Recombinant Human Angiopoietin-related protein 3(ANGPTL3)

Code CSB-YP896903HU
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Source Yeast
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Code CSB-EP896903HU
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Source E.coli
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Code CSB-EP896903HU-B
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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-BP896903HU
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Source Baculovirus
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Code CSB-MP896903HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names ANGPTL3
Uniprot No. Q9Y5C1
Alternative Names ANG 5; ANG-5; ANG5; Angiopoietin 5; Angiopoietin like 3; Angiopoietin related protein 3; Angiopoietin-5; Angiopoietin-like protein 3; Angiopoietin-related protein 3; ANGL3_HUMAN; ANGPT5; ANGPTL3; ANL3; FHBL2; OTTHUMP00000010719; UNQ153/PRO179
Species Homo sapiens (Human)
Expression Region 17-460
Target Protein Sequence SRID QDNSSFDSLS PEPKSRFAML DDVKILANGL LQLGHGLKDF VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR RTTYKLQVKN EEVKNMSLEL NSKLESLLEE KILLQQKVKY LEEQLTNLIQ NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ TVEDQYKQLN QQHSQIKEIE NQLRRTSIQE PTEISLSSKP RAPRTTPFLQ LNEIRNVKHD GIPAECTTIY NRGEHTSGMY AIRPSNSQVF HVYCDVISGS PWTLIQHRID GSQNFNETWE NYKYGFGRLD GEFWLGLEKI YSIVKQSNYV LRIELEDWKD NKHYIEYSFY LGNHETNYTL HLVAITGNVP NAIPENKDLV FSTWDHKAKG HFNCPEGYSG GWWWHDECGE NNLNGKYNKP RAKSKPERRR GLSWKSQNGR LYSIKSTKML IHPTDSESFE
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 Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism
Gene References into Functions
  1. Association of low-density lipoprotein receptor-related protein 1 rs11613352 and angiopoietin-like 3 rs2131925 with hypertension might imply a direct effect at the artery wall. PMID: 29989339
  2. The present data leads to new insights into the role of ANGPTL3 in glioblastomas and provides an independent predictive factor PMID: 26639238
  3. The role of ANGPLT3 in controlling lipoprotein metabolism and risk of cardiovascular diseases is reviewed here. PMID: 29334984
  4. these results suggest that the DOCK-ANGPTL3 SNPs and their haplotypes were associated with the angiographic severity to coronary artery atherosclerosis and the risk of coronary artery disease (CAD) and ischemic stroke in the Southern Chinese Han population. PMID: 29454388
  5. Subjects who carried ANGPTL3 sequence variants rs12563308 and rs199772471 had abnormally high total cholesterol and LDL-cholesterol concentrations. PMID: 28972399
  6. circulating ANGPTL3 and ANGPTL 4 expression was significantly elevated in hepatocellular carcinoma cases compared to chronic hepatitis patients and controls PMID: 28371666
  7. ANGPTL8 has a functional LPL inhibitory motif, but only inhibits LPL and increases plasma TG levels in mice in the presence of ANGPTL3 PMID: 28413163
  8. Our findings demonstrate that complete ANGPTL3 deficiency associates with highly reduced postprandial lipemia probably due to faster catabolism of intestinally derived lipoproteins, larger expansion of the postprandial FFA pool, and decreased influx of dietary-derived fatty acids into the liver. These results add information on mechanisms underlying hypolipidemia in familial combined hypolipidemia (FHBL2). PMID: 27040449
  9. participants with heterozygous loss-of-function variants in ANGPTL3 had significantly lower serum levels of triglycerides, HDL cholesterol, and LDL cholesterol than participants without these variants. PMID: 28538136
  10. ANGPTL3 deficiency is associated with protection from coronary artery disease. PMID: 28385496
  11. our data shows that ANGPTL3, 4 and 8 are increased in obesity and type 2 diabetes (T2D). ANGPTL8 associates with ANGPTL3 in the non-diabetic subjects while it associated more with ANGPTL4 in the obese and T2D subjects. PMID: 27733177
  12. ANGPTL3 is specifically correlated with HDL-c, apoA-I, SAA and HDL function in female non-diabetic participants. The decrease of ANGPTL3 level in female T2DM patients might contribute to its weak association to HDL components and function. PMID: 27620179
  13. The ANGPTL3 gene lies within DOCK7, although the variant is within non-coding regions outside of ANGPTL3, within DOCK7, suggesting complex long-range regulatory effects on gene expression in coronary artery disease. PMID: 26800306
  14. ANGPTL3 levels were associated with fasting insulin and the homeostasis model assessment of insulin resistance in Korean children. PMID: 26739706
  15. An ANGPTL3-4-8 model was proposed to explain the variations of lipoprotein lipase (LPL) activity during the fed-fast cycle. Feeding induces ANGPTL8, activating the ANGPTL8-ANGPTL3 pathway, which inhibits LPL in cardiac and skeletal muscles to direct circulating triglycerides (TG) to white adipose tissue; the reverse is true during fasting, which suppresses ANGPTL8 but induces ANGPTL4, thereby directing TG to muscles. PMID: 27053679
  16. Inactivation of ANGPTL3 reduces hepatic VLDL-triglyceride secretion PMID: 25954050
  17. Novel mutation Y344S found in ANGPTL3 gene in two diabetic patients with familial hypobetalipoproteinemia. PMID: 25733326
  18. Data suggest that silencing of ANGPTL 3 (angiopoietin-like protein 3) improves insulin sensitivity. PMID: 25495645
  19. HCV core represses ANGPTL-3 expression through loss of HNF-1alpha binding activity and blockage of LXR/RXR transactivation PMID: 23978712
  20. Data suggest that genetic polymorphisms in ANGPTL3 (angiopoietin-like 3 protein), TIMD4 (T cell immunoglobulin mucin-4), and apolipoproteins A5 and B are among the genetic determinants of hypertriglyceridemia in Amerindian populations. [REVIEW] PMID: 24768220
  21. ANGPTL3 is positively associated with low-density lipoprotein cholesterol and high-density lipoprotein cholesterol and not with metabolic syndrome traits including triglycerides. PMID: 24626437
  22. Identification of loss-of-function ANGPTL3 mutation is shedding light on a possible role of ANGPTL3 at the crossroads of lipoproteins, fatty acids, and glucose metabolism. [Review] PMID: 23839332
  23. Although partial Angptl3 deficiency did not affect the activities of lipolytic enzymes, the complete absence of Angptl3 results in an increased lipoprotein lipase activity and mass and low circulating free fatty acid levels. PMID: 23661675
  24. No gene-gene interaction was identified other than an interaction between SNPs in the ANGPTL3 and RXRA regions, which results in the inhibition of ApoB reduction in response to statin-FNA therapy. PMID: 22896670
  25. ANGPTL3 activation is modulated by O-glycosylation and the proprotein undergoes convertase processing for activation. PMID: 20837471
  26. Familial combined hypolipidemia segregates as a recessive trait so that apolipoprotein B- and apolipoprotein A-I-containing lipoproteins are comprehensively affected only by the total deficiency of Angptl3. PMID: 22659251
  27. the homozygous or compound heterozygous for ANGPTL3 loss-of-function mutations (p.G400VfsX5, p.I19LfsX22/p.N147X) had low plasma ANGPTL3 and moderately reduced low-density lipoprotein cholesterol but normal plasma high-density lipoprotein cholesterol. PMID: 22062970
  28. It denominated familial combined hypolipidemia, which consist of a biochemical phenotype of low LDLc, low apoB, low TG and, unlike APOB mutations, low HDL cholesterol, due to a loss-of-function mutation in ANGPTL3. PMID: 22155345
  29. The prevalence and effect of mutations in ANGPTL3, in carriers of pathogenic autosomal dominant hypercholesterolemia mutations with unexpected low LDL-C levels. PMID: 22095935
  30. In a cohort of subjects with severe primary hypobetalipoproteinemia the prevalence of ANGPTL3 gene mutations responsible for a combined hypolipidemia phenotype is about 10%. PMID: 22247256
  31. Serum Angptl3 was positively correlated with adiponectin in metabolic syndrome patients. PMID: 20360639
  32. Dysmorphic findings in two cases involving FBHL2 are reported. PMID: 19282754
  33. relationship between plasma angiopoietin-like protein 3 (ANGPTL3), and lipoprotein lipase (LPL) activity and hepatic triglyceride lipase PMID: 20595410
  34. Found two distinct nonsense mutations in ANGPTL3 in 2 family members out of 38 with combined hypolipidemia. PMID: 20942659
  35. Data suggest roles for ANGPTL3 and ANGPTL4 in modulation of serum TG and HDL levels in obesity in a Finnish population sample. PMID: 19826106
  36. Like ANGPTL4, ANGPTL3 inhibited nonstabilized LPL but not GPIHBP1-stabilized LPL PMID: 19542565
  37. ANGPTL3 may be a novel factor contributing to uremic dyslipidemia. PMID: 19540497
  38. ANGPTL3 stimulates endothelial cell adhesion and migration via integrin alpha vbeta 3 and induces blood vessel formation in vivo PMID: 11877390
  39. Angptl3 gene is a direct target of the liver X receptor (LXR). PMID: 12518032
  40. Data show that angiopoietin-like protein 3 (ANGPTL3) targets adipose cells and induces lipolysis. PMID: 12565906
  41. the cleavage of ANGPTL3 at two sites is important for the activation of ANGPTL3 in vivo PMID: 12909640
  42. liver-derived Angptl3 inhibits lipoprotein lipase activity primarily in the fed state PMID: 16531751
  43. Angptl3 acts as an inhibitor of EL and may be involved in the regulation of plasma HDL cholesterol and HDL-PL levels in humans and rodents. PMID: 17110602
  44. The pilot study supports the hypothesis about the role of Angptl3 as a new class of lipid metabolism modulator. PMID: 18063851
  45. probucol decreases plasma ANGPTL3 and HDL phospholipids while increasing prebeta1-HDL and cholesteryl ester transfer protein PMID: 18279878
  46. Our results also indicated that the integrin alphaVbeta3 antibody (LM609) could block the Angptl3-induced protein kinase B phosphorylation. PMID: 18535744
  47. ANGPTL3, the inhibitor of endothelial lipase, may be strongly associated with increased HDL-cholesterol PMID: 18804459
  48. The finding that ANGPTL3 and ANGPTL4 inhibit LPL activity through distinct mechanisms indicates that the two proteins play unique roles in modulation of lipid metabolism in vivo. PMID: 19028676
  49. The present study underlines the role of ANGPTL3 in HDL-cholesterol metabolism as early as in adolescence PMID: 19890028
  50. ANGPTL3 is the first member of the angiopoietin-like family of secreted factors binding to integrin alpha(v)beta(3), which suggests a possible role in the regulation of angiogenesis. PMID: 11877390

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Involvement in disease Hypobetalipoproteinemia, familial, 2 (FHBL2)
Subcellular Location Secreted, Cell projection, lamellipodium
Tissue Specificity Expressed principally in liver. Weakly expressed in kidney. Binds to adipocytes. Increased expression and colocalization with activated ITGB3 in glomeruli of patients with nephrotic syndrome showing effaced podocyte foot processes (at protein level).
Database Links

HGNC: 491

OMIM: 604774

KEGG: hsa:27329

STRING: 9606.ENSP00000360170

UniGene: Hs.209153

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