Western blot shows lysates of 293T human embryonic kidney cell line either mock transfected or transfected with human LRP‑6. PVDF Membrane was probed with 1 µg/mL of Goat Anti-Human LRP‑6 Antigen Affinity-purified ...read more
Mouse myeloma cell line NS0-derived recombinant human LRP-6 Ala20-Pro1368 Accession # O75581
Detects human LRP-6 in direct ELISAs and Western blots. In direct ELISAs, approximately 40% cross-reactivity with recombinant mouse LRP-6 is observed, and less than 1% cross-reactivity with recombinant human (rh) LRP-1, rhLRP-4, and rhLRP-5 is observed.
Immunogen affinity purified
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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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Immunogen affinity purified
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for LRP-6 Antibody
low density lipoprotein receptor-related protein 6
low-density lipoprotein receptor-related protein 6
The low-density lipoprotein (LDL) receptor-related protein 5 (LRP-5) and LRP-6 constitute a distinct subgroup of the LDL receptor family. Both LRP-5 and LRP-6 are type I transmembrane proteins that function as co-receptors with Frizzled (FZD) in the canonical Wnt signaling pathway (1, 2). LRP-6 cDNA encodes a 1613 amino acid residue (aa) precursor with a 19 aa signal sequence, a 1353 aa extracellular region, a 23 aa transmembrane (TM) segment and a 218 aa cytoplasmic domain (3). The extracellular region contains four N-terminal cysteine-rich EGF-like repeats, followed by three cysteine-rich LDLR repeats. This pattern of the EGF and LDLR repeat arrangement is different than that typically found in other LDL receptor family proteins. The intracellular region of LRP6 contains protein-protein interaction motifs and is required for canonical Wnt signal transduction (4). Human LRP-6 shares 98% and 74% aa sequence identity with mouse LRP-6 and human LRP-5, respectively. Based on the current model, canonical Wnt signaling requires the interaction of Wnt with FZD and LRP to form a trimeric complex which signals downstream to stabilize cytoplasmic beta -catenin. The stabilized beta -catenin is then translocated to the nucleus where it complexes with the transcription factor LEF/TCF to regulate the transcription of target genes (5). LRP-6 has also been shown to interact with the Dickkopf proteins (DKKs), which are modulators of Wnt signaling (6-8). Binding of DKK-1 to LRP-6 dissociates LRP-6 from FZD, and antagonizes the formation of the functional receptor complex. On cells where the transmembrane proteins Kremens are also present, a ternary complex of LRP-6, DKK-1 and Kremen is formed to trigger the internalization of the complex and removal LRP6 from the cell surface. Thus, DKK-1 and Kremen function synergistically to antagonize LRP-6-mediated Wnt activity. Although DKK-2 also functions as a Wnt antagonist on cells that express Kremen, DKK-2 binding to LRP-6 in the absence of Kremen activates rather than inhibits LRP mediated beta -catenin signaling (9, 10).
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Mao, B. et al. (2002) Nature 417:664.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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