Recombinant Mouse Angiopoietin-like Protein 4/ANGPTL4, CF Summary
Additional Information |
C-Terminal Fragment |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Angiopoietin‑like Protein 4/ANGPTL4
is immobilized at 1 μg/mL, 100 μL/well, the concentration of LILRB2/CD85d/ILT4 Fc Chimera (Catalog # 2078-T4)
that
produces 50% of
the optimal
binding response
is 0.09-0.54 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse Angiopoietin-like Protein 4/ANGPTL4 protein Leu169-Ser410, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Leu169 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
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 |
36-43 kDa, reducing conditions |
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 PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Angiopoietin-like Protein 4/ANGPTL4, CF
Background
Angiopoietin-like
4 (ANGPTL4), also known as FIAF, FARP, and PGAR, is a 55 kDa glycoprotein
secreted by the liver and fat tissue. It is structurally related to the
angoipoietins and contains an N-terminal coiled coil domain and a
C-terminal fibrinogen-like domain which can be proteolytically separated in vivo (1).
Amino acid 169‑410 contains the C-terminal fibrinogen like domain within
mouse ANGPTL4, and this domain shares 75% and 97% sequence identity with human
and rat homologs, respectively. The
coiled coil domain, which is not glycosylated, mediates the formation of
variable sized disulfide-linked oligomers (2). This domain directly inhibits
lipoprotein lipase, resulting in increased circulating triglyceride levels
(3, 4). In humans, the N-terminal fragment and full length ANGPTL4
physically associate with HDL (4). In mouse, however, full length ANGPTL4
associates with HDL, while the N-terminal fragment associates with LDL (4).
Circulating ANGPTL4 is decreased in type II diabetics with a subsequent
loss of its normal plasma glucose lowering activity (5). Its expression in
adipose tissue is induced by fasting and suppressed by feeding (6). In hypoxic
areas, ANGPTL4 is induced in both vascular endothelial cells and tumor cells
(7, 8). The N-terminal fragment can function as an angiogenesis inhibitor
(7, 8). In contrast, the C-terminal fragment modulates cell adhesion
through interactions with heparan sulfate proteoglycans, Integrins beta 1
and beta 5, Vitronectin, and Fibronectin, thereby promoting keratinocyte
migration and wound healing (7, 9, 10). ANGPTL4 additionally enhances
the survival of hematopoietic and mesenchymal stem cells (11, 12). The
expression of an undersialylated form of ANGPTL4 in renal podocytes contributes
to proteinuria and nephrotic syndrome (13). The immune-inhibitory receptor
human leukocyte immunoglobulin-like receptor B2 (LILRB2) and its mouse
orthologue paired immunoglobulin-like receptor (PIRB) have been identified as
receptors for several ANGPTLs (14) including ANGPTL4.
-
Zhu, P. et al. (2012) Biosci. Rep. 32:211.
- Ge, H. et al. (2004) J. Biol. Chem. 279:2038.
- Sukonina, V. et al. (2006) Proc. Natl. Acad. Sci. USA 103:17450.
- Mandard, S. et al. (2006) J. Biol. Chem. 281:934.
- Xu, A. et al. (2005) Proc. Natl. Acad. Sci. USA 102:6086.
- Kersten, S. et al. (2000) J. Biol. Chem. 275:28488.
- Cazes, A. et al. (2006) Circ. Res. 99:1207.
- Le Jan, S. et al. (2003) Am. J. Pathol. 162:1521.
- Goh, Y.Y. et al. (2010) Am. J. Pathol. 177:2791.
- Goh, Y.Y. et al. (2010) J. Biol. Chem. 285:32999.
- Blank, U. et al. (2012) Eur. J. Haematol. 89:198.
- Hou, M. et al. (2014) PLoS ONE 9:e85808.
- Clement, L.C. et al. (2011) Nat. Med. 17:117.
- Zhang, C.C. et al. (2012) Nature 485:656.
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