Recombinant Mouse ANGPTL8/Betatrophin Fc Chimera Protein, CF Summary
Accession # Q8R1L8
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in MOPS,NaCl and CHAPS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in water.|
|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.
When Recombinant Mouse Angiopoietin-like 3 (Catalog # 9899-AN) is immobilized at 1 µg/mL, Recombinant Mouse Betatrophin Fc Chimera (Catalog # 9983-AN) binds with an ED50 of 0.12-0.72 µg/mL.
2 μg/lane of Recombinant Mouse Angiopoietin-like Protein 8/Betatrophin was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 52-56 kDa and 105-110 kDa, respectively.
Background: Angiopoietin-like Protein 8/Betatrophin
Betatrophin (also called ANGPTL8, lipasin and RIPL), a novel secretory protein from liver and fatty tissues, is believed to be involved in lipid and glucose metabolism. It is most homologous to ANGPTL3 but lacks the fibrinogen-like domain of ANGPTL3 and other ANGPTL family members (1). Mouse Betatrophin is 183 amino acids (aa) in length and shares 72% aa identity with human Betatrophin. Betatrophin is a crucial modulator in lipid metabolism. It can form a complex with the N-terminal of ANGPTL3, and the complex is necessary for inhibition of LPL and triglyceride modulation (2). Betatrophin did not control beta-cell expansion in the mouse model (3). In addition to the lipid and glucose metabolism, ANGPTL8 has been reported to be involved in many other disorders (4).
- Quagliarini, F. et al. (2012) PNAS 109(48):19751.
- Chi, X., et al. (2017) Molecular Metabolism 6:1137.
- Cox A.R. et al. PLoS One (2016) 11:e0159276.
- Luo, M. et al. (2018) Front Endocrino 9:169.
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