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

• Reactivity: Hu
• Applications: Binding Activity
• Format: Carrier-Free

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 #: Q07954
• 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

• Dilutions:
  • Binding Activity
• 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

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
• A2MR;APOER;APR;CD91;IGFBP3R;IGFBP-3R;IGFBP3R1;KPA;LRP;LRP1A;Prolow-density lipoprotein receptor-related protein 1;TGFBR5
• 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 PrP^C (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.

Publications for LRP-1 Cluster II (2368-L2)(7)

Publications using 2368-L2

• K Sakamoto Generation of KS-487 as a novel LRP1-binding cyclic peptide with higher affinity, higher stability and BBB permeability Biochemistry and Biophysics Reports, 2022-10-08;32(0):101367. 2022-10-08 [PMID: 36237444] (ELISA Capture, N/A)
• 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, 2017-10-30;2(5):561-574. 2017-10-30 [PMID: 30062170] (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, 2018-04-19;0(0):. 2018-04-19 [PMID: 29679668] (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, 2017-08-12;12(0):135-139. 2017-08-12 [PMID: 29090274] (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., 2016-10-29;0(0):. 2016-10-29 [PMID: 27794518] (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, 2014-07-30;9(7):e103839. 2014-07-30 [PMID: 25075518] (Bioassay)
• 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, 2013-03-07;33(5):935-42. 2013-03-07 [PMID: 23471233] (Bioassay)

Bioinformatics

• Gene Symbol: LRP1
• Uniprot:
  • Q07954(Human)