Recombinant Human Angiopoietin-like 4 Biotin Protein, CF
Recombinant Human Angiopoietin-like 4 Biotin Protein, CF Summary
Product Specifications
Gly26-Arg161, with 3xGSL and a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
BT8249
| Formulation | Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl and CHAPS. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Both Biotinylated recombinant human (rh) ANGPTL4 (Catalog # BT8249) and unlabeled rhANGPTL4 (Catalog # 8249-AN) stimulate the expansion of E16-E18 rat liver mononuclear cellsin vitro, in the presence of recombinant mouse (rm) SCF (Catalog # 455-MC), rmTpo (Catalog # 488-TO), and rmFlt-3L (Catalog # 427-FL). The ED50 for this effect is 25-125 ng/mL in the presence of a cross-linking antibody, His Tag MAb (Catalog # MAB050). The similarity in activity highlights that the biotinylated protein is fully functional.
Reconstitution Calculator
Background: Angiopoietin-like Protein 4/ANGPTL4
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). Within the
N-terminal region, it shares approximately 67% aa sequence identity with mouse and rat ANGPTL4. 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 human, 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).
- 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.
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