Recombinant Mouse LRP-6 N-Terminal Fragment Fc Protein, CF

2 μg/lane of Recombinant Mouse LRP‑6 N-Terminal Fragment Fc Chimera 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 200-220 kDa, respectively.

In a Goat Anti-Mouse IgG Fc Antibody (Catalog # G-202-C) coatedplate, Recombinant Mouse LRP‑6 N-Terminal Fragment Fc Chimera(Catalog # 9950-LR) binds Recombinant Mouse Dkk-1 (Catalog # 5897-DK) with anED50 of 15-120 ng/mL.

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse LRP-6 N-Terminal Fragment Fc Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. In a Goat Anti-Mouse IgG Fc Antibody (Catalog # G-202-C) coated plate, Recombinant Mouse LRP‑6 N-Terminal Fragment Fc Chimera binds Recombinant Mouse Dkk-1 (Catalog # 5897-DK) with an ED₅₀ of 15-120 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived mouse LRP-6 protein
  

  Mouse LRP-6 (Ala20-Ile628) Accession # NP_032540	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: NP_032540
• N-terminal Sequence: Ala20
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Theoretical MW: 96 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 100-120 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse LRP-6 N-Terminal Fragment Fc Protein, CF

• ADCAD2
• FLJ90062
• FLJ90421
• low density lipoprotein receptor-related protein 6
• low-density lipoprotein receptor-related protein 6
• LRP6
• LRP-6

Background

The low-density lipoprotein (LDL) receptor-related protein 6 (LRP-6), along with LRP-5, constitute a distinct subgroup of the LDL receptor family (1). Both LRP-5 and LRP-6 are type I transmembrane proteins that function as Wnt co-receptors with Frizzled proteins and mediate the down-regulation of GSK-3 activity and the initiation of the canonical Wnt/beta-catenin signaling cascade (1, 2). Mouse LRP-6 consists of a 19 amino acid (aa) signal sequence, a 1351 aa extracellular domain (ECD), a 23 aa transmembrane domain, and a 20 aa cytoplasmic domain (3). The LRP-6 ECD is composed of four distinct YWTD beta -propeller (BP) motifs followed by three LDLR type A repeats (4). The first two LRP-6 BP motifs bind Wnt-1, -2, -2b, -6, -8a, -9a, -9b, and -10b, while the third and fourth BP motifs bind Wnt-3a (5-10). This product includes the first and second BP motifs of mouse LRP-6 (aa 20-628) that share 98% aa sequence identity with the first two BP motifs of rat and human LRP-6.  Dkk-1, a known antagonist of Wnt signaling, interacts with LRP-6 as a bipartite inhibitor, binding the first and third BP motifs of LRP-6 simultaneously (8, 11). Mice lacking LRP-6 die at birth with a truncation of the axial skeleton, limb defects, microphthalmia, and malformation of the urogenital system (2). Additionally, LRP-6 may be essential for osteoblast differentiation during bone remodeling and, along with LRP-5, is required for postnatal bone development (12, 13).

1. Joiner, D.M. et al. (2013) Trends Endocrinol. Metab. 24:31.
2. Pinson, K.I. et al. (2000) Nature 407:535.
3. Brown, S.D. et al. (1998) Biochem. Biophys. Res. Commun. 248:879.
4. He, X. et al. (2004) Development 131:1663.
5. Ai, M. et al. (2005) Mol. Cell. Biol. 25:4946.
6. Gong, Y. et al. (2010) PLoS One 5:e12682.
7. Itasaki, N. et al. (2003) Development 130:4295.
8. Mao, B. et al. (2001) Nature 411:321.
9. Zhang, Y. et al. (2004) Mol. Cell. Biol. 24:4677.
10. Bourhis, E. et al. (2010) J. Biol. Chem. 285:9172.
11. Ahn, V.E. et al. (2011) Dev. Cell 21:862.
12. Li, C. et al. (2013) J. Bone Miner. Res. 28:2094.
13. Riddle, R.C. et al. (2013) PLoS One 8:e63323.

Bioinformatics

• Uniprot:
  • NP_032540()