Recombinant Human Angiopoietin-like 4 C-Terminal Frag, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Inhibition Activity
Format
Carrier-Free

Order Details

Recombinant Human Angiopoietin-like 4 C-Terminal Frag, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Angiopoietin‑like 4/ANGPTL4 C‑Terminal Fragment is immobilized at 1 μg/mL, 100 μL/well, the concentration of Recombinant Human LILRB2/CD85d/ILT4 Fc Chimera  (Catalog # 2078-T4) binds with an ED50 of 70.0-350 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human Angiopoietin-like Protein 4/ANGPTL4 protein
Leu165-Ser406, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Leu165
Structure / Form
Oligomer
Protein/Peptide Type
Recombinant Proteins
Gene
ANGPTL4
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Inhibition Activity
Theoretical MW
28 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
36 kDa, reducing conditions
Publications
Read Publications using
3485-AN in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris-Citrate and NaCl.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Angiopoietin-like 4 C-Terminal Frag, CF

  • Angiopoietin like Protein 4
  • angiopoietin-like 4
  • Angiopoietin-like Protein 4
  • ANGPTL4
  • ARP4fasting-induced adipose factor
  • FIAF
  • FIAFhepatic angiopoietin-related protein
  • Hepatic fibrinogen/angiopoietin-related protein
  • HFARP
  • HFARPANGPTL2
  • NL2
  • peroxisome proliferator-activated receptor (PPAR) gamma inducedangiopoietin-related protein
  • PGAR
  • PGARangiopoietin-related protein 4
  • pp1158
  • PPARG angiopoietin related protein

Background

ANGPT-L4, also known as FIAF, FARP, and PGAR, is a 55 kDa glycoprotein secreted by the liver and fat tissue that is structurally related to the angiopoietins. It contains an N‑terminal coiled coil domain and a C‑terminal fibrinogen-like domain which can be proteolytically separated in vivo (1, 2). Mature human ANGPT‑L4 shares 26%‑30% amino acid (aa) sequence identity with ANGPT-L1, 2, 3, 5, 6, and 7. It shares approximately 75% aa sequence identity with mouse and rat ANGPT‑L4. The coiled coil domain, which is not glycosylated, mediates the formation of variable sized disulfide-linked oligomers (3, 4). This domain directly inhibits lipoprotein lipase, resulting in increased circulating triglyceride levels (5-9). In human, the N-terminal fragment and full length ANGPT-L4 physically associate with HDL (9). In mouse, however, full length ANGPT-L4 associates with HDL, while the N-terminal fragment associates with LDL (9). Circulating ANGPT-L4 is decreased in type II diabetics with a subsequent loss of its normal plasma glucose lowering activity (10). Its expression in adipose tissue is induced by fasting and suppressed by feeding (3, 11). Its expression in both liver and fat is up‑regulated by PPAR alpha , beta , gamma , and δ agonists and down‑regulated by insulin (3, 12, 13). ANGPT-L4 is induced in vascular endothelial cells by hypoxia and in hypoxic areas surrounding tumors (14-16). The full length molecule but not the C-terminal fragment is bound by heparan sulfate proteoglycans and functions as an angiogenesis inhibitor (14, 15).
  1. Li, C. (2006) Curr. Opin. Lipidol. 17:152.
  2. Kersten, S. (2005) Biochem. Soc. Transact. 33:1059.
  3. Ge, H. et al. (2005) J. Lipid Res. 46:1484.
  4. Ge, H. et al. (2004) J. Biol. Chem. 279:2038.
  5. Sukonina, V. et al. (2006) Proc. Natl. Acad. Sci. 103:17450.
  6. Koster, A. et al. (2005) Endocrinology 146:4943.
  7. Yoshida, K. et al. (2002) J. Lipid Res. 43:1770.
  8. Ge, H. et al. (2004) J. Lipid Res. 45:2071.
  9. Mandard, S. et al. (2006) J. Biol. Chem. 281:934.
  10. Xu, A. et al. (2005) Proc. Natl. Acad. Sci. 102:6086.
  11. Kersten, S. et al. (2000) J. Biol. Chem. 275:28488.
  12. Mandard, S. et al. (2004) J. Biol. Chem. 279:34411.
  13. Yamada, T. et al. (2006) Biochem. Biophys. Res. Commun. 347:1138.
  14. Cazes, A. et al. (2006) Circ. Res. 99:1207.
  15. Le Jan, S. et al. (2003) Am. J. Pathol. 162:1521.
  16. Ito, Y. et al. (2003) Cancer Res. 63:6651.

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Publications for Angiopoietin-like Protein 4/ANGPTL4 (3485-AN)(6)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 2 applications: Bioassay, ELISA (Standard).


Filter By Application
Bioassay
(2)
ELISA (Standard)
(4)
All Applications
Filter By Species
Human
(4)
All Species
Showing Publications 1 - 6 of 6.
Publications using 3485-AN Applications Species
Hefni, E;Menon, D;Ma, T;Asiedu, EB;Sultan, A;Meiller, T;Schneider, A;Sodhi, A;Montaner, S; Angiopoietin-like 4 induces head and neck squamous cell carcinoma cell migration through the NRP1/ABL1/PXN pathway Cellular signalling 2023-05-09 [PMID: 37169211] (Bioassay, Human) Bioassay Human
BW van der Ko, RG Vink, JWE Jocken, NJT Roumans, GH Goossens, ECM Mariman, MA van Baak, EE Blaak Effect of diet-induced weight loss on angiopoietin-like protein 4 and adipose tissue lipid metabolism in overweight and obese humans Physiol Rep, 2018-07-01;6(13):e13735. 2018-07-01 [PMID: 29998530] (ELISA (Standard), Human) ELISA (Standard) Human
EG Gruppen, S Kersten, RPF Dullaart Plasma angiopoietin-like 4 is related to phospholipid transfer protein activity in diabetic and non-diabetic subjects: role of enhanced low grade inflammation Lipids Health Dis, 2018-03-27;17(1):60. 2018-03-27 [PMID: 29587751] (ELISA (Standard)) ELISA (Standard)
K Baba, Y Kitajima, S Miyake, J Nakamura, K Wakiyama, H Sato, K Okuyama, H Kitagawa, T Tanaka, M Hiraki, K Yanagihara, H Noshiro Hypoxia-induced ANGPTL4 sustains tumour growth and anoikis resistance through different mechanisms in scirrhous gastric cancer cell lines Sci Rep, 2017-09-11;7(1):11127. 2017-09-11 [PMID: 28894280] (Bioassay, Human) Bioassay Human
Alex S, Lange K, Amolo T, Grinstead J, Haakonsson A, Szalowska E, Koppen A, Mudde K, Haenen D, Al-Lahham S, Roelofsen H, Houtman R, van der Burg B, Mandrup S, Bonvin A, Kalkhoven E, Muller M, Hooiveld G, Kersten S Short-chain fatty acids stimulate angiopoietin-like 4 synthesis in human colon adenocarcinoma cells by activating peroxisome proliferator-activated receptor gamma. Mol Cell Biol, 2013-01-22;33(7):1303-16. 2013-01-22 [PMID: 23339868] (ELISA (Standard), Human) ELISA (Standard) Human
Kersten S, Lichtenstein L, Steenbergen E, Mudde K, Hendriks HF, Hesselink MK, Schrauwen P, Muller M Caloric restriction and exercise increase plasma ANGPTL4 levels in humans via elevated free fatty acids. Arterioscler. Thromb. Vasc. Biol., 2009-04-02;29(6):969-74. 2009-04-02 [PMID: 19342599] (ELISA (Standard)) ELISA (Standard)

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Bioinformatics

Gene Symbol ANGPTL4
Uniprot