Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.1 EU per 1 μg of the protein by the LAL method.
Activity
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-1C2
(Arg786 - Leu1165)
Accession # Q07954IEGRMD Human IgG1
(Pro100 - Lys330)N-terminus C-terminus Accession #
N-terminal Sequence
AnalysisArg786
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
68.1 kDa
SDS-PAGE
90-100 kDa, reducing conditions
2368-L2 |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
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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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).
References:
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.
Long Name:
LDL Receptor-related Protein 1, Cluster II
Entrez Gene IDs:
4035 (Human); 16971 (Mouse); 299858 (Rat)
Alternate Names:
A2MR; Alpha-2-Macroglobulin Receptor; APOER; APR; CD91; LRP1 Cluster II; LRP-1 Cluster II; LRP1; TGFBR5
