Recombinant Human LRP-1 Cluster III Fc Chimera Protein, CF

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Recombinant Human LRP-1 Cluster III Fc Chimera Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA.

When recombinant human (rh) LRP‑1 Cluster III Fc Chimera is immobilized at 50 ng/mL (100 μL/well), the concentration of rhLRPAP (Catalog # 4296‑LR) that produces 50% of the optimal binding response is found to be approximately 1-5 ng/mL.

Chinese Hamster Ovary cell line, CHO-derived human LRP-1 Cluster III protein
Human LRP-1 Cluster III
(Ser2522 - Ile2941)
Accession # Q07954
(Pro100 - Lys330)
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
72.8 kDa (monomer)
115-130 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 500 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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 to -70 °C under sterile conditions after reconstitution.
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Background: LRP-1 Cluster III

LDL receptor-related protein 1 (LRP-1), also known as CD91 and the alpha 2-macroglobulin receptor, is a type I membrane protein in the LDL receptor superfamily. It is expressed on neurons, hepatocytes, adipocytes, vascular smooth muscle cells, fibroblasts, keratinocytes, macrophages, and megakaryocytes. LRP-1 is important for the clearance of a large number of circulating molecules involved in fatty acid metabolism and complexes of serine proteases with their inhibitors (1 - 4). LRP-1 also associates directly or through intracellular scaffold proteins with other membrane associated proteins on the same cell. This allows LRP-1 to modulate the activity or internalization of PDGF R beta, NMDA receptor subunits, TGF-beta receptors, Frizzled‑1, various integrins, and the prion protein PrPC (1, 5 ‑ 10). Human LRP-1 is an N‑glycosylated and sialylated molecule that is cleaved in the Golgi to produce an 85 kDa transmembrane  beta chain and a 515 kDa  alpha chain that associates noncovalently with the  beta chain but does not itself cross the membrane (11, 12). The alpha chain of LRP-1 contains 31 LDLR class A repeats, 34 LDLR class B repeats, and 22 EGF‑like repeats (13). The LDLR domains are clustered in four regions throughout the protein (13). LRP-1 Cluster III (aa 2522 ‑ 2941) contains ten LDLR-A cysteine-rich domains (14). Within this region, human LRP-1 shares 97% aa sequence identity with mouse and rat LRP-1. A soluble form of LRP-1 is shed into the serum and cerebrospinal fluid and retains ligand binding properties (15, 16). LRP-1 Cluster III contains binding sites for LRPAP/RAP (14).

  1. Lillis, A.P. et al. (2008) Physiol. Rev. 88:887.
  2. Galliano, M.-F. et al. (2008) PLoS ONE 3:e2729.
  3. Bouchard, B.A. et al. (2007) J. Thromb. Haemost. 6:638.
  4. Sendra, J. et al. (2008) Cardiovasc. Res. 78:581.
  5. Muratoglu, S.C. et al. (2010) J. Biol. Chem. 258:14308.
  6. Martin, A.M. et al. (2008) J. Biol. Chem. 283:12004.
  7. Cabello-Verugio, C. and E. Brandan (2007) J. Biol. Chem. 282:18842.
  8. Zilberberg, A. et al. (2004) J. Biol. Chem. 279:17535.
  9. Taylor, D.R. and N.M. Hooper (2007) Biochem. J. 402:17.
  10. Parkyn, C.J. et al. (2007) J. Cell Sci. 121:773.
  11. Herz, J. et al. (1990) EMBO J. 9:1769.
  12. Strickland, D.K. et al. (1990) J. Biol. Chem. 265:17401.
  13. Herz, J. et al. (1988) EMBO J. 7:4119.
  14. Neels, J.G. et al. (1999) J. Biol. Chem. 274:31305.
  15. Liu, Q. et al. (2009) Mol. Neurodegener. 4:17.
  16. Gorovoy, M. et al. (2010) J. Leukoc. Biol. Jul 7 epub.
Long Name
LDL Receptor-related Protein 1, Cluster III
Entrez Gene IDs
4035 (Human); 16971 (Mouse); 299858 (Rat)
Alternate Names
A2MR;APOER;APR;CD91;IGFBP3R;IGFBP-3R;IGFBP3R1;KPA;LRP;LRP1A;Prolow-density lipoprotein receptor-related protein 1;TGFBR5; LRP1 Cluster III; LRP-1 Cluster III

Citations for Recombinant Human LRP-1 Cluster III Fc Chimera Protein, CF

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.

3 Citations: Showing 1 - 3
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  1. Generation of KS-487 as a novel LRP1-binding cyclic peptide with higher affinity, higher stability and BBB permeability
    Authors: K Sakamoto
    Biochemistry and Biophysics Reports, 2022;32(0):101367.
    Species: N/A
    Sample Types: Peptide
    Applications: ELISA Capture
  2. 2-O, 3-O desulfated heparin mitigates murine chemotherapy- and radiation-induced thrombocytopenia
    Authors: E Tkaczynski, A Arulselvan, J Tkaczynski, S Avery, L Xiao, B Torok-Stor, K Abrams, NV Rao, G Johnson, TP Kennedy, M Poncz, MP Lambert
    Blood Adv, 2018;2(7):754-761.
    Species: Mouse
    Sample Types: Protein
    Applications: ELISA Capture
  3. Evidence that factor VIII forms a bivalent complex with the LDL receptor-related protein 1 (LRP1): Identification of cluster IV on LRP1 as the major binding site
    Authors: Dudley K Strickland
    J. Biol. Chem., 2016;0(0):.
    Applications: Bioassay


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