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

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Catalog# & Formulation Size Price

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

Additional Information
This item is in process of being discontinued.
Details of Functionality
Measured by its binding ability in a functional ELISA. In a Human IgG Fc Antibody (Catalog # G-102-C) coated plate, Recombinant Human LRP‑1 Cluster IV Fc Chimera binds Recombinant Human LRPAP (Catalog # 4296-LR) with an ED50 of 0.25‑1.25 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human LRP-1 Cluster IV protein
Human LRP1-C4
(Ser3332-Asp3779)
Accession # Q07954
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Ser3332
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
LRP1
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
76.7 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
110-120 kDa, reducing conditions
Publications
Read Publications using
5395-L4 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 with Trehalose.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 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 IV Fc Chimera Protein, CF

  • LRP1 Cluster IV
  • LRP-1 Cluster IV

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. 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). Cluster IV (aa 3332-3779) contains eleven LDLR class A repeats (14). 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 (15). Cluster IV contains binding sites for Apolipoprotein E, LPL, and LRPAP/RAP,  alpha 2-macroglobulin, Coagulation Factor VIII light chain, Lactoferrin, PAI-1, tPA-PAI-1 complexes, Pro-uPA, and TFPI (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. 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. Neels, J.G. et al. (1999) J. Biol. Chem. 274:31305.
  15. Quinn, K.A. et al. (1999) Exp. Cell Res. 251:433.

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5395-L4
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Publications for LRP-1 Cluster IV (5395-L4)(6)

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

We have publications tested in 3 applications: Bioassay, ELISA Capture, Enzyme Assay.


Filter By Application
Bioassay
(4)
ELISA Capture
(1)
Enzyme Assay
(1)
All Applications
Filter By Species
Human
(1)
N/A
(1)
All Species
Showing Publications 1 - 6 of 6.
Publications using 5395-L4 Applications Species
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) ELISA Capture N/A
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) 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) 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) Bioassay
Schorch B, Song S, van Diemen F, Bock H, May P, Herz J, Brummelkamp T, Papatheodorou P, Aktories K LRP1 is a receptor for Clostridium perfringens TpeL toxin indicating a two-receptor model of clostridial glycosylating toxins. Proc Natl Acad Sci U S A, 2014-04-15;111(17):6431-6. 2014-04-15 [PMID: 24737893] (Enzyme Assay) Enzyme Assay
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) Bioassay

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Bioinformatics

Gene Symbol LRP1
Uniprot