein Lipase Kits (68) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
LPL 4023 P06858
LPL 16956 P11152
LPL 24539 Q06000
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Top Lipoprotein Lipase Proteins at

Showing 10 out of 15 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
Insect Cells Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 60 Days
Insect Cells Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 60 Days
Escherichia coli (E. coli) Human His tag,T7 tag 100 μg Log in to see 15 to 18 Days
HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Log in to see 10 to 12 Days
Wheat germ Human GST tag 2 μg Log in to see 11 to 12 Days
Yeast Guinea Pig His tag   1 mg Log in to see 60 to 71 Days
Yeast Primates His tag   1 mg Log in to see 60 to 71 Days
Yeast Cow His tag   1 mg Log in to see 60 to 71 Days
Yeast Sheep His tag   1 mg Log in to see 60 to 71 Days
Yeast Wild boar His tag   1 mg Log in to see 60 to 71 Days

LPL Proteins by Origin and Source

Origin Expressed in Conjugate
Human , , ,
, , ,
Mouse (Murine)

Rat (Rattus)

More Proteins for Lipoprotein Lipase (LPL) Interaction Partners

Human Lipoprotein Lipase (LPL) interaction partners

  1. ANGPTL8 has a functional LPL (show LCP1 Proteins) inhibitory motif, but only inhibits LPL (show LCP1 Proteins) and increases plasma TG levels in mice in the presence of ANGPTL3 (show ANGPTL3 Proteins)

  2. The expression of COBLL1, LPL, and ZAP70 corresponded to patient prognosis and to IGHV mutational status, although not absolutely. When we combined all three markers together and performed the ROC analysis, AUC increased compared to the AUC of individual gene expression.

  3. heterozygous N291S mutation in the lipoprotein lipase gene impairs whole-body insulin (show INS Proteins) sensitivity and affects a distinct set of plasma metabolites in humans

  4. LPL (show LCP1 Proteins) is important for the maturation of small discoidal HDL (show HSD11B1 Proteins) particles into large spherical HDL (show HSD11B1 Proteins) particles, while HL is important for HDL (show HSD11B1 Proteins) remodeling of very large HDL (show HSD11B1 Proteins) particles into intermediate-size HDL (show HSD11B1 Proteins) particles, as shown in lipoprotein lipase and hepatic lipase (show LIPC Proteins) deficiency

  5. The authors now show: (1) that ANGPTL4 (show ANGPTL4 Proteins) inactivates LPL (show LCP1 Proteins) by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 (show GPIHBP1 Proteins) renders LPL (show LCP1 Proteins) largely refractory to this inhibition; and (3) that both the LU domain and the intrinsically disordered acidic domain of GPIHBP1 (show GPIHBP1 Proteins) are required for this protective effect.

  6. Carrier status for the two common LPL (show LCP1 Proteins) variants: 447Ter (low TG/high HDL (show HSD11B1 Proteins)-C) and 291Ser (high TG/low HDL (show HSD11B1 Proteins)-C) was determined. Compared with the reference variant, the prevalence of metabolic syndrome was lower in carriers of the 447Ter variant (11.2% vs. 17.9%, P < 0.001) but with no difference in carriers of the 291Ser variant (18.4% vs. 16.5%, P = 0.59).

  7. A rare variant in APOC3 (show APOC3 Proteins)(rs138326449) has been associated with triglyceride, very low-density lipoprotein, and high-density lipoprotein levels, as well as risk of coronary heart disease. Effects are unlikely to be solely predictable by the action of APOC3 (show APOC3 Proteins) through LPL (show LCP1 Proteins).

  8. LPL (show LCP1 Proteins) gene polymorphisms are not genetic markers for the development of stroke in the Colombian sample used.

  9. Acute hypoxia strongly inhibits lipoprotein lipase activity in differentiated human preadipocytes.

  10. novel mutations cause type 1 hyperlipoproteinemia by inducing a loss or reduction in LPL (show LCP1 Proteins) secretion accompanied by a loss of LPL (show LCP1 Proteins) enzymatic activity

Cow (Bovine) Lipoprotein Lipase (LPL) interaction partners

  1. isothermal titration calorimetry (ITC) can be used for quantitative measurements of LPL activity and interactions under in vivo-like conditions, for comparisons of the properties of plasma samples from patients and control subjects as substrates for LPL, as well as for testing of drug candidates developed with the aim to affect the LPL system.

  2. miR (show MYLIP Proteins)-29b targets LPL and TDG (show TDG Proteins) genes and regulates apoptosis and triglyceride production in mammary epithelial cells.

  3. apoC-I (show APOC1 Proteins) and apoC-III (show APOC3 Proteins) inhibit lipolysis by displacing LPL from lipid emulsion particles. We also propose a role for these apolipoproteins in the irreversible inactivation of LPL by factors such as angptl4 (show ANGPTL4 Proteins).

  4. ANGPTL4 (show ANGPTL4 Proteins) is more accurately described as a reversible, noncompetitive inhibitor of LPL.

  5. Our findings confirmed that three novel SNPs we identified in the LPL gene can affect fatty acid composition and carcass traits. Therefore, selection for AA and GA genotypes should be recommended to genetically improve beef quality and flavor.

  6. Single nucleotide polymorphisms of the LPL gene might be useful genetic markers for growth traits in the bovine reproduction and breeding.

  7. Results describe the functional role of the secondary structure in the lipoprotein lipase-binding portion of apolipoprotein CII (show APOC2 Proteins).

  8. regions that are responsive to activation by apoC-II (show APOC2 Proteins)

  9. domain (192-238) is absolutely necessary for apolipoprotein AV (show APOA5 Proteins) in lipid binding and lipoprotein lipase activation

Mouse (Murine) Lipoprotein Lipase (LPL) interaction partners

  1. The data suggests that ANGPTL3 (show ANGPTL3 Proteins) is part of the machinery causing dyslipidemia majorily via LPL inhibition in mastitis mice.

  2. 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 (show ANGPTL3 Proteins))-lipoprotein lipase (LPL)pathway, and suppressed the expression of HMGCS2 (show HMGCS2 Proteins) through the increased expression of STAT5b (show STAT5B Proteins).

  3. physiological changes in adipose tissue ANGPTL4 (show ANGPTL4 Proteins) expression during fasting and cold resulted in inverse changes in the amount of mature-glycosylated LPL in wild-type mice, but not Angptl4 (show ANGPTL4 Proteins)(-/-) mice. We conclude that ANGPTL4 (show ANGPTL4 Proteins) promotes loss of intracellular LPL by stimulating LPL degradation after LPL processing in the endoplasmic reticulum (ER).

  4. LPL moved quickly from heparan sulfate proteoglycans (HSPGs) on adipocytes to GPIHBP1 (show GPIHBP1 Proteins)-coated beads, thereby depleting LPL stores on the surface of adipocytes. We conclude that HSPG (show SDC2 Proteins)-bound LPL in the interstitial spaces of tissues is mobile, allowing the LPL to move to GPIHBP1 (show GPIHBP1 Proteins) on endothelial cells

  5. our study reveals that hepatic LPL is involved in the regulation of plasma LPL activity and lipid homeostasis.

  6. The induction of LPL activity by fasting in core transgenic mice activated PPARalpha (show PPARA Proteins) downstream target genes that are involved in fatty acid beta-oxidation.

  7. This study shows that TNF-alpha (show TNF Proteins), by a Foxo1 (show FOXO1 Proteins) dependent pathway, increases the transcription of ANGPTL4 (show ANGPTL4 Proteins) which is secreted by the cells and causes inactivation of LPL.

  8. 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

  9. An LPL structural model suggests that the LPL S447X truncation exposes residues implicated in LPL binding to lipoprotein binding uptake receptors, such as GPIHBP1 (show GPIHBP1 Proteins).

  10. feeding induces lipasin, activating the lipasin-Angptl3 (show ANGPTL3 Proteins) pathway, which inhibits LPL in cardiac and skeletal muscles to direct circulating TAG to WAT for storage

Lipoprotein Lipase (LPL) Protein Profile

Protein Summary

LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. LPL functions as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Severe mutations that cause LPL deficiency result in type I hyperlipoproteinemia, while less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism.

Gene names and symbols associated with Lipoprotein Lipase Proteins (LPL)

  • lipoprotein lipase (lpl)
  • lipoprotein lipase (LPL)
  • lipoprotein lipase (Lpl)
  • fb62e04 protein
  • fc49b03 protein
  • HDLCQ11 protein
  • LIPD protein
  • LOC100223817 protein
  • lpl protein
  • wu:fb62e04 protein
  • wu:fc49b03 protein

Protein level used designations for Lipoprotein Lipase Proteins (LPL)

lipoprotein lipase , O 1-4-5 , adipose lipoprotein lipase , triacylglycerol lipase

30354 Danio rerio
464031 Pan troglodytes
100126663 Papio anubis
100127862 Xenopus (Silurana) tropicalis
100136622 Oncorhynchus mykiss
100223817 Taeniopygia guttata
712887 Macaca mulatta
100534504 Oreochromis niloticus
4023 Homo sapiens
280843 Bos taurus
16956 Mus musculus
24539 Rattus norvegicus
396219 Gallus gallus
403626 Canis lupus familiaris
100055358 Equus caballus
397537 Sus scrofa
727696 Felis catus
100135570 Cavia porcellus
443408 Ovis aries
100860750 Capra hircus
100340171 Oryctolagus cuniculus
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