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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 69 products:
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 ABIN2663864
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 ABIN1724876
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.
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.
These data show that cholesterol homeostasis through NPC1 plays a crucial role in maintaining insulin (show INS Antibodies) action at multiple levels in adipocytes.
Data suggest that axonal pathologies in Npc1 mutant spinal cord are strongly correlated with the increase of activated glial cells, which produce IL-1beta (show IL1B Antibodies) and ApoE (show APOE Antibodies), resulting in activation of p38-MAPK (show MAPK14 Antibodies) signaling pathway and enhanced phosphorylated tau protein
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
Study determined the crystal structure of the primed GP (GPcl) of Ebola virus bound to domain C of NPC1 (NPC1-C); NPC1-C utilizes two protruding loops to engage a hydrophobic cavity on head of GPcl. Upon enzymatic cleavage and NPC1-C binding, conformational change in the GPcl further affects the state of the internal fusion loop, triggering membrane fusion.
Here, using live cell imaging, the authors obtained evidence that in contrast to the new model, ebolavirus enters cells through endolysosomes that contain both NPC1 and TPC2 (show TPCN2 Antibodies).
These experiments support a model in which NPC1 protein functions to transfer cholesterol past a lysosomal glycocalyx.
An isobaric labeling-based quantitative analysis of proteome of NPC1(I1061T) primary fibroblasts when compared with wild-type cells identified 281 differentially expressed proteins based on stringent data analysis criteria, is reported.
NPC1 gene sequencing revealed that he was a compound heterozygote for the p.S954L and p.N1156S mutations.
results uncover Akt (show AKT1 Antibodies) as a key regulator of NPC1 degradation and link NPC1 to cancer cell proliferation and migration.
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