|Other Names||Niemann-Pick C1 protein, NPC1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP13472c was selected from the Center region of NPC1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment. Both NPC1 and NPC2 function as the cellular 'tag team duo' (TTD) to catalyze the mobilization of cholesterol within the multivesicular environment of the late endosome (LE) to effect egress through the limiting bilayer of the LE. NPC2 binds unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes and transfers it to the cholesterol-binding pocket of the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket and is exported from the limiting membrane of late endosomes/ lysosomes to the ER and plasma membrane by an unknown mechanism. Binds oxysterol with higher affinity than cholesterol. May play a role in vesicular trafficking in glia, a process that may be crucial for maintaining the structural and functional integrity of nerve terminals.|
|Cellular Location||Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein|
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This gene encodes a large protein that resides in thelimiting membrane of endosomes and lysosomes and mediatesintracellular cholesterol trafficking via binding of cholesterol toits N-terminal domain. It is predicted to have a cytoplasmicC-terminus, 13 transmembrane domains, and 3 large loops in thelumen of the endosome - the last loop being at the N-terminus. Thisprotein transports low-density lipoproteins to lateendosomal/lysosomal compartments where they are hydrolized andreleased as free cholesterol. Defects in this gene causeNiemann-Pick type C disease, a rare autosomal recessiveneurodegenerative disorder characterized by over accumulation ofcholesterol and glycosphingolipids in late endosomal/lysosomalcompartments.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Fontaine-Bisson, B., et al. Diabetologia 53(10):2155-2162(2010)Kagedal, K., et al. Biochim. Biophys. Acta 1801(8):831-838(2010)Rodriguez-Rodriguez, E., et al. J. Alzheimers Dis. 21(2):619-625(2010)Ma, W., et al. BMC Med. Genet. 11, 149 (2010) :
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