Recombinant Human BPI Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit LPS-induced IL-8 secretion by THP-1 human acute monocytic leukemia cells. Wilde, C.G. et al. (1994) J. Biol. Chem. 269:17411. The ED50 for this effect is 0.4-2.4 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human BPI protein
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
77.3 kDa (monomer). 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
75-85 kDa, reducing conditions
Publications
Read Publications using 7468-BP in the following applications:
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
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 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 BPI Fc Chimera Protein, CF
bactericidal permeability-increasing protein
bactericidal/permeability-increasing protein
BPI
BPIFD1
CAP 57
rBPI
Background
Bactericidal/Permeability Increasing protein (BPI) is a 55 kDa antibacterial glycoprotein that plays a role in innate immunity (1, 2). It belongs to the lipid transfer protein family that also includes LPS binding protein (LBP), cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). Circulating levels of BPI are positively correlated with the levels of cholesterol, LDL cholesterol, and HDL cholesterol (3). Mature human BPI shares approximately 55% amino acid (aa) sequence identity with mouse and rat BPI. It can be seceted as a monomer or as a disulfide‑linked homodimer (4). It consists of a highly basic N‑terminal and a hydrophobic C‑terminal domain (5). Its N‑terminal domain confers the ability of BPI to bind bacterial lipopolysaccharide (LPS) found in the cell walls of Gram negative bacteria and to induce the lysis and phagocytosis of these bacteria (6‑9). It also blocks the endothelial cell response to endotoxin (10). BPI is stored in neutrophil and eosinophil granules for induced secretion during inflammation (11, 12). It is additionally expressed in mucosal epithelia and testis (10, 13). BPI can be retained on the surface of both neutrophils and epithelial cells, presumably by its hydrophobic C‑terminal domain (8, 10). BPI also functions as an anti-angiogenic molecule by inhibiting vascular endothelial cell proliferation and tubule formation (14). Like the antibacterial actions, this function is mediated by the N‑terminal region (15).
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Holweg, A. et al. (2011) Biochem. Soc. Trans. 39:1045.
Esteve, E. et al. (2010) Thromb. Haemost. 103:780.
Horwitz, A.H. et al. (1996) Protein Exp. Purif. 8:28.
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Ooi, C.E. et al. (1987) J. Biol. Chem. 262:14891.
Tobias, P.S. et al. (1997) J. Biol. Chem. 272:18682.
Weersink, A.J. et al. (1993) J. Immunol. 150:253.
Nishimura, H. et al. (2001) Immunology 103:519.
Canny, G. et al. (2002) Proc. Natl. Acad. Sci. 99:3902.
Weiss, J. and I. Olsson (1987) Blood 69:652.
Calafat, J. et al. (1998) Blood 91:4770.
Lennartsson, A. et al. (2005) J. Leukoc. Biol. 77:369.
van der Schaft, D.W.J. et al. (2000) Blood 96:176.
Rauniyar, R.K. et al. (2002) Invest. Ophthalmol. Vis. Sci. 43:503.
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