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

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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

Details of Functionality
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.

Source
Chinese Hamster Ovary cell line, CHO-derived human LRP-1 Cluster III protein
Human LRP-1 Cluster III
(Ser2522 - Ile2941)
Accession # Q07954
DIEGRMD Human IgG1
(Pro100 - Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Ser2522
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
LRP1
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
72.8 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
115-130 kDa, reducing conditions
Publications
Read Publication using 4824-L3.

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 500 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 LRP-1 Cluster III Fc Chimera Protein, CF

  • LRP1 Cluster III
  • LRP-1 Cluster III

Background

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.

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Publications for LRP-1 Cluster III (4824-L3)(1)

We have publications tested in 1 application: Bioassay.


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Bioinformatics

Gene Symbol LRP1
Uniprot