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NRP1 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 Neuropilin 1 Antibodies (225) and Neuropilin 1 Kits (35) and many more products for this protein.
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Human Neuropilin 1 Protein expressed in Human Cells - ABIN2001890
He, Tessier-Lavigne: Neuropilin is a receptor for the axonal chemorepellent Semaphorin III. in Cell 1997
Show all 5 references for ABIN2001890
Cynomolgus Neuropilin 1 Protein expressed in Human Cells - ABIN2010114
Soker, Takashima, Miao, Neufeld, Klagsbrun: Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. in Cell 1998
Show all 5 references for ABIN2010114
Human Neuropilin 1 Protein expressed in HEK-293 Cells - ABIN2181550
Tamagnone, Artigiani, Chen, He, Ming, Song, Chedotal, Winberg, Goodman, Poo, Tessier-Lavigne, Comoglio: Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates. in Cell 1999
Show all 2 references for ABIN2181550
Human Neuropilin 1 Protein expressed in HEK-293 Cells - ABIN2181552
Appleton, Wu, Maloney, Yin, Liang, Stawicki, Mortara, Bowman, Elliott, Desmarais, Bazan, Bagri, Tessier-Lavigne, Koch, Wu, Watts, Wiesmann: Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding. in The EMBO journal 2007
Show all 2 references for ABIN2181552
NRP-1 (show NELL1 Proteins) was found to be overexpressed in gastric cancer (GC) tissues, and its expression correlates with the clinical staging, tumor differentiation and pathological types of gastric cancer.
Both placental NRP1 and VEGF were expressed at lower levels in women with pre-eclampsia and homocysteine-treated mice, which may contribute to endothelial damage.
NRP1 (show NELL1 Proteins) was targeted by miR130a and miR130b at the binding site of chromosome 10: 334668643466870, which was involved in the axon guidance signaling pathway.
Semaphorin-3a (show SEMA3A Proteins), neuropilin-1 and plexin-A1 (show PLXNA1 Proteins) are axonal guidance molecules that have been recently implicated in regulating bone metabolism.
neuropilin-1 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) 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.
suppression of beta3-integrin (show ITGB3 Proteins) in mice leads to the activation of a neuropilin-1 (NRP1)-dependent cell migration pathway in endothelial cells via a mechanism that depends on NRP1's mobilisation away from mature focal adhesions following VEGF (show VEGFA Proteins)-stimulation
The results show that high vs. low expression of Nrp-1 or Helios (show ZNFN1A2 Proteins) does not unequivocally identify Treg clones of thymic or peripheral origin.
Nrp1 in endothelial cells suppresses TGFbeta (show TGFB1 Proteins) activation and signaling by forming intercellular protein complexes with beta8 integrin.
In vascular sprouting, neuropilin-1 suppresses the stalk-cell phenotype by limiting Smad2 (show SMAD2 Proteins)/3 activation through Alk1 (show ACVRL1 Proteins) and Alk5 (show TGFBR1 Proteins). Notch (show NOTCH1 Proteins) downregulates Nrp1, thus relieving the inhibition of Alk1 (show ACVRL1 Proteins) and Alk5 (show TGFBR1 Proteins), thereby driving stalk-cell behaviour.
NRP1 enables ECM (show MMRN1 Proteins)-induced filopodia formation for tip cell function during sprouting angiogenesis.
demonstrate that in mice on the C57Bl/6 background EMX1 (show EMX1 Proteins) plays an essential role in the midline crossing of an axonal subpopulation of the corpus callosum derived from the anterior cingulate cortex. In the absence of EMX1 (show EMX1 Proteins), cingulate axons display reduced expression of the axon guidance receptor NRP1 and form aberrant axonal bundles within the rostral corpus callosum.
Study showed that Nrp1 expression paralleled with that of DDR2 (show DDR2 Proteins) during osteoblast differentiation. Nrp1 assisted the promoting role of DDR2 (show DDR2 Proteins) in osteoblast differentiation, via activation of DDR2 (show DDR2 Proteins)-mediated downstream signaling.
These findings indicate a new role for Nrp1 in the maintenance of the visceral SMC (show DYM Proteins) contractile phenotype required for normal GI motility in aged mice.
These data suggest that graft rejection occurs, at least in part, through the loss of Nrp1 expression on regulatory CD4 (show CD4 Proteins)(+) T cells, their stability or both.
Neuropilin-1 and its co-receptor plexinA1 (show PLXNA1 Proteins) are necessary to bias the extension of the dendrites of retinal ganglion cells to the apical side of the cell, and ectopically expressed class III semaphorins (Sema3s) disrupt this process.
binding of Neuropilin-1 to VEGFR-2 (show KDR Proteins) requires the PDZ-binding domain of neuropilin-1
Neuropilin-1 is essential for enhanced VEGF(165)-mediated vasodilatation in collateral-dependent coronary arterioles of exercise-trained pigs.
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.
, A5 antigen
, transmembrane receptor
, vascular endothelial cell growth factor 165 receptor
, A5 protein
, Neuropilin-1 precursor (A5 protein)