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Validated All-in-One™ qPCR Primer for LRP6(NM_002336.2) Search again
Product ID:
HQP010877
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ADCAD2, STHAG7
Gene Description:
LDL receptor related protein 6
Target Gene Accession:
NM_002336.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
The LRP6 gene encodes a member of the low density lipoprotein receptor (LDLR) gene family, which consists of cell surface proteins involved in receptor-mediated endocytosis of specific ligands. LDLR proteins are comprised of the same basic structural motifs: an extracellular domain that contains LDLR binding repeats and EGF repeats with associated spacer domains containing the YWTD motif; a single transmembrane-spanning domain; and a C-terminal cytoplasmic domain that generally contains at least 1 copy of the NPXY motif (Brown et al., 1998 [PubMed 9704021]). LRP6 and LRP5 (MIM 603506) function as coreceptors for WNT (MIM 164820) ligands and thus play a role in WNT signaling, which is important in a wide variety of biologic processes during pre- and postnatal life in invertebrates and vertebrates (Kokubu et al., 2004 [PubMed 15469977]).[supplied by OMIM].
Gene References into function
- Wnt canonical signaling through LRP6 establishes a novel mechanism for receptor activation which is opposite to the general paradigm of ligand-induced receptor oligomerization
- role for an LDL receptor-related protein in the regulation of vascular smooth muscle cell proliferation and survival through the evolutionary conserved Wnt signaling cascade.
- LRP6 may function as a potential oncogenic protein by modulating Wnt/beta-catenin signaling
- SOST antagonizes Wnt signaling by binding to the extracellular domain of the Wnt coreceptors LRP5 and LRP6 and disrupting Wnt-induced Frizzled-LRP complex formation.
- Together our results show that in addition to serving as a folding chaperone, Mesd can function as a receptor antagonist by inhibiting ligand binding to mature LRP6.
- a direct interaction between LRP6 and GSK3 results in an attenuation of GSK3 activity
- These data suggest that LRP6, VEGF, and VLDLR may play a role in the risk of developing (age-related macular degeneration)AMD.
- active CKIepsilon generation may induce a negative feedback loop by phosphorylation of sites on LRP5/6 that modulate axin binding and hence beta-catenin degradation
- LRP6 is required for anthrax toxin lethality; LRP6 enables toxin internalization by interacting at the cell surface with PA receptors
- Mesd and LRP6 modulate Wnt signaling.
- These findings suggest a novel mechanism for LRP6 in Wnt signaling: induction of ectodomain shedding of LRP6, followed by the gamma-secretase involved proteolytic releasing its intracellular domain.
- results link a mutation in LRP6 which encodes a co-receptor in the Wnt signaling pathway to coronary artery disease and multiple cardiovascular risk factors
- The finding that GRB10 interferes with the binding of Axin to LRP6 indicated a possible molecular mechanism by which the overexpression of GRB10 suppresses Wnt signaling.
- report the association between common LRP6 variants and late-onset Alzheimer's disease in a multicenter case-control series as well as in a large family-based series ascertained
- it is proposed that Wnts induce coclustering of receptors and Dvl in LRP6-signalosomes, which in turn triggers LRP6 phosphorylation to promote Axin recruitment and beta-catenin stabilization
- Results identify a novel feedback mechanism by which Wnt, including Wnt3a, negatively regulates LRP6 at the mRNA level.
- While secreted Wise either synergizes or inhibits the Wnt signals depending on the partner ligand, ER-retained Wise consistently blocks the Wnt pathway. ER-retained Wise reduces LRP6 on the cell surface, making cells less susceptible to the Wnt signal.
- RSPO1 regulates Wnt signaling by inhibiting internalization of LRP6.
- Both Fz and Dvl functions are critical for Wnt-induced Lrp6 phosphorylation through Fz-Lrp6 interaction. Axin, a key scaffolding protein in the Wnt pathway, is required for Lrp6 phosphorylation via its ability to recruit Gsk3.
- each LRP6 PPPS/TP motif contributes in a combinatorial fashion to activate the canonical Wnt-beta-catenin pathway
- data argue against a human-specific role for LRP6 in anthrax toxin entry and suggest instead that involvement of this protein may be restricted to certain cell types independently of their species of origin
- PPPSP motifs represents a built-in amplifier for Wnt signaling by the LRP6 family of receptors.
- propose that palmitoylation serves to tilt the long, 23-residue transmembrane domain of LRP6 with respect to the plane of membrane to prevent a hydrophobic mismatch and subsequent recognition by the ER quality control
- No association was seen between FRZB, LRP5 and LRP6 variants with radiographic osteoarthritic outcomes in two population-based cohorts
- We found no evidence for a substantial effect of LRP5 or LRP6 SNPs on susceptibility to type 2 diabetes or clinical characteristics of diabetic subjects in Japanese population.
- Kremen may not be essential for Dkk1-mediated Wnt antagonism and Kremen may only play a role when cells express a high level of LRP5/6
- DKK1 inhibition of LRP6 is independent of LRP6 internalization and degradation
- analysis of the structural basis of the interaction between Dkk and low density lipoprotein receptor-related protein (LRP) 5/6
- WNT3 and DKK1 regulate distinct internalization pathways of LRP6 to tune the activation of beta catenin signaling.
- The authors show that LRP6 can indeed form a complex with anthrax toxin receptors, and that this interaction plays a role both in Wnt signalling and in anthrax toxin endocytosis.
- Wnt3a stimulates formation of phosphatidylinositol 4,5-bisphosphate through frizzled & dishevelled; in turn PtdIns (4,5)P2 regulated phosphorylation of LRP6 at Thr1479 & Ser1490; study reveals signaling mechanism for Wnt to regulate LRP6 phosphorylation
- BAMBI interacts with Wnt receptor Frizzled5, coreceptor LRP6, and Dishevelled2 and increases the interaction between Frizzled5 and Dishevelled2
- PTH treatment led to phosphorylation of LRP6 and an increase in amount of beta-catenin in osteoblasts with a concurrent increase in bone formation in rat. Thus, LRP6 coreceptor is a key element of the PTH signaling that regulates osteoblast activity.
- Phosphorylated LRP6/5 both recruits and directly inhibits GSK3beta using two distinct portions of its cytoplasmic sequence.