Recombinant Mouse ANGPTL4 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0216

Recombinant Mouse ANGPTL4 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0216
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Product Overview

Tag His
Host Species Mouse
Accession Q9Z1P8
Synonym Arp4, Bk89, Fiaf, Hfarp, Ng27, Pgar, Pgarg, Pp1158
Background ANGPTL4, also known as ANGPTL2, is a protein with hypoxia-induced expression in endothelial cells. It contains 1 fibrinogen C-terminal domain and is expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney. ANGPTL4 inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. It may act as a regulator of angiogenesis and modulate tumorigenesis. It inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. It may also exert a protective function on endothelial cells through an endocrine action. ANGPTL4 is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity. In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation.
Description A DNA sequence encoding the mouse ANGPTL4 (Q9Z1P8) (Lys167-Ser410) was expressed with a His tag at the N-terminus.
Source HEK293
Predicted N Terminal His
AA Sequence Lys167-Ser410
Molecular Weight The recombinant mouse ANGPTL4 consists of 264 a.a. and predicts a molecular mass of 29.9 KDa. It migrates as an approximately 38-45 KDa band in SDS-PAGE under reducing conditions due to glycosylation.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. May also play a role in regulating glucose homeostasis and insulin sensitivity. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro). Depending on context, may modulate tumor-related angiogenesis (Probable).; Mediates inactivation of the lipoprotein lipase LPL, and thereby plays an important role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. Has higher activity in LPL inactivation than the uncleaved protein.
Subcellular Location Secreted. Secreted, extracellular space, extracellular matrix.
Database References
Tissue Specificity Detected in liver and kidney. Predominantly expressed in adipose tissue and is strongly up-regulated by fasting in white adipose tissue and liver.

Gene Functions References

  1. miR-134 accelerates atherogenesis by promoting lipid accumulation and proinflammatory cytokine secretion via the ANGPTL4/LPL pathway PMID: 28867683
  2. Functional studies in Angptl4-deficient mice confirm improved insulin sensitivity and glucose homeostasis. PMID: 29899519
  3. Data show that angiopoietin-like protein 4 (ANGPTL4)deficiency in mice knockout (ANGPTL4(-/-)) exacerbated colonic inflammation induced by dextran sulfate sodium (DSS) or stearic acid. PMID: 28287161
  4. Angptl4 is induced early in fasting to divert uptake of fatty acids and triglycerides away from adipose tissues. PMID: 28752045
  5. haematopoietic ANGPTL4 deficiency increases atherogenesis through regulating myeloid progenitor cell expansion and differentiation, foam cell formation and vascular inflammation. PMID: 27460411
  6. Following ANGPTL4 downregulation, the proliferation and invasion abilities of gastric cancer (GC)cell lines were suppressed as determined by MTT and Transwell assays, and cell apoptosis level and sensitivity to cisplatin were increased as determined by flow cytometry and MTT assay. In conclusion, these findings suggest that ANGPTL4 may be a new potential therapeutic target for GC PMID: 29436683
  7. The influence of H2O2 on ANGPTL4 provided new insight into the mechanism of atherosclerosis. PMID: 28849063
  8. The reduction of plasma triglyceride levels in Angptl4(-/-) mice and increase following Angptl4 overexpression suggest that changes in plasma triglyceride metabolism do not regulate alpha-cells in the pancreas. Our findings corroborate recent data showing that increased plasma amino acids and their transport into alpha-cells link glucagon receptor blockage to alpha-cell hyperplasia PMID: 28143927
  9. study demonstrates the key role of Angptl4 in glucocorticoid-augmented hepatic ceramide production that induces whole-body insulin resistance. PMID: 28743803
  10. 1) ANGPTL4 is not involved in the triglyceride-lowering effect ofbile acids ; 2) ANGPTL4 promotes bile acids absorption during taurocholic acid supplementation via a mechanism dependent on the gut microbiota. PMID: 28733267
  11. 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
  12. Angptl4-deficient mice show impaired insulin secretion and dysmorphic pancreatic islets. PMID: 28188788
  13. Angptl4 induces obesity-associated metabolic disorders. The present study suggested that Angptl4 promotes liver steatosis and lipolysis, in addition to impairing liver function; while Angptl4 improves glucose tolerance and insulin resistance, in addition to causing the downregulation of various insulin signaling pathway-associated genes. PMID: 27573470
  14. ANGPTL4 is part of a shuttling mechanism that directs fatty acids derived from circulating triglyceride-rich lipoproteins to brown adipose tissue during cold. PMID: 26476336
  15. these results suggest that IL-1beta increases Angptl4 expression through a mechanism dependent on the JNK-MAPK signaling pathway in MC3T3-E1 cells. PMID: 26069075
  16. glucagon receptor antagonist improves glycemia in diet-induced obese angptl4 knockout mice without increasing glucagon levels or alpha-cell proliferation, underscoring the importance of this protein. PMID: 26621734
  17. 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
  18. Letter: Angiopoietin-like 4 is induced during sebocyte differentiation and regulates sebaceous lipogenesis in vitro but is dispensable for sebaceous gland function in vivo. PMID: 24815769
  19. GR and FoxO1 are required for Angptl4 transcription activation, and that FoxO1 negatively mediates the suppressive effect of insulin PMID: 24565756
  20. ANGPTL4 is a genetically and epigenetically inactivated secreted tumor suppressor that inhibits tumor angiogenesis. PMID: 23686315
  21. 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
  22. Angptl4 is necessary for rapid modulation of lipoprotein lipase activity in adipose tissue. PMID: 23176178
  23. Depletion of adipose angiopoietin-like 4 abolishes intermittent hypoxia-induced dyslipidemia and atherosclerosis in mice, and is regulated by hypoxia-inducible factor-1. PMID: 23328524
  24. Angptl4 suppresses foam cell formation to reduce atherosclerosis development. PMID: 23640487
  25. Angptls would be useful in instances where there is a need to maintain HSCs ex vivo, such as during transduction for gene therapy applications PMID: 22639947
  26. Locally expressed Angptl4 might play a role in local uterine/placental lipid metabolism. PMID: 22350948
  27. The effect of Toll-like Receptor activation on the expression of macrophage ANGPTL4 was studied. PMID: 22538368
  28. Angptl4 mRNA expression was increased through the elevated free FAs in diabetic mice. PMID: 22068616
  29. Data showed that PPARbeta/delta regulates epidermal maturation via ANGPTL4-mediated signalling pathway. PMID: 21966511
  30. ANGPTL4 tunes endothelial cell junction organization and pericyte coverage and controls vascular permeability and angiogenesis, both during development and in pathological conditions. PMID: 21832056
  31. serum LDL, HDL and TG levels are decreased in LDLR-, Angptl- mice. PMID: 21549101
  32. the cleavage of ANGPTL4 by these PCs modulates its inhibitory effect on LPL activity. PMID: 21398697
  33. Angiopoietin-like 4 interacts with integrins beta1 and beta5 to modulate keratinocyte migration. PMID: 20952587
  34. Angptl4 protects against severe proinflammatory effects of saturated fat by inhibiting fatty acid uptake into mesenteric lymph node macrophages. PMID: 21109191
  35. Decreased fat storage by Lactobacillus paracasei is associated with increased levels of ANGPTL4. PMID: 20927337
  36. Valsartan reduced fiaf gene expression in subcutaneous, but not visceral, fat in the ob/ob mouse. PMID: 20472602
  37. Angptl4-null mice were resistant to diet-induced obesity, indicating obesity-promoting effects of Angptl4 under the condition of fat-enriched diet. PMID: 20798332
  38. ANGPTL4 interacts with vitronectin and fibronectin in the wound bed, delaying their proteolytic degradation by metalloproteinases. PMID: 20729546
  39. Stimulation of cardiac Angptl4 gene expression by dietary fatty acids and via PPARbeta/delta is part of a feedback mechanism aimed at protecting the heart against lipid overload and consequently fatty acid-induced oxidative stress. PMID: 20378851
  40. These studies demonstrate that ANGPTL4 is a positive acute phase protein and the increase in ANGPTL4 could contribute to the hypertriglyceridemia that characteristically occurs during the acute phase response by inhibiting LPL activity. PMID: 20043872
  41. potent hyperlipidemia-inducing factor in mice and inhibitor of lipoprotein lipase PMID: 12401877
  42. FIAF may partially exert its function via a truncated form PMID: 15190076
  43. angiopoietin-like protein 4 has an oligomerization state-dependent hyperlipidemic effect PMID: 15292369
  44. Induction of Angptl4 in the heart inhibits lipoprotein-derived fatty acid delivery. PMID: 15659544
  45. Differential regulation of Angptl3 & Angptl4 by sites of expression, nutritional status, & ligands of nuclear receptors may confer unique roles of each in lipoprotein metabolism. Angptl4 expression is activated by ligands of all PPAR. PMID: 15863837
  46. Angptl4 is a potential angiogenic mediator in arthritis. PMID: 15870027
  47. Angptl4-deficient mice had hypotriglyceridemia and increased postheparin plasma lipoprotein lipase, with greater effects in fasted state. Deficiecy in both Angptl proteins had additive effect on plasma triglycerides with survival not past 2 months of age. PMID: 16081640
  48. via physical association with plasma lipoproteins, FIAF acts as a powerful signal from fat and other tissues to prevent fat storage and stimulate fat mobilization PMID: 16272564
  49. First report of molecular cloning and characterization of ANGPT4in pigs, which will be helpful for a better understanding of the role of ANGPTLs in lipid metabolism. PMID: 16717449
  50. Hypoxia/ischaemia rapidly increased fiaf mRNA in the injured cortex and hippocampus at 2 and 7 days after hypoxia/ischaemia. PMID: 16837853


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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.

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