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NPC1 encodes a large protein that resides in the limiting membrane of endosomes and lysosomes and mediates intracellular cholesterol trafficking via binding of cholesterol to its N-terminal domain. Additionally we are shipping NPC1 Proteins (10) and NPC1 Kits (6) and many more products for this protein.
Showing 10 out of 81 products:
Chinese Hamster Polyclonal NPC1 Primary Antibody for EM, ICC - ABIN152916
Infante, Abi-Mosleh, Radhakrishnan, Dale, Brown, Goldstein: Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein. in The Journal of biological chemistry 2008
Show all 32 Pubmed References
Human Monoclonal NPC1 Primary Antibody for IHC, ELISA - ABIN1724876
Morales, Amigo, Balboa, Acuña, Castro, Molina, Miquel, Nervi, Rigotti, Zanlungo: Deficiency of Niemann-Pick C1 protein protects against diet-induced gallstone formation in mice. in Liver international : official journal of the International Association for the Study of the Liver 2010
Show all 2 Pubmed References
Human Monoclonal NPC1 Primary Antibody for ELISA, WB - ABIN396466
Maetzel, Sarkar, Wang, Abi-Mosleh, Xu, Cheng, Gao, Mitalipova, Jaenisch: Genetic and chemical correction of cholesterol accumulation and impaired autophagy in hepatic and neural cells derived from Niemann-Pick Type C patient-specific iPS cells. in Stem cell reports 2014
this is the first report, showing a role of NPC1 in platelet function and formation but further studies are needed to define how cholesterol storage interferes with these processes
npc1 is required early for proper cell movement and cholesterol localization and later for cell survival
Availability of assays to measure NPC1 binding to membrne proteins may further the understanding of ways in which oxysterols regulate intracellular lipid transport.
Mutation in the NPC1 gene is associated with Niemann-Pick type C.
This study shown Microglia can aggravate olfactory dysfunction by mediating neuronal death in the olfactory bulb (OB) of a murine model of Niemann-Pick disease type C1 (NPC1)
High-resolution respirometry analyses revealed that GSH-EE improved oxidative phosphorylation, coupled respiration and maximal electron transfer in cerebellum of Npc1(-/-) mice
Lysosomal oxLDL accumulation within macrophages contributes to murine atherosclerosis. Prevention of oxLDL uptake leads to decreased atherosclerosis in hematopoietic NPC1-deficient Ldlr (show LDLR Antibodies)(-/-) mice
the spleen is significantly enlarged in Npc1(-/-) mice.
Study is the first data to reveal motor and behavioral deficits in early maturity of Npc1+/- mice.
Npc1 gene interacts with a high fat diet to promote weight gain through differential regulation of central energy metabolism pathways.
AAV9-mediated NPC1 delivery significantly promoted Purkinje cell survival, restored locomotor activity and coordination, and increased the lifespan of NPC1(-/-) mice. Our work suggests that AAV-based gene therapy is a promising means to treat NPC disease.
Here, we identify lamellar inclusions as the subcellular site of lipid accumulation in neurons, we uncover a vicious cycle of cholesterol synthesis and accretion, which may cause gradual neurodegeneration, and we reveal how beta-cyclodextrin, a potential therapeutic drug, reverts these changes. Our study provides new mechanistic insight in NPC disease and uncovers new targets for therapeutic approaches.
Male NPC1+/- mice had increased fat storage while eating a high-fat diet.
pronounced alterations in several proteins linked to autophagy and lysosomal catabolism reflecting vesicular transport obstruction and defective lysosomal turnover resulting from NPC1 deficiency, were observed.
Niemann-Pick C1 (NPC1) protein structures suggest mapping of all of the disease-causing mutations for future molecular insights into the pathogenesis of Niemann-Pick type C disease (NPC) disease.
This study demonistrated that heterozygous mutations of NPC1 genes could contribute to dementia plus, at least in a subset of patients.
Docking of the NPC1-NPC2 (show NPC2 Antibodies) complex onto the full-length NPC1 structure reveals a direct cholesterol transfer tunnel between NPC2 (show NPC2 Antibodies) and N-terminal domain cholesterol binding pockets, supporting the "hydrophobic hand-off" cholesterol transfer model.
Taken together, these studies suggest that Ebola virus requires phosphatidylinositol (3,5) bisphosphate production in cells to promote efficient delivery to NPC1.
identification of NPC1 and/or NPC2 (show NPC2 Antibodies) mutations combined with descriptions of clinical phenotype, will improve our knowledge of pathogenic mutations and our understanding of genotype-phenotype correlations.
Here we report a crystal structure of a large fragment of human NPC1 at 3.6 A resolution, which reveals internal twofold pseudosymmetry along TM 2 (show TPM2 Antibodies)-13 and two structurally homologous domains that protrude 60 A into the endosomal lumen, and we propose a model for NPC1 function in cholesterol sensing and transport.
Sequencing of genomic DNA from GM03123 Led to the identification of a mutation in NPC1 GENE, g.41940G>C (c.1947 + 5G>C; rs770321568) (Fig. 1A), with a minor allele frequency of 0.0000082
We identified major events in NPC1 evolution and revealed and compared orthologs and paralogs of the human NPC1 gene through phylogenetic and protein sequence analyses. We predicted whether an amino acid substitution affects protein function by reducing the organism's fitness.
This gene encodes a large protein that resides in the limiting membrane of endosomes and lysosomes and mediates intracellular cholesterol trafficking via binding of cholesterol to its N-terminal domain. It is predicted to have a cytoplasmic C-terminus, 13 transmembrane domains, and 3 large loops in the lumen of the endosome - the last loop being at the N-terminus. This protein transports low-density lipoproteins to late endosomal/lysosomal compartments where they are hydrolized and released as free cholesterol. Defects in this gene cause Niemann-Pick type C disease, a rare autosomal recessive neurodegenerative disorder characterized by over accumulation of cholesterol and glycosphingolipids in late endosomal/lysosomal compartments.
Niemann-Pick C1 protein
, Niemann-Pick type C1 disease protein
, Nasopharyngeal carcinoma 1
, Niemann-Pick C1
, Niemann-Pick disease, type C1
, Niemann-Pick C disease protein