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NPC2 encodes a protein containing a lipid recognition domain. Additionally we are shipping NPC2 Proteins (23) and NPC2 Kits (6) and many more products for this protein.
Showing 10 out of 86 products:
Human Polyclonal NPC2 Primary Antibody for IHC, IHC (p) - ABIN4339705
Pernemalm, De Petris, Eriksson, Brandén, Koyi, Kanter, Lewensohn, Lehtiö: Use of narrow-range peptide IEF to improve detection of lung adenocarcinoma markers in plasma and pleural effusion. in Proteomics 2009
Show all 3 Pubmed References
Human Polyclonal NPC2 Primary Antibody for ELISA, WB - ABIN4339704
Légaré, Thabet, Gatti, Sullivan: HE1/NPC2 status in human reproductive tract and ejaculated spermatozoa: consequence of vasectomy. in Molecular human reproduction 2006
Show all 2 Pubmed References
Human Polyclonal NPC2 Primary Antibody for WB - ABIN524003
Giacomini, Ura, Giolo, Luppi, Martinelli, Garcia, Ricci: Comparative analysis of the seminal plasma proteomes of oligoasthenozoospermic and normozoospermic men. in Reproductive biomedicine online 2015
AAV9-mediated NPC1 (show NPC1 Antibodies) delivery significantly promoted Purkinje cell survival, restored locomotor activity and coordination, and increased the lifespan of NPC1 (show NPC1 Antibodies)(-/-) mice. Our work suggests that AAV-based gene therapy is a promising means to treat NPC (show NPC1 Antibodies) disease.
These findings show that NPC2 secreted by premalignant lung tumours suppresses immature macrophage-lineage cell recruitment to the microenvironment in a paracrine manner.
Using the inhibitors of cathepsin enzymatic activity, it was found that cathepsins B and L regulate TNF-alpha (show TNF Antibodies) production, the expression and secretion of NPC2 protein, and the mRNA levels of the genes involved in cholesterol trafficking in macrophages.
Npc1 (show NPC1 Antibodies) and npc2 deficiencies result in pulmonary abnormalities observed in human Niemann-Pick type C disease.
This is the first report demonstrating that GNMT (show GNMT Antibodies) plays an important role in regulating cholesterol homeostasis via interaction with NPC2
NPC1 (show NPC1 Antibodies) and NPC2 proteins participate in endosomal/lysosomal processing of both sphingolipids and cholesterol
In liver, absence of either NPC1 (show NPC1 Antibodies) or NPC2 resulted in similar alterations in the carbohydrate processing of the lysosomal protease, tripeptidyl peptidase I (show TPP1 Antibodies).
The lack of fibronectin (show FN1 Antibodies) did not interfere with reconstruction of collagen fibril organization in response to liver injury.
NPC2 is a positive regulator of biliary cholesterol secretion via stimulation of ABCG5 (show ABCG5 Antibodies)/G8-mediated cholesterol transport.
Studies showed that processing and export of sterol from the late E/L compartment was quantitatively different in mice lacking LAL (show LIPA Antibodies), NPC2, or NPC1 (show NPC1 Antibodies) function.
Overall, we provide a mechanism by which npc2-mediated cholesterol transport is controlled by the membrane composition and how npc2-lipid interactions can regulate the transport rate.
Our results suggest that NPC2 is in a mitochondrially associated autophagosome and plays an important role in regulating mitophagy, mitochondrial quality control, and mitochondrial function.
NEGR1 (show NEGR1 Antibodies) interacts with NPC2 and increases its protein stability
suggest a general mechanism for NPC2 mediated sterol transfer, in which Phe66, Val96, and Tyr100 act as reversible gate keepers. These residues stabilize the sterol in the binding pose via pi-pi stacking but move transiently apart during sterol release
Study demonstrates that Niemann-Pick type C disease can present in early years of life with pulmonary complications like alveolar proteinosis and hepatosplenomegaly or hepatomegaly due to mutation in NPC2 gene.
Our data suggest an incidence rate for NPC1 (show NPC1 Antibodies) and NPC2 of 1/92,104 and 1/2,858,998, respectively. Evaluation of common NPC1 (show NPC1 Antibodies) variants, however, suggests that there may be a late-onset NPC1 (show NPC1 Antibodies) phenotype with a markedly higher incidence.
Structure of glycosylated NPC1 (show NPC1 Antibodies) luminal domain C reveals insights into NPC2 and Ebola virus interactions
hypothesize that, in part, NPC2 rapidly traffics cholesterol between closely appositioned membranes within the multilamellar interior of late endosomal/lysosomal proteins, ultimately effecting cholesterol egress from this compartment
NPC2 may play an important role in negatively regulate cell proliferation.
heterozygous mutations in the NPC1 (show NPC1 Antibodies)/2 gene might be a risk factor for Alzheimer's disease
Data suggest ASM (acid sphingomyelinase (show SMPD1 Antibodies)) activity is regulated by membrane lipids and facilitates cholesterol transfer by NPC2 (Niemann Pick protein type C2); hydrolysis of sphingomyelin by ASM (show SMPD1 Antibodies) may be crucial for endosomal lipid degradation/sorting.
Data show that the effects of the lipids on cholesterol transfer mediated by NPC2 were similar to their effect on membrane fusion induced by NPC2 and saposin-C.
analysis of sterol binding by NPC2, a lysosomal protein deficient in Niemann-Pick type C2 disease
The seminal plasma protein, Niemann-Pick C2 protein, is involved in cholesterol and GM1 depletion within detergent-resistant membrane, then leading to membrane redistribution of P25b that occurs in a very rapid and capacitation-independent manner.
NPC2 plays an important role in endo/lysosomal cholesterol trafficking by markedly accelerating the rates of cholesterol transport. Rates of sterol transfer from and between membranes were increased by as much as 2 orders of magnitude by NPC2.
This gene encodes a protein containing a lipid recognition domain. The encoded protein may function in regulating the transport of cholesterol through the late endosomal/lysosomal system. Mutations in this gene have been associated with Niemann-Pick disease, type C2 and frontal lobe atrophy.
epididymal secretory protein E1
, niemann Pick type C2 protein homolog
, Niemann-Pick disease type C2 protein
, epididymal protein 1
, human epididymis-specific protein 1
, tissue-specific secretory protein
, Niemann Pick type C2
, epididymal secretory protein 1
, 16 kDa secretory protein
, 16kDa secretory protein
, 16.5 kDa secretory protein