Recombinant Human LRP-1 Cluster IV Fc Chimera Protein, CF
Recombinant Human LRP-1 Cluster IV Fc Chimera Protein, CF Summary
Product Specifications
Human LRP1-C4 (Ser3332-Asp3779) Accession # Q07954.2 | IEGRMD | Human IgG1 (Pro100-Lys330) |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
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.
5395-L4B
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
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.
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Scientific Data
When Recombinant Human LRP‑1 Cluster IV Fc Chimera (Catalog # 5395-L4B) is immobilized at 50 ng/mL (100 µL/well), Recombinant Human LRPAP (4296-LR) binds with an ED50 of 0.0250-0.350 ng/mL.
2 μg/lane of Recombinant Human LRP-1 Cluster IV Fc Chimera Protein (Catalog # 5395-L4B) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 100-120 kDa and 200-240 kDa, respectively.
Reconstitution Calculator
Background: LRP-1 Cluster IV
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).
- Lillis, A.P. et al. (2008) Physiol. Rev. 88:887.
- Galliano, M.-F. et al. (2008) PloS ONE 3:e2729.
- Bouchard, B.A. et al. (2007) J. Thromb. Haemost. 6:638.
- Sendra, J. et al. (2008) Cardiovasc. Res. 78:581.
- Takayama, Y. et al. (2005) J. Biol. Chem. 280:18504.
- Martin, A.M. et al. (2008) J. Biol. Chem. 283:12004.
- Cabello-Verugio, C. and E. Brandan (2007) J. Biol. Chem. 282:18842.
- Zilberberg, A. et al. (2004) J. Biol. Chem. 279:17535.
- Taylor, D.R. and N.M. Hooper (2007) Biochem. J. 402:17.
- Parkyn, C.J. et al. (2007) J. Cell Sci. 121:773.
- Herz, J. et al. (1990) EMBO J. 9:1769.
- Strickland, D.K. et al. (1990) J. Biol. Chem. 265:17401.
- Herz, J. et al. (1988) EMBO J. 7:4119.
- Neels, J.G. et al. (1999) J. Biol. Chem. 274:31305.
- Quinn, K.A. et al. (1999) Exp. Cell Res. 251:433.
Citations for Recombinant Human LRP-1 Cluster IV 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.
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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, 2022-10-08;32(0):101367.
Species: N/A
Sample Types: Peptide
Applications: ELISA Capture -
A novel LRP1-binding peptide L57 that crosses the blood brain barrier
Authors: K Sakamoto, T Shinohara, Y Adachi, T Asami, T Ohtaki
Biochem Biophys Rep, 2017-08-12;12(0):135-139.
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay -
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., 2016-10-29;0(0):.
Applications: Bioassay -
Low-density lipoprotein receptor-related protein-1 mediates endocytic clearance of tissue inhibitor of metalloproteinases-1 and promotes its cytokine-like activities.
Authors: 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
PLoS ONE, 2014-07-30;9(7):e103839.
Applications: Bioassay -
LRP1 is a receptor for Clostridium perfringens TpeL toxin indicating a two-receptor model of clostridial glycosylating toxins.
Authors: Schorch B, Song S, van Diemen F, Bock H, May P, Herz J, Brummelkamp T, Papatheodorou P, Aktories K
Proc Natl Acad Sci U S A, 2014-04-15;111(17):6431-6.
Applications: Enzyme Assay -
A small molecule inhibitor to plasminogen activator inhibitor 1 inhibits macrophage migration.
Authors: 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
Arterioscler Thromb Vasc Biol, 2013-03-07;33(5):935-42.
Applications: Bioassay
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