Human LRP-1 Cluster II Antibody Summary
Accession # Q07954
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
LRP‑1 Cluster II in HepG2 Human Cell Line. LRP‑1 Cluster II was detected in immersion fixed HepG2 human hepatocellular carcinoma cell line using Goat Anti-Human LRP‑1 Cluster II Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2368) at 3 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm and nuclei. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
LRP‑1 Cluster II in Human Liver. LRP‑1 Cluster II was detected in immersion fixed paraffin-embedded sections of human liver using Goat Anti-Human LRP‑1 Cluster II Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2368) at 3 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC004). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cell membranes and cytoplasm. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: LRP-1 Cluster II
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).
- 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.
- Horn, I.R. et al. (1997) J. Biol. Chem. 272:13608.
- Neels, J.G. et al. (1999) J. Biol. Chem. 274:31305.
- Quinn, K.A. et al. (1999) Exp. Cell Res. 251:433.
Citations for Human LRP-1 Cluster II Antibody
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.
Citations: Showing 1 - 2
Filter your results:
Low-Density Lipoprotein Receptor-Related Protein-1 Is a Therapeutic Target in Acuteï¿½Myocardial Infarction
Authors: S Toldo, D Austin, AG Mauro, E Mezzaroma, BW Van Tassel, C Marchetti, S Carbone, S Mogelsvang, C Gelber, A Abbate
JACC Basic Transl Sci, 2017;2(5):561-574.
Applications: Western Blot
Bovine lactoferrin inhibits Japanese encephalitis virus by binding to heparan sulfate and receptor for low density lipoprotein.
Authors: Chien YJ, Chen WJ, Hsu WL, Chiou SS
Sample Types: Whole Cells
No product specific FAQs exist for this product, however you mayView all Antibody FAQs
Cell and Tissue Staining Kits
Reviews for Human LRP-1 Cluster II Antibody
There are currently no reviews for this product. Be the first to review Human LRP-1 Cluster II Antibody and earn rewards!
Have you used Human LRP-1 Cluster II Antibody?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥1250 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image