Cell Signaling Technology

Product Pathways - Development

LRP5 (D23F7) Rabbit mAb #3889

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H Endogenous 200 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

LRP5 (D23F7) Rabbit mAb detects endogenous levels of total LRP5 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro1527 of human LRP5 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using LRP5 (D23F7) Rabbit mAb.

Background

LRP5 and LRP6 are single-pass transmembrane proteins belonging to the low-density lipoprotein receptor (LDLR)-related protein family. Unlike other members of the LDLR family, LRP5 and LRP6 have four EGF and three LDLR repeats in the extracellular domain, and proline-rich motifs in the cytoplasmic domain (1). They function as co-receptors for Wnt and are required for the canonical Wnt/β-catenin signaling pathway (2,3). LRP5 and LRP6 are highly homologous and have redundant roles during development (4,5). The activity of LRP5 and LRP6 can be inhibited by the binding of some members of the Dickkopf (DKK) family of proteins (6,7). Upon stimulation with Wnt, LRP6 is phosphorylated at multiple sites including Thr1479, Ser1490, and Thr1493 by kinases such as GSK-3 and CK1 (8-10). Phosphorylated LRP6 recruits axin to the membrane and presumably activates β-catenin signaling (8-10).

LRP5 is involved in the regulation of bone homeostasis. Mutations and polymorphisms in LPR5 are associated with bone diseases like osteoporosis-pseudoglioma syndrome and high-bone-mass disorders (11-13). In addition, mutations in LRP5 are found in patients with hyperparathyroid tumor and breast cancer (14,15).

  1. Brown, S.D. et al. (1998) Biochem. Biophys. Res. Commun. 248, 879-888.
  2. Pinson, K.I. et al. (2000) Nature 407, 535-538.
  3. Tamai, K. et al. (2000) Nature 407, 530-535.
  4. Kelly, O.G. et al. (2004) Development 131, 2803-2815.
  5. He, X. et al. (2004) Development 131, 1663-1677.
  6. Semënov, M.V. et al. (2001) Curr Biol 11, 951-61.
  7. Bafico, A. et al. (2001) Nat. Cell Biol. 3, 683-668.
  8. Tamai, K. et al. (2004) Mol. Cell 13, 149-156.
  9. Zeng, X. et al. (2005) Nature 438, 873-877.
  10. Davidson, G. et al. (2005) Nature 438, 867-872.
  11. Levasseur, R. et al. (2005) Joint Bone Spine 72, 207-214.
  12. Ferrari, S.L. et al. (2005) Curr. Opin. Lipidol. 16, 207-214.
  13. Balemans, W. and Van Hul, W. (2007) Endocrinology 148, 2622-2629.
  14. Björklund, P. et al. (2007) PLoS Med. 4, e328.
  15. Björklund, P. et al. (2009) PLoS One 4, e4243.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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