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NPX1 encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Additionally we are shipping Neuronal Pentraxin 1 Antibodies (131) and Neuronal Pentraxin 1 Kits (14) and many more products for this protein.
Showing 9 out of 9 products:
Results demonstrate a novel mechanism of neuronal death and predict that inhibition of NP1 expression is a promising strategy to prevent hypoxic-ischemic injury in immature brain
results demonstrate that extracellular release of NP1 promote hypoxic-ischemic neuronal death possibly via surface clustering with GluR1 (show GRIA1 Proteins) at synaptic sites and that NP1, not its family member NP2 (show NRP2 Proteins), is involved in the neuronal death mechanisms
Genetic deletion of NP1 prevents hypoxic-ischemic neuronal death by reducing synaptic clustering of GluR1 (show GRIA1 Proteins).
These findings suggest that Narp (show NPTX2 Proteins) in the mPFC mediates the extinction of morphine conditioned place preference.
our findings demonstrate a novel mechanism by which NP1 regulates mitochondria-driven hippocampal cell death
NP1 facilitates the accumulation of BCL2-associated X protein (BAX (show BAX Proteins)) in mitochondria and regulates mitochondrial dynamics during apoptosis in mouse cerebellar granule neurons in culture.
Neuronal pentraxin 1 induction in hypoxic-ischemic neuronal death is regulated via a glycogen synthase kinase-3alpha/beta dependent mechanism
data indicate that the loss of NP1/2 disrupts several aspects of retinogeniculate development including the initial establishment of AMPAR transmission and the subsequent elimination of inappropriate circuit connections
The Id3 (show ID3 Proteins) and NP1 genes become transcriptionally active after MyoD (show MYOD1 Proteins) induction in undifferentiated myoblasts. This is a stable, heritable event that does not need continued MyoD (show MYOD1 Proteins) activity & is not subject to negative regulation by activated H-Ras (show HRAS Proteins) G12V.
Neuronal pentraxin 1 and 2 are necessary for early synaptic refinements in mammalian retina and dorsal lateral geniculate nucleus. May exert their effects through mechanisms paralleling known role of short pentraxins outside the CNS. (Pentraxin 1 (show CRP Proteins) and 2)
Semaphorin-3a (show SEMA3A Proteins), neuropilin-1 (show NRP1 Proteins) and plexin-A1 (show PLXNA1 Proteins) are axonal guidance molecules that have been recently implicated in regulating bone metabolism.
neuropilin-1 (show NRP1 Proteins) is regulated in the oral epithelium and is selectively up-regulated during epithelial dysplasia
NRP1 (show NELL1 Proteins) over-expression in miR (show MLXIP Proteins)-365 expressing cells could rescue invasion and growth defects of miR (show MLXIP Proteins)-365. In addition, miR (show MLXIP Proteins)-365 expression inversely correlated with NRP1 (show NELL1 Proteins) protein levels in malignant melanoma
VEGF (show VEGFA Proteins)/NRP (show NAP1L1 Proteins)-1axis promotes progression of breast cancer via enhancement of epithelial-mesenchymal transition and activation of NF-kappaB (show NFKB1 Proteins) and beta-catenin (show CTNNB1 Proteins).
Data show that binding of pleiotrophin (PTN (show PTN Proteins)) to neuropilin-1 (NRP-1 (show NRP1 Proteins)) stimulated the internalization and recycling of NRP-1 (show NELL1 Proteins) at the cell surface.
Study found significant down-regulation of placental NRP-1 (show NELL1 Proteins) expression in fetal growth restriction pregnancies complicated with absent end-diastolic flow in the umbilical artery.
PDE4D (show PDE4D Proteins) interacts directly with Neuropilins, positive regulators of Hedgehog (show SHH Proteins) signal transduction pathway.
NPTX1 was significantly associated with bipolar disorder.
MiR (show MLXIP Proteins)-365 can decrease migratory, invasive and proliferative behavior of malignant melanomas by attenuating the expression of NRP1 (show NELL1 Proteins).
Neuropilin (show NRP1 Proteins) has a role as an essential cell surface receptor [review]
This gene encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Neuropilins contain a large N-terminal extracellular domain, made up of complement-binding, coagulation factor V/VIII, and meprin domains. These proteins also contains a short membrane-spanning domain and a small cytoplasmic domain. Neuropilins bind many ligands and various types of co-receptors\; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. Several alternatively spliced transcript variants that encode different protein isoforms have been described for this gene.
neuronal pentraxin 1
, neuronal pentraxin I
, neuronal pentraxin-1
, 47 kDa taipoxin-binding protein
, transmembrane receptor
, vascular endothelial cell growth factor 165 receptor