Recombinant Human LBP (Histidine-tagged) Protein Summary
Product Specifications
Ala26-Val481 with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
6445-LP
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
6445-LP/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in PBS. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: LBP
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).
- Beamer, L.J. et al. (1998) Protein Sci. 7:906.
- Kirschning, C.J. et al. (1997) Genomics 46:416.
- Schroder, N.W.J. & R.R. Schumann (2005) J. Endotoxin Res. 11:237.
- Miyake, K. (2006) J. Endotoxin Res. 12:195.
- Grube, B.J. et al. (1994) J. Biol. Chem. 269:8477.
- Ren, L. et al. (2004) J. Periodont. Res. 39:242.
- Hansen, G.H. et al. (2009) Histochem. Cell Biol. 131:727.
- Dentener, M.A. et al. (2000) Am. J. Respir. Cell Mol. Biol. 23:146.
- Blais, D.R. et al. (2005) Invest. Ophthalmol. Vis. Sci. 46:4235.
- Malm, J. et al. (2005) J. Reprod. Immunol. 66:33.
- Schumann, R.R. et al. (1996) Mol. Cell. Biol. 16:3490.
- Weber, J.R. et. al. (2003) Immunity 19:269.
- Schroder, N.W.J. et al. (2004) J. Immunol. 173:2683.
- Su, G.L. et al. (1994) J. Immunol. 153:743.
- Schroder, N.W.J. et al. (2003) J. Biol. Chem. 178:15587.
- Wright, S.D. et al. (1989) J. Exp. Med. 170:1231.
- Hallatschek, W. et al. (2004) Eur. J. Immunol. 34:1441.
- Schumann, R.R. & E. Latz (2000) Chem. Immunol. 74:42.
- Mannel, D.N. & B. Echtenacher (2000) Chem. Immunol. 74:141.
- Tsukamoto, H. et al. (2010) Int. Immunol. 22:271.
- Heinzelmann, M. & H. Bosshart (2005) J. Immunol. 174:2280.
- Gallay, P. et al. (1993) Infect. Immun. 61:378.
- Levels, J.H.M. et al. (2005) Infect. Immun. 73:2321.
- Hubacek, J.A. et al. (1997) Biochem. Biophys. Res. Commun. 236:427.
- Thompson, P.A. & R.L. Kitchens (2006) J. Immunol. 177:4880.
- Schumann, R.R. et al. (1990) Science 249:1429.
- Theofan, G. et al. (1994) J. Immunol. 152:3623.
Citation for Recombinant Human LBP (Histidine-tagged) Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts
Authors: HK Jun, YJ Jung, S Ji, SJ An, BK Choi
Cell Death Differ., 2017-10-27;0(0):.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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