Render Target: STATIC
Render Timestamp: 2024-12-20T11:07:56.269Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:59:16.006
Product last modified at: 2024-12-09T12:30:18.885Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

NPC1 (E7S4N) Rabbit mAb #33422

Filter:
  • WB
  • IHC
  • IF

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 190
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunohistochemistry (Paraffin) 1:50 - 1:200
    Immunofluorescence (Immunocytochemistry) 1:800 - 1:1600

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    NPC1 (E7S4N) Rabbit mAb recognizes endogenous levels of total NPC1 protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg1266 of human NPC1 protein.

    Background

    Niemann-Pick type C (NPC) disease is a lysosomal storage disease in which endocytosed cholesterol becomes sequestered in late endosomes/lysosomes (LEs/Ls) due to mutations in either the NPC1 or NPC2 gene, which encode NPC1 (Niemann-Pick type C1) or NPC2 (Niemann-Pick type C2) protein (1,2). NPC1 is a multipass transmembrane protein located at the LEs/Ls membrane, and NPC2 is located in the lumen of the vesicles. NPC2 directly binds to sequestered unesterified cholesterol in the lumen and delivers the cholesterol to the N-terminal domain of membrane-bound NPC1. The cholesterol further interacts with the sterol-sensing domain of NPC1 and is eventually exported from LEs/Ls to Golgi, ER, or plasma membrane (3,4). In cells with dysfunctional NPC1, cholesterol is sequestered in the lysosome, resulting in lysosomal dysfunction and NPC. Loss of function of NPC1 leads to progressive neurodegeneration (5), neuroinflammation and myelin defects, severe neonatal liver disease and lung failure, and immune dysfunction (1,6,7). Elevated NPC1 is linked to cancer progression and drug resistance. Reagents that target NPC1 activity provide opportunities for disease treatment strategies (8,9).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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