|Reactivity||Human, Mouse, Rat|
|Calculated MW||179145 Da|
|Application & Usage||Western blotting (0.5-4 µg/ml). However, the optimal concentrations should be determined individually. Jurkat cell lysate can also be detected. Reactivity to other species has not been tested.|
|Other Names||LRP-5 , LRP -6|
|Formulation||100 µg (0.5 mg/ml) affinity purified rabbit polyclonal antibody in phosphate-buffered saline (PBS) containing 30% glycerol, 0.5% BSA and 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||LRP-5/6 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor- ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. Plays a role in norrin (NDP) signal transduction (PubMed:27228167). The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta- catenin. Appears be required for postnatal control of vascular regression in the eye (By similarity). Required for posterior patterning of the epiblast during gastrulation (By similarity).|
|Cellular Location||Membrane; Single-pass type I membrane protein. Endoplasmic reticulum. Note=Chaperoned to the plasma membrane by MESD.|
|Tissue Location||Widely expressed, with the highest level of expression in the liver and in aorta|
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Provided below are standard protocols that you may find useful for product applications.
LDL-related proteins LRP-5 and LRP-6. are members of the LDL receptor superfamily, which were found to be involved in the canonical Wnt signaling pathway. Mammalian LRP-6 was shown to bind to Wnt-1 and enhance Induced-induced developmental processes in Xenopus embryos. Mice lacking LRP-6 exhibited developmental defects that are similar to those caused by deficiencies in various Want proteins. Recent work also shows that Want proteins induce the binding of LRP-5 to Axin, leading Axin degradation and β-catenin stabilization.
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