Recombinant Human ANGPTL4 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0215

Recombinant Human ANGPTL4 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0215
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Product Overview

Tag His
Host Species Human
Accession Q9BY76
Synonym ANGPTL2, ARP4, FIAF, HARP, HFARP, NL2, PGAR, pp1158, TGQTL, UNQ171
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 human ANGPTL4 (Q9BY76) (Pro166-Ser406) was expressed with an N-terminal His tag.
Source HEK293
Predicted N Terminal His
AA Sequence Pro166-Ser406
Molecular Weight The recombinant human ANGPTL4 comprises 261 a.a. and has a predicted molecular mass of 29.5 kDa. The apparent molecular mass of the protein is approximately 35 kDa 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 (Probable). 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.; 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 blood plasma (at protein level). Detected in liver. Detected in white fat tissue and placenta. Expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney.

Gene Functions References

  1. Carriers of p.E40K, a variant that abolishes ANGPTL4 ability to inhibit lipoprotein lipase, have lower odds of T2D (odds ratio 0.89, 95% confidence interval 0.85-0.92, p = 6.3 x 10(-10)), lower fasting glucose, and greater insulin sensitivity. PMID: 29899519
  2. A relevant role of ANGPTL-4 in human obesity and its involvement in long-term body weight changes. PMID: 29536615
  3. Data indicate that the angiopoietin-like protein 4 (ANGPTL4)-mediated upregulation of tristetraprolin expression regulates the stability of chemokines in human colon epithelial cells. PMID: 28287161
  4. The data suggest that exercise-induced ANGPTL4 is secreted from the liver and driven by a glucagon-cAMP-PKA pathway in humans. These findings link the liver, insulin/glucagon, and lipid metabolism together. PMID: 29031727
  5. Study data support dual roles for ANGPTL4 in urothelial carcinoma progression, either as a tumor suppressor or oncogene, in response to microenvironmental context. PMID: 29035390
  6. ANGPTL4 levels are increased in both plasma and adipose tissues of subjects with hypertension. PMID: 29490644
  7. Low ANGPTL4 expression is associated with childhood obesity. PMID: 28733963
  8. SNP rs11672433, a high-frequency locus in the ANGPTL4 gene, does not influence the predisposition to brain arteriovenous malformation or its effect is too small to be detected in the present size sample set. PMID: 29221972
  9. Levels of ANGPTL4 in the circulation and HDLs were increased in type 2 diabetics altering lipid metabolism. PMID: 28645936
  10. High expression of ANGPTL4 is associated with drug resistance in prostate cancer. PMID: 28560449
  11. this study suggests that the presence of C allele of rs1044250 and G allele of rs2278236 in ANGPTL4 gene is associated with higher risk of moderate/severe proteinuria in renal transplant patients PMID: 27913276
  12. These results suggested that ANGPTL4 was essential for proliferation and metastasis of lung cancer cells. PMID: 27166634
  13. The mutant tumors exhibited impaired proliferation, anoikis resistance, and migratory capability and had reduced adenylate energy charge. Further investigations also revealed that cANGPTL4 regulated the expression of Glut2 PMID: 28641978
  14. Data indicate angiopoietin-like 4 (ANGPTL4) as a key player that coordinates an increase in cellular energy flux crucial for EMT via an ANGPTL4/14-3-3gamma signaling axis. PMID: 28745316
  15. The authors now show: (1) that ANGPTL4 inactivates LPL by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 renders LPL largely refractory to this inhibition; and (3) that both the LU domain and the intrinsically disordered acidic domain of GPIHBP1 are required for this protective effect. PMID: 27929370
  16. One of the variants, rs116843064, is a damaging missense variant within the ANGPTL4 gene. PMID: 27036123
  17. reduced expression of one of the survival-associated transcripts, Angiopoietin-like 4, impairs growth of a gemcitabine-resistant pancreatic cancer cell line. PMID: 27282075
  18. Serum ANGPTL4 is elevated in coronary artery disease, but levels do not reflect severity of disease. PMID: 28795637
  19. identify ANGPTL4 as a Wnt signaling antagonist that binds to syndecans and forms a ternary complex with the Wnt co-receptor Lipoprotein receptor-related protein 6 PMID: 29017031
  20. results suggest that ANGPTL4 could contribute to the development of retinal neovascularization in sickle cell patients and could therefore be a therapeutic target for the treatment of PSR PMID: 28832635
  21. Data suggest that purified FLD (C-terminal fibrinogen-like domain) of ANGPTL4 is sufficient to stimulate lipolysis in primary adipocytes; increasing circulating FLD levels in mice not only induces white adipose tissue lipolysis in vivo but also reduces diet-induced obesity without affecting LPL (lipoprotein lipase) activity; increasing systemic FLD levels induces beige conversion in white adipose tissue. PMID: 28842503
  22. enhanced expression of angiopoietin-like 4 in rheumatoid arthritis may explain the occurrence of insulin resistance, cardiovascular risk, and joint destruction [review] PMID: 28004425
  23. Neither serum nor urine Angptl4 appear to be good biomarkers in minimal change disease. Elevated urinary Angptl4 in glomerular disease appears to reflect the degree of proteinuria rather than any specific disease. PMID: 28441404
  24. results reveal that liganded GR spatiotemporally controls ANGPTL4 transcription in a chromosomal context. PMID: 28056052
  25. analyzed samples from our previously published studies on ANGPL4 levels in patients on hemodialysis and patients with diabetes type 2. These samples did not show false positive reactions. The levels of ANGPTL4 were comparable to those detected previously PMID: 28107351
  26. Oleic acid enhances head and neck squamous cell carcinoma metastasis through the ANGPTL4/fibronectin/Rac1/Cdc42 and ANGPTL4/fibronectin/MMP-9 signaling axes. PMID: 27865799
  27. Cyclic stretching of tendon fibroblasts stimulated the expression and release of ANGPTL4 protein. PMID: 26670924
  28. ANGPTL4 is secreted by human forearm muscle in postprandial conditions after a high-saturated fatty acid meal. Plasma ANGPTL4 concentrations were not associated with in vivo skeletal muscle LPL activity after a high-saturated fatty acid meal. Dietary fat quality affects plasma ANGPTL4, but it remains to be elucidated whether this influences short-term skeletal muscle lipid handling. PMID: 27011113
  29. angiopoietin-like 4 plays an important role in the regulation of epidermal growth factor induced cancer metastasis PMID: 27797381
  30. Beyond rare-variant genetic association study determined rare hypertriglyceridemia causal ANGPTL4 variants based on high throughput sequencing. PMID: 26903168
  31. ANGPTL4 variants are associated with, not only lower fasting triglyceride levels, but also a decreased cardiovascular risk in type 2 diabetic Tunisian patients. So, T266M and E40K polymorphism predicts cardiovascular disease risk in type 2 diabetic Tunisian population. PMID: 27004807
  32. Increased ANGPTL4 expression is associated with uveal melanoma. PMID: 26761211
  33. This study showed that the tagged SNPs and high serum levels of ANGPTL4 are associated with large artery atherosclerotic stroke and the lipid characteristics. PMID: 26944173
  34. ANGPTL4 mRNA expressions and serum levels were significantly higher in high grade breast carcinoma. PMID: 26745120
  35. Knockdown of ANGPTL4 inhibits proliferation and promotes apoptosis in cervical cancer. PMID: 27053616
  36. ANGPTL4 levels were higher in both obese and non-obese PCOS patients compared to healthy controls. PMID: 26291814
  37. circulating ANGPTL4 levels are up-regulated in COPD patients, and have correlations with pulmonary function and systematic inflammation in COPD PMID: 26813452
  38. Collectively, our findings indicate that miR-134 may regulate lipid accumulation and proinfiammatory cytokine secretion in macrophages by targeting the ANGPTL4 gene. PMID: 26546816
  39. This study is the first to show that podocyte-secreted Angptl4 is upregulated in diabetic neuropathy and can be detected in urine. PMID: 25424436
  40. Data suggest that up-regulation of plasma levels of Angptl4 (angiopoietin-like 4 protein) and LPL (lipoprotein lipase) can be used as biomarkers specific to detecting the stage of diabetic cardiovascular complications. PMID: 25597500
  41. Hepatocellular carcinoma (HCC) tissues expressed significantly lower levels of ANGPTL4 mRNA than non-tumor tissues; copy number of ANGPTL4 gene in tumor tissues was significantly lower than in non-tumor tissues of HCC patients. Higher frequency of methylation of CpG sites of ANGPTL4 promoter was detected in tumor tissues compared to non-tumor tissues. PMID: 25148701
  42. results demonstrate ANGPTL4 contributes to OSCC metastasis by stimulating cell invasion. ANGPTL4 is potential therapeutic target for preventing cancer metastasis. PMID: 25060575
  43. Carriers of E40K and other inactivating mutations in ANGPTL4 had lower levels of triglycerides and a lower risk of coronary artery disease than did noncarriers. PMID: 26933753
  44. We found that carriers of loss-of-function mutations in ANGPTL4 had triglyceride levels that were lower than those among noncarriers; these mutations were also associated with protection from coronary artery disease. PMID: 26934567
  45. ANGPTL4 might promote metastasis and might inhibit apoptosis of colorectal cancer cells by up-regulation of BMP7. PMID: 26417691
  46. A1AT binds to FA, and it is this form of A1AT that induces Angptl4 and FABP4 expression via a PPAR-dependent pathway. PMID: 26363050
  47. High serum ANGPTL4 with circulating RANKL suggests that ANGPTL4 may represent a novel marker for bone destruction in rheumatoid arthritis. PMID: 25289668
  48. results suggest targeting both ANGPTL4 and VEGF may be necessary for effective treatment or prevention of PDR and provide the foundation for studies evaluating aqueous ANGPTL4 as a biomarker to help guide individualized therapy for diabetic eye disease PMID: 26039997
  49. plasma ANGPTL4 levels as well as ANGPTL4 variants significantly predict cardiovascular events independently of conventional cardiovascular risk factors PMID: 25463098
  50. ANGPTL4 can both bind and inactivate lipoprotein lipase (LPL) complexed to GPIHBP1 and inactivation of LPL by ANGPTL4 greatly reduces the affinity of LPL for GPIHBP1 PMID: 25809481


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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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