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anti-Human LRP4 Antibodies:
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Mammalian Monoclonal LRP4 Primary Antibody for ISt, IHC - ABIN1304795
Barik, Lu, Sathyamurthy, Bowman, Shen, Li, Xiong, Mei: LRP4 is critical for neuromuscular junction maintenance. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2014
Show all 5 Pubmed References
Human Polyclonal LRP4 Primary Antibody for ELISA, WB - ABIN451735
Styrkarsdottir, Halldorsson, Gretarsdottir, Gudbjartsson, Walters, Ingvarsson, Jonsdottir, Saemundsdottir, Snorradóttir, Center, Nguyen, Alexandersen, Gulcher, Eisman, Christiansen, Sigurdsson, Kong et al.: New sequence variants associated with bone mineral density. ... in Nature genetics 2008
Human Polyclonal LRP4 Primary Antibody for ICC, IF - ABIN4331498
Pevzner, Schoser, Peters, Cosma, Karakatsani, Schalke, Melms, Kröger: Anti-LRP4 autoantibodies in AChR- and MuSK-antibody-negative myasthenia gravis. in Journal of neurology 2012
The results showed that LRP4 suppressed both Wnt/beta-Catenin and Notch signaling pathways, and these activities were perturbed either by LRP4 missense mutations or by a knockdown of LRP4.
In vitro experiments demonstrated that LRP4 downregulation significantly inhibited the colony formation, proliferation, migration, and invasion of the three papillary thyroid cancer cell lines.
LRP4 c.2552C>G (p.(T851R) variant was identified in the family with Chiari malformation type 1.
A novel splice variant in LRP4 (c.316+1G > A) segregated with Cenani-Lenz syndactyly phenotype in a five generations family.
LRP4 mutations alter Wnt/beta catenin signaling and cause limb and kidney malformations in Cenani-Lenz syndrome.
the first evidence suggesting that LRP4 is responsible for the retention of sclerostin in the bone environment in humans.
study presents 2 sibling fetuses with a prenatal lethal presentation of mesomelic limb reductions, oligosyndactyly, genitourinary malformation and compound heterozygosity for 2 novel truncating mutations in LRP4
MuSK myasthenia gravis IgG4 disrupts the interaction of LRP4 with MuSK but both IgG4 and IgG1-3 can disperse preformed agrin-independent AChR clusters
LRP4 is essential for maintaining the structural and functional activity of the neuromuscular junction.
LRP4 is a new CMS disease gene and the 3rd beta propeller domain of LRP4 mediates two signaling pathways in a position-specific manner.
[review] Autoantibodies against LRP4 differentially alter neuromuscular transmission, demonstrating how myasthenia gravis can be classified according to the profile of the antibodies; management of myasthenia gravis patients can be adapted accordingly.
pathogenic IgG4 antibodies to MuSK bind to a structural epitope in the first Ig-like domain of MuSK, prevent binding between MuSK and Lrp4, and inhibit Agrin-stimulated MuSK phosphorylation.
Cenani-Lenz syndrome in a large Pakistani pedigree is associated with a novel LRP4 missense mutation.
Data conclude that common variation in the LRP4 gene determines hip and whole body BMD
The roles of LRP4 in muscle fibers and motoneurons in neuromuscular junction formation have been dissected by cell-specific mutation.
Data suggest that LRP4 and interaction between LRP4 and genes in the Wnt and BMP signaling pathways modulate bone phenotypes including peak bone mass and fracture, the clinical endpoint of osteoporosis.
Lrp4 is a cis-acting ligand for MuSK
the interaction of sclerostin with LRP4 is required to mediate the inhibitory function of sclerostin on bone formation, thus identifying a novel role for LRP4 in bone.
The present studies suggest that LRP10 may play a significant role in the brain physiology other than lipoprotein metabolism.
he loss of Lrp4 enhanced the incidence of aberrant retinal folds, which appeared pleated and corrugated in the eyeball.
Wise and Lrp4 are thus likely to control palatal rugae development by regulating reaction-diffusion mechanisms through Shh and Fgf signaling.
Agrin induced an Lrp4-independent increase in dendritic branch complexity, an Lrp4-dependent increase of excitatory synaptic puncta and an Lrp4- and MuSK-independent decrease in the density of puncta containing inhibitory synapse-associated proteins. Results establish selective roles for agrin, Lrp4 and MuSK during dendritogenesis and synaptogenesis in cultured CNS neurons.
the serum sclerostin levels were strongly increased and the level of sclerostin in the tibia was decreased in Lrp4R1170Q/R1170Q mice, confirming the role of LRP4 as an anchor for sclerostin in bone.
The astrocytic Lrp4 plays an important role in ischemic brain injury response. Lrp4 deficiency in astrocytes seems to be protective in response to ischemic brain injury, likely because of the increased ATP release and adenosine-A2AR signaling.
LRP4 is expressed by embryonic cortical and hippocampal neurons, and downregulation of LRP4 in these neurons causes a reduction in density of synapses and number of primary dendrites. Collectively, the results demonstrate an essential and novel role of neuronal LRP4 in dendritic development and synaptogenesis in the central nervous system.
data suggest a model whereby Lrp4 modulates Wnt/beta-catenin signaling via interaction with Wnt ligands and antagonists in a context-dependent manner.
a critical role for Lrp4, in response to agrin, in modulating astrocytic ATP release and synaptic transmission
We show that prepatterning in mice requires Lrp4 but not the MuSK Fz-like domain
The loss of low density lipoprotein receptor-related protein 4 compromised foetal swallowing and breathing-like movements and downregulated the expression of aquaporin-9 in the foetal membrane and aquaporin-1 in the placenta, which possibly affected the amniotic fluid clearance.
Reveal novel roles for APP in regulating neuromuscular synapse formation through hetero-oligomeric interaction with LRP4 and agrin and thereby provide new insights into the molecular mechanisms that govern NMJ formation and maintenance.
Results suggest that mdig may contribute to silica-induced lung fibrosis by altering the balance between Th17 and Treg cells.
These studies demonstrate a role for Lrp4 in hippocampal function.
Lrp4 is a critical player in bone-mass homeostasis.
Data indicate that LRP4 (low-density lipoprotein receptor-related protein 4) deficiency in bone dramatically elevated serum sclerostin levels whereas bone expression of Sost encoding for sclerostin was unaltered.
found by laser capture microdissection that LRP4 expression was induced during chondrocyte differentiation in the growth plate
Mice immunized with the extracellular domain of LRP4 generated anti-LRP4 antibodies & exhibited myasthenia-gravis-associated symptoms & neuromuscular junction abnormality. LRP4 contributes to neuromuscular junction maintenance in adulthood.
Lrp4 is essential for patterning of the mammary placodes.
Lrp4 acts bidirectionally and coordinates synapse formation by binding agrin, activating MuSK and stimulating postsynaptic differentiation, and functioning in turn as a muscle-derived retrograde signal that is necessary and sufficient for presynaptic differentiation
identification of a doublet mutation in complete linkage disequilibrium with syndactyly in one gene of the critical interval: LRP4
autosomal recessive loss-of-function mutations in Megf7/Lrp4 result in a form of syndactyly, mulefoot disease
4 new LRP4 non-synonymous missense point mutations co-segregating in Holstein, German Simmental & Simmental-Charolais families represent independent mutations affecting different conserved protein domains.
This gene encodes a member of the low-density lipoprotein receptor-related protein family. The encoded protein may be a regulator of Wnt signaling. Mutations in this gene are associated with Cenani-Lenz syndrome.
low-density lipoprotein receptor-related protein 4
, multiple epidermal growth factor-like domains 7
, LDLR dan
, low density lipoprotein receptor-related protein 4
, low density lipoprotein receptor-related protein 4-like
, low-density lipoprotein receptor-related protein 4-like