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

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

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

Details of Functionality
Measured by its binding ability in a functional ELISA. When rhLRP-1C2/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 0.5-2.5 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human LRP-1 Cluster II protein
Human LRP-1C2
(Arg786 - Leu1165)
Accession # Q07954
IEGRMD Human IgG1
(Pro100 - Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Arg786
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
LRP1
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.1 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
68.1 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.
SDS-PAGE
90-100 kDa, reducing conditions
Publications
Read Publications using
2368-L2 in the following applications:

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
>90%, 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 II Fc Chimera Protein, CF

  • A2MR
  • Alpha-2-Macroglobulin Receptor
  • APOER
  • APR
  • CD91
  • LRP1 Cluster II
  • LRP-1 Cluster II
  • LRP1
  • TGFBR5

Background

LDL receptor-related protein 1 (LRP-1), also known as CD91 and the alpha 2-macroglobulin receptor, is a type I transmembrane 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 the inhibition of serine proteases (1 - 4). LRP-1 also associates, 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 N glycosylated and sialylated, and cleaved in the Golgi to produce an 85 kDa transmembrane beta chain, and a 515 kDa alpha chain. Both associate noncovalently, with the beta chain remaining completely extracellular (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). Cluster II (aa 786 - 1165) contains one EGF-like and eight LDLR class A repeats (14, 15). Cluster II contains binding sites for Apolipoprotein E, LPL, LRPAP/RAP, alpha 2 Macroglobulin, Coagulation Factor VIII light chain, Lactoferrin, PAI-1, tPA-PAI-1 complexes, Pro-uPA, and TFPI (14, 15). Within this region, human LRP-1 shares 99% aa sequence identity with mouse and rat LRP-1. A shed soluble form of LRP-1 circulates in the serum and retains ligand binding properties (16).

  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. Takayama, Y. et al. (2005) J. Biol. Chem. 280:18504.
  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. Horn, I.R. et al. (1997) J. Biol. Chem. 272:13608.
  15. Neels, J.G. et al. (1999) J. Biol. Chem. 274:31305.
  16. Quinn, K.A. et al. (1999) Exp. Cell Res. 251:433.

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2368-L2
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Publications for LRP-1 Cluster II (2368-L2)(6)

We have publications tested in 2 confirmed species: Human, N/A.

We have publications tested in 2 applications: Bioassay, Surface Plasmon Resonance (SPR.


Filter By Application
Bioassay
(4)
Surface Plasmon Resonance (SPR
(1)
All Applications
Filter By Species
Human
(2)
N/A
(1)
All Species
Showing Publications 1 - 6 of 6.
Publications using 2368-L2 Applications Species
S Toldo, D Austin, AG Mauro, E Mezzaroma, BW Van Tassel, C Marchetti, S Carbone, S Mogelsvang, C Gelber, A Abbate Low-Density Lipoprotein Receptor-Related Protein-1 Is a Therapeutic Target in Acute�Myocardial Infarction JACC Basic Transl Sci, 2017;2(5):561-574. 2017 [PMID: 30062170] (Bioassay) Bioassay
H Ruan, Z Chai, Q Shen, X Chen, B Su, C Xie, C Zhan, S Yao, H Wang, M Zhang, M Ying, W Lu A novel peptide ligand RAP12 of LRP1 for glioma targeted drug delivery J Control Release, 2018;0(0):. 2018 [PMID: 29679668] (Surface Plasmon Resonance (SPR, Human) Surface Plasmon Resonance (SPR Human
K Sakamoto, T Shinohara, Y Adachi, T Asami, T Ohtaki A novel LRP1-binding peptide L57 that crosses the blood brain barrier Biochem Biophys Rep, 2017;12(0):135-139. 2017 [PMID: 29090274] (Bioassay, Human) Bioassay Human
Dudley K Strickland 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 J. Biol. Chem., 2016;0(0):. 2016 [PMID: 27794518] (Bioassay) Bioassay
Thevenard J, Verzeaux L, Devy J, Etique N, Jeanne A, Schneider C, Hachet C, Ferracci G, David M, Martiny L, Charpentier E, Khrestchatisky M, Rivera S, Dedieu S, Emonard H Low-density lipoprotein receptor-related protein-1 mediates endocytic clearance of tissue inhibitor of metalloproteinases-1 and promotes its cytokine-like activities. PLoS ONE, 0;9(7):e103839. 0 [PMID: 25075518]
Ichimura A, Matsumoto S, Suzuki S, Dan T, Yamaki S, Sato Y, Kiyomoto H, Ishii N, Okada K, Matsuo O, Hou F, Vaughan D, van Ypersele de Strihou C, Miyata T A small molecule inhibitor to plasminogen activator inhibitor 1 inhibits macrophage migration. Arterioscler Thromb Vasc Biol, 2013;33(5):935-42. 2013 [PMID: 23471233] (Bioassay, N/A) Bioassay N/A

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Bioinformatics

Gene Symbol LRP1
Uniprot