Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. Also binds alpha2-macroglobulin. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity). Homooligomer. Interacts with VLDLR. Reelin associates with two or more receptor molecules (By similarity). Interacts with DAB1 and JNK-interacting proteins. Interacts with SNX17 (By similarity). Interacts with PCSK9. Interacts with MDK; this interaction is calcium dependent (By similarity). Interacts with CLU (By similarity). A number of isoforms are produced. Mainly in brain. O-glycosylated. Tyrosine phosphorylated upon apoE binding. Belongs to the LDLR family.