Recombinant Human GPIHBP1 Fc Chimera Protein, CF Summary
Accession # Q8IV16
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 PBS.|
|Reconstitution||Reconstitute at 500 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.
When Recombinant Human Lipoprotein Lipase (Catalog # 9888-LL) is coated at 2 μg/mL,100 μL/well, Recombinant Human GPIHBP1 Fc Chimera (Catalog # 10091-GB) binds with an ED50 of 1.5-9 μg/mL.
2 μg/lane of Recombinant Human GPIHBP1 Fc Chimera was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 52-63 kDa and 100-130 kDa, respectively.
GPIHBP1 (Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1) is a member of the Ly6 family of proteins (1, 2). Human GPIHBP1 is synthesized as a 184 amino acid (aa) protein that includes a 20 aa signal peptide, a 131 aa GPIHBP1 chain containing the Ly6 domain, and a 33 aa propeptide. Within the main chain region, human GPIHBP1 shares 54% and 53% aa sequence identity with mouse and rat GPIHBP1, respectively. It is found on capillaries of heart, skeletal muscle, and adipose tissue (3), but not expressed in endothelial cells of larger blood vessels or expressed in capillaries of the brain (3, 4). GPIHBP1 binds both lipoprotein lipase (LPL) and chylomicrons (CM), and the acidic domain of GPIHBP1 is required for LPL binding (3, 5). Triglyceride-rich lipoproteins undergo lipolysis by LPL bound by GPIHBP1 and transported across the cells to the capillary lumen (6-7). GPIHBP1 is an important regulator of triglyceride metabolism by increasing the efficiency of lydrolysis by LPL and uptake of fatty acids (3, 8-9).
- Young, S.G. et al. (2011) J. Lipid Res. 52:1869.
- Ioka, R.X. et al. (2003) J. Biol. Chem. 278:7344.
- Beigneux, A.P. et al. (2007). Cell Metab. 5:279.
- Davies, B.S.J. et al. (2010) Cell Metab. 12:42.
- Gin, P. (2008) J. Biol. Chem. 283:29554.
- Davies, B.S. et al. (2012) J. Lipid Res. 53:2690.
- Goulborne, C.N. et al. 2014 Cell Metabolism 19:849.
- Young, S.G. et al. (2007) Curr. Opin. Lipidol. 18:389.
- Sonneburg, W.K. et al. (2009) J Lipid Research 50:2421.
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