Recombinant Human LBP (Histidine-tagged) Protein, CF


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Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human LBP (Histidine-tagged) Protein, CF Summary

Details of Functionality
Measured by its ability to enhance LPS-stimulated IL-8 secretion by THP‑1 human acute monocytic leukemia cells. The ED50 for this effect is 0.25‑1.5 ng/mL.
Mouse myeloma cell line, NS0-derived human LBP protein
Ala26-Val481 with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Structure / Form
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


Theoretical MW
51.7 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.
60-65 kDa, reducing conditions
Read Publication using
6445-LP/CF in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in PBS.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human LBP (Histidine-tagged) Protein, CF

  • LBP
  • lipopolysaccharide binding protein
  • lipopolysaccharide-binding protein
  • LPS-binding protein
  • MGC22233


LBP (Lipopolysaccharide binding protein) is a 58 ‑ 62 kDa, glycoprotein member of the BPI/LBP family of lipid-binding proteins (1 ‑ 4). It is secreted by hepatocytes, gingival keratinocytes, intestinal paneth cells, type II Greater alveolar cells, lacrimal and submandibular gland epithelium, and caudal epididymal epithelium (5 - 10). LBP is a class 1 APR (acute phase reactant) that is induced upon exposure to both IL-1 and IL-6 (11). Following its synthesis and release, LBP interacts with bacterial wall components, lipopolysaccharide/LPS/Lipid A from Gram- (Gm-) bacteria, and lipoteichoic acid/LTA from Gm+ bacteria (12 ‑ 16). In the case of LPS, this interaction occurs both in the bacterial cell wall, and within the intercellular space, where LPS micelles naturally form following bacterial death and cell wall dissolution (17 ‑ 20). LBP induces disassembly of LPS micelles, allowing for LPS binding to LBP, and a heparin-mediated transfer of LPS from LBP to membrane-bound CD14 on the surface of monocytes/macrophages (18, 21). This CD14:LPS complex activates a TLR4:MD2 membrane complex, resulting in the production of NO and TNF alpha (22). TNF alpha serves as a chemoattractant for PMNs, and an initiator of coagulation that helps to wall-off and localize microbial elements (19). In addition to the above, LBP is also reported to transfer LPS to lipoproteins, particularly HDL and LDL (22 ‑ 25). For LDL, this transfer inhibits monocyte activation; for HDL, the effect may be either stimulatory or inhibitory, depending upon the circumstances (22). Human LBP is synthesized as a 481 amino acids (aa) precursor that contains a 25 aa signal sequence and a 456 aa mature region (aa 26 ‑ 481) (26). It contains an N-terminal LPS binding region (aa 29 ‑ 252) plus a likely C-terminal LPS transfer region (aa 276 ‑ 477) (26, 27). There are two potential splice variants. One shows a four aa substitution for aa 154 - 157 coupled to an Ala substitution for aa 266 ‑ 270, while another contains a seven aa substitution for aa 468 ‑ 481. Mature human LBP shares 68% and 69% aa identity with mouse and rat LBP, respectively (14, 22).

  1. Beamer, L.J. et al. (1998) Protein Sci. 7:906.
  2. Kirschning, C.J. et al. (1997) Genomics 46:416.
  3. Schroder, N.W.J. & R.R. Schumann (2005) J. Endotoxin Res. 11:237.
  4. Miyake, K. (2006) J. Endotoxin Res. 12:195.
  5. Grube, B.J. et al. (1994) J. Biol. Chem. 269:8477.
  6. Ren, L. et al. (2004) J. Periodont. Res. 39:242.
  7. Hansen, G.H. et al. (2009) Histochem. Cell Biol. 131:727.
  8. Dentener, M.A. et al. (2000) Am. J. Respir. Cell Mol. Biol. 23:146.
  9. Blais, D.R. et al. (2005) Invest. Ophthalmol. Vis. Sci. 46:4235.
  10. Malm, J. et al. (2005) J. Reprod. Immunol. 66:33.
  11. Schumann, R.R. et al. (1996) Mol. Cell. Biol. 16:3490.
  12. Weber, J.R. et. al. (2003) Immunity 19:269.
  13. Schroder, N.W.J. et al. (2004) J. Immunol. 173:2683.
  14. Su, G.L. et al. (1994) J. Immunol. 153:743.
  15. Schroder, N.W.J. et al. (2003) J. Biol. Chem. 178:15587.
  16. Wright, S.D. et al. (1989) J. Exp. Med. 170:1231.
  17. Hallatschek, W. et al. (2004) Eur. J. Immunol. 34:1441.
  18. Schumann, R.R. & E. Latz (2000) Chem. Immunol. 74:42.
  19. Mannel, D.N. & B. Echtenacher (2000) Chem. Immunol. 74:141.
  20. Tsukamoto, H. et al. (2010) Int. Immunol. 22:271.
  21. Heinzelmann, M. & H. Bosshart (2005) J. Immunol. 174:2280.
  22. Gallay, P. et al. (1993) Infect. Immun. 61:378.
  23. Levels, J.H.M. et al. (2005) Infect. Immun. 73:2321.
  24. Hubacek, J.A. et al. (1997) Biochem. Biophys. Res. Commun. 236:427.
  25. Thompson, P.A. & R.L. Kitchens (2006) J. Immunol. 177:4880.
  26. Schumann, R.R. et al. (1990) Science 249:1429.
  27. Theofan, G. et al. (1994) J. Immunol. 152:3623.

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Publications for LBP (6445-LP/CF)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Bioassay.

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Gene Symbol LBP