Recombinant Human GPIHBP1 Fc Chimera Protein, CF

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.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human GPIHBP1 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Lipoprotein Lipase (Catalog # 9888-LL) is coated at 2 μg/mL (100 μL/well), the concentration of Recombinant Human GPIHBP1 Fc Chimera that produces 50% optimal binding response is 1.5-9 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human GPIHBP1 protein
  

  Human GPIHBP1 (Thr22-Gly151) Accession # Q8IV16	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q8IV16
• N-terminal Sequence: Thr22
• Structure / Form: Disulfide-linked homodimer
• 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:
  • Bioactivity
• Theoretical MW: 41 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: 52-63 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 °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 Human GPIHBP1 Fc Chimera Protein, CF

• glycosylphosphatidylinositol anchored high density lipoprotein binding protein1
• glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein1
• GPI anchored high density lipoprotein binding protein 1
• GPI-Anchored HDL-Binding Protein 1
• GPIHBP1
• GPI-HBP1
• GPI-HBP1LOC338328
• HBP1
• High density lipoprotein-binding protein 1
• HYPL1D

Background

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).

1. Young, S.G. et al. (2011) J. Lipid Res. 52:1869.
2. Ioka, R.X. et al. (2003) J. Biol. Chem. 278:7344.
3. Beigneux, A.P. et al. (2007). Cell Metab. 5:279.
4. Davies, B.S.J. et al. (2010) Cell Metab. 12:42.
5. Gin, P. (2008) J. Biol. Chem. 283:29554.
6. Davies, B.S. et al. (2012) J. Lipid Res. 53:2690.
7. Goulborne, C.N. et al. 2014 Cell Metabolism 19:849.
8. Young, S.G. et al. (2007) Curr. Opin. Lipidol. 18:389.
9. Sonneburg, W.K. et al. (2009) J Lipid Research 50:2421.

Bioinformatics

• Uniprot:
  • Q8IV16()