Anti-LRP6 [1c10]
Invented at Icahn School Of Medicine At Mount Sinai
- Datasheet
- References (6)
- Inventor Info
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![Adapted from van Dinther et al. 2013. PLoS One. 8(4):e62295. PMID: 23638027 Figure. Sclerostin differentially interacts with LRP5/6.
(A) C2C12, C3H10T1/2, ATDC5 and KS483 were affinity labeled using [125I]Sclerostin, followed by chemical crosslinking. Cells were lysed and an immunoprecipitation was performed using LRP5 and LRP6 antibodies. Samples were separated on a SDS-PAGE gel and the radioactive signal was visualized using a phosphorimager screen. The unknown 50 kD band is marked with an asteriks on the short exposure of the KS483 input. (B) C2C12, C3H10T1/2, ATDC5 and KS483 cells were lysed and Western blot was performed to determine the expression of LRP5 and LRP6, GAPDH was used as a loading control. (C) Lysates were made of KS483 control cells (pLKO and NT-shRNA) and KS483 cells with stable LRP5 or LRP6 knockdown. Knockdown efficiency was determined by Western blotting. (D) KS483 control cells and KS483 cells with stable LRP5 or LRP6 knockdown were affinity labeled using [125I]Sclerostin, followed by chemical crosslinking. Cells were lysed and an immunoprecipitation was performed using LRP5 and LRP6 antibodies. LRP5 and LRP6 antibodies do not cross-react (Fig. S1a). Samples were separated on a SDS-PAGE gel and the radioactive signal was visualized using a phosphorimager screen. (E) High molecular weight bands corresponding to LRP5 and LRP6 were quantified using ImageQuant TL v2003.03 software (Amersham Biosciences), and normalized to the pLKO control.](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,q_auto/39bff6ea-5319-4099-8c34-a38e977f82ef.jpg)
![Adapted from van Dinther et al. 2013. PLoS One. 8(4):e62295. PMID: 23638027 Figure. Sclerostin differentially interacts with LRP5/6.
(A) C2C12, C3H10T1/2, ATDC5 and KS483 were affinity labeled using [125I]Sclerostin, followed by chemical crosslinking. Cells were lysed and an immunoprecipitation was performed using LRP5 and LRP6 antibodies. Samples were separated on a SDS-PAGE gel and the radioactive signal was visualized using a phosphorimager screen. The unknown 50 kD band is marked with an asteriks on the short exposure of the KS483 input. (B) C2C12, C3H10T1/2, ATDC5 and KS483 cells were lysed and Western blot was performed to determine the expression of LRP5 and LRP6, GAPDH was used as a loading control. (C) Lysates were made of KS483 control cells (pLKO and NT-shRNA) and KS483 cells with stable LRP5 or LRP6 knockdown. Knockdown efficiency was determined by Western blotting. (D) KS483 control cells and KS483 cells with stable LRP5 or LRP6 knockdown were affinity labeled using [125I]Sclerostin, followed by chemical crosslinking. Cells were lysed and an immunoprecipitation was performed using LRP5 and LRP6 antibodies. LRP5 and LRP6 antibodies do not cross-react (Fig. S1a). Samples were separated on a SDS-PAGE gel and the radioactive signal was visualized using a phosphorimager screen. (E) High molecular weight bands corresponding to LRP5 and LRP6 were quantified using ImageQuant TL v2003.03 software (Amersham Biosciences), and normalized to the pLKO control.](https://res.cloudinary.com/ximbio/image/upload/c_limit,fl_lossy,h_282,q_auto,w_368/39bff6ea-5319-4099-8c34-a38e977f82ef.jpg)
![Image thumbnail for Anti-LRP6 [1c10]](https://res.cloudinary.com/ximbio/image/upload/c_fit,fl_lossy,h_45,q_auto/39bff6ea-5319-4099-8c34-a38e977f82ef.jpg)
| Applications | WB |
| Antigen/Gene or Protein Targets | LRP6 |
| Synonyms | ADCAD2, C030016K15Rik, Cd, FLJ90062, FLJ90421, Low density lipoprotein receptor related protein 6, Low-density lipoprotein receptor-related protein 6, LRP-6 |
| Reactivity | Human and Mouse |
| Relevance | 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. 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. Required for posterior patterning of the epiblast during gastrulation. |
| Host | Mouse |
| Subclass | IgG1 |
| Research Area | Cell Signaling & Signal Transduction, Stem Cell Biology |
References: 6 entries
van Dinther et al. 2013. PLoS One. 8(4):e62295. PMID: 23638027.
Anti-Sclerostin antibody inhibits internalization of Sclerostin and Sclerostin-mediated antagonism of Wnt/LRP6 signaling.
Europe PMC ID: 23638027
Goel et al. 2012. J Biol Chem. 287(20):16454-66. PMID: 22433869.
Both LRP5 and LRP6 receptors are required to respond to physiological Wnt ligands in mammary epithelial cells and fibroblasts.
Europe PMC ID: 22433869
Khan et al. 2007. Mol Cell Biol. 27(20):7291-301. PMID: 17698587.
Analysis of endogenous LRP6 function reveals a novel feedback mechanism by which Wnt negatively regulates its receptor.
Europe PMC ID: 17698587
Add a reference
References: 6 entries
van Dinther et al. 2013. PLoS One. 8(4):e62295. PMID: 23638027.
Anti-Sclerostin antibody inhibits internalization of Sclerostin and Sclerostin-mediated antagonism of Wnt/LRP6 signaling.
Goel et al. 2012. J Biol Chem. 287(20):16454-66. PMID: 22433869.
Both LRP5 and LRP6 receptors are required to respond to physiological Wnt ligands in mammary epithelial cells and fibroblasts.
Khan et al. 2007. Mol Cell Biol. 27(20):7291-301. PMID: 17698587.
Analysis of endogenous LRP6 function reveals a novel feedback mechanism by which Wnt negatively regulates its receptor.
Add a reference
