Render Target: STATIC
Render Timestamp: 2024-12-20T10:57:04.966Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-20 06:16:28.008
Product last modified at: 2024-11-02T15:15:07.642Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

nSMase1 Antibody #3867

Filter:
  • WB

    Supporting Data

    REACTIVITY H Mk
    SENSITIVITY Endogenous
    MW (kDa) 50
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

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

    Protocol

    Specificity / Sensitivity

    nSMAase Antibody detects endogenous levels of total nSMase1 protein.

    Species Reactivity:

    Human, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala200 of human nSMase1.

    Background

    Sphingomyelinases (SMases) catalyze the hydrolysis of sphingomyelin to produce ceramide and phosphocholine (1). Ceramide is an important bioactive lipid triggering signal transduction involved in cell proliferation, apoptosis and differentiation (1,2). A number of SMases have been described and categorized based on their optimum pH activity, cation dependence, tissue distribution, and subcellular localization (1). These include a lysosomal acid SMase, a Zn++-dependent secreted acid SMase, a membrane-bound Mg++-dependent neutral SMase, a Mg++-independent neutral SMase, and an alkaline SMase.
    nSMase1 (also termed SMPD2) is a Mg++-dependent neutral SMase that is widely expressed and predominantly localized to the endoplasmic reticulum (3,4). This protein has also been shown to have lyso-platelet activating factor (PAF) phospholipase C activity (5). A second neutral SMase, nSMase2 (also termed SMPD3) is predominantly expressed in the brain (6). The activity of neutral SMases is regulated by oxidative stress, chemotherapeutic drugs, inflammatory cytokines, and apoptotic stimuli (1). Analysis of single and double knockouts of the SMPD2 and SMPD3 has revealed that loss of both genes leads to complete loss of neutral SMase activity with developmental defects observed with loss of nSMase2 (7,8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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