Recombinant Mouse LBP Protein


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Recombinant Mouse LBP Protein 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 0.5-3 ng/mL.

Mouse myeloma cell line, NS0-derived mouse LBP protein
Gly25-Val481 (Ser102Arg, Tyr284His), with a C-terminal 6-His tag
Accession #
N-terminal Sequence
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
51.5 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 Publications using
6635-LP 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 MES, NaCl, PEG and CHAPS with BSA as a carrier protein.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.


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

Alternate Names for Recombinant Mouse LBP Protein

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


LBP (Lipopolysaccharide binding protein) is a 58 ‑ 62 kDa, single-chain glycoprotein member of the BPI/LBP family, BPI/PLUNC/PSP superfamily of lipid-binding proteins (1 - 3). It is secreted by a number of mammalian cell types, including hepatocytes (4), gingival keratinocytes (5), intestinal Paneth cells (6), and type II Greater alveolar cells (7). LBP is considered to be a class 1 APR (acute phase reactant) that is induced upon exposure to both IL-1 and IL-6 (8). These two cytokines appear upon immune cell exposure to pathogenic microbes. Following its synthesis and release, LBP is known to interact with bacterial wall components, lipopolysaccharide/LPS/Lipid A from Gram- (Gm-) bacteria, and lipoteichoic acid/LTA from Gm+ bacteria (9 - 13). In the case of LPS, this interaction appears to occur both in the bacterial cell wall, and within the intercellular space, where LPS micelles naturally form following bacterial death and cell wall dissolution (14 - 17). LBP is posited to induce 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 (15, 18). This CD14:LPS complex activates a TLR4:MD2 membrane complex, resulting in the production of NO and TNF-alpha (19). TNF-alpha serves as a chemoattractant for PMNs, and an initiator of coagulation that helps to wall-off and localize microbial elements (16). Notably, increased concentrations of LBP are also associated with parasitic infections (Trypanosoma), and may contribute to the immune response towards parasites (20). In addition to the above, LBP is also reported to transfer LPS to lipoproteins, particularly HDL and LDL (19, 21 - 23). For LDL, this transfer appears to be inhibitory to monocyte activation; for HDL, the effect may be either stimulatory or inhibitory, depending upon the circumstances (19). Mouse 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) (24). It contains an N‑terminal LPS binding region plus a likely C-terminal LPS transfer region (24 - 25). Mature mouse LBP shares 68% and 88% aa identity with human and rat LBP, respectively (11, 25).

  1. Beamer, L.J. et al. (1998) Protein Sci. 7:906.
  2. Schroder, N.W.J. & R.R. Schumann (2005) J. Endotoxin Res. 11:237.
  3. Miyake, K. (2006) J. Endotoxin Res. 12:195.
  4. Grube, B.J. et al. (1994) J. Biol. Chem. 269:8477.
  5. Ren, L. et al. (2004) J. Periodont. Res. 39:242.
  6. Hansen, G.H. et al. (2009) Histochem. Cell Biol. 131:727.
  7. Dentener, M.A. et al. (2000) Am. J. Respir. Cell Mol. Biol. 23:146.
  8. Schumann, R.R. et al. (1996) Mol. Cell. Biol. 16:3490.
  9. Weber, J.R. et. al. (2003) Immunity 19:269.
  10. Schroder, N.W.J. et al. (2004) J. Immunol. 173:2683.
  11. Su, G.L. et al. (1994) J. Immunol. 153:743.
  12. Schroder, N.W.J. et al. (2003) J. Biol. Chem. 178:15587.
  13. Wright, S.D. et al. (1989) J. Exp. Med. 170:1231.
  14. Hallatschek, W. et al. (2004) Eur. J. Immunol. 34:1441.
  15. Schumann, R.R. & E. Latz (2000) Chem. Immunol. 74:42.
  16. Mannel, D.N. & B. Echtenacher (2000) Chem. Immunol. 74:141.
  17. Tsukamoto, H. et al. (2010) Int. Immunol. 22:271.
  18. Heinzelmann, M. & H. Bosshart (2005) J. Immunol. 174:2280.
  19. Gallay, P. et al. (1993) Infect. Immun. 61:378.
  20. Ngure, R.M. et al. (2009) Res. Vet. Sci. 86:394.
  21. Levels, J.H.M. et al. (2005) Infect. Immun. 73:2321.
  22. Hubacek, J.A. et al. (1997) Biochem. Biophys. Res. Commun. 236:427.
  23. Thompson, P.A. & R.L. Kitchens (2006) J. Immunol. 177:4880.
  24. Lengacher, S. et al. (1995 - 1996) J. Inflamm. 47:165.
  25. Schumann, R.R. et al. (1990) Science 249:1429.

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Gene Symbol Lbp