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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 (5) and many more products for this protein.
Showing 10 out of 70 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 references for 152916
Human Monoclonal NPC1 Primary Antibody for FACS - ABIN2663864
Robertson, Gip, Schaffer: Neural stem cell engineering: directed differentiation of adult and embryonic stem cells into neurons. in Frontiers in bioscience : a journal and virtual library 2007
Show all 3 references for 2663864
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 references for 1724876
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.
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.
Our data show that: i) HDAC2 (show HDAC2 Antibodies) levels and activity are increased in NPC neuronal models and in Npc1(-/-) mice; ii) inhibition of c-Abl (show ABL1 Antibodies) or c-Abl (show ABL1 Antibodies) deficiency prevents the increase of HDAC2 (show HDAC2 Antibodies) protein levels and activity in NPC neuronal models
This study showed that deleting the Npc1 gene is accompanied by an increase in germ cell apoptosis and compensatory imbalances in the expression of cholesterol enzymatic and transporter factors.
These results show that NPC1 is critical for ebolavirus replication and pathogenesis in animals.
abnormal neuronal expression of matrix metalloproteinase-12 (show MMP12 Antibodies) may contribute to axonal degeneration in Niemann-Pick type C disease
There was a transient increase in biliary cholesterol concentration in Npc1(-/-) mice.
data suggest that aberrant expression of Pcdhs is a pathological process accompanied by neurodegeneration in Npc1 mutant mice
This study deministrated that lack of NPC1 in either neurons or glial cells did not affect the excitability of Purkinje cells, the formation of dendrites or their excitatory synaptic activity.
Hearing loss is an early consequence of Npc1 gene deletion in the mouse model of Niemann-Pick disease, type C.
knockdown of TMEM97 (show TMEM97 Antibodies) also increases levels of residual NPC1 in NPC1-mutant patient fibroblasts and reduces cholesterol storage in an NPC1-dependent manner. Our findings propose TMEM97 (show TMEM97 Antibodies) inhibition as a novel strategy to increase residual NPC1 levels in cells and a potential therapeutic target for Niemann-Pick type C disease (NP-C).
Rare loss-of-function NPC1 mutations were identified as being associated with human adiposity with a high penetrance in a Chinese population.
Furthermore saturation and intracellular distribution of alpha-Toc (show RHBDF2 Antibodies) seem to be strongly dependent on the availability of this vitamin as well as on the presence of the lysosomal protein NPC1
Two mutations were identified in the NPC1 gene, one of which was novel and its pathogenetic nature was unknown
Our data suggest an incidence rate for NPC1 and NPC2 (show NPC2 Antibodies) of 1/92,104 and 1/2,858,998, respectively. Evaluation of common NPC1 variants, however, suggests that there may be a late-onset NPC1 phenotype with a markedly higher incidence.
Fibroblasts from Niemann-Pick type C (NPC) disease patients with low levels of NPC1 protein have high amounts of procathepsin D but reduced quantities of the mature protein, thus showing a diminished cathepsin D (show CTSD Antibodies) activity.
Results identified six novel mutations (PKHD1 (show PKHD1 Antibodies): p.Thr777Met, p.Tyr2260Cys; ABCB11 (show ABCB11 Antibodies): p.Val1112Phe, c.611+1G > A, p.Gly628Trpfs*3 and NPC1: p.Glu391Lys) for the diagnostic of inherited infantile cholestatic disorders.
NPC1 mutations are substantially enriched in unexplained early onset ataxia (show USP14 Antibodies), making it high risk group for Niemann-Pick disease type C.
these results clearly demonstrated that the over-expression of NPC1 with a defective function in an imatinib-resistant Ph+ acute lymphoblastic leukemia cell line
Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 (show NPC2 Antibodies) and Ebola virus interactions
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