Render Target: STATIC
Render Timestamp: 2024-11-08T10:09:28.959Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-08-01 15:26:43.005
Product last modified at: 2024-10-10T11:30:13.430Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Ambra1 Antibody #24907

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 135-150
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    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

    Ambra1 Antibody recognizes endogenous levels of total Ambra1 protein. A band of unknown origin is observed at 75 kDa in some cell lines.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu220 of human Ambra1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Activating molecule in Beclin1-regulated autophagy (Ambra1) is a WD40-containing protein expressed during neurodevelopment that is required for neural tube development and autophagy (1). Several studies have identified interactions between Ambra1 with regulators of autophagy and apoptosis (reviewed in 2). Ambra1 was originally found to interact with Beclin-1, a key protein responsible for activating the class III PI3K Vps34 (1). Further studies showed that Ambra1 tethers the Beclin-1-Vps34 complex to the cytoskeletal network through dynein light chains and that during autophagy ULK1 phosphorylates Ambra1, resulting in disassociation with dynein and translocation of the Beclin-Vps34 complex to the endoplasmic reticulum to initiate autophagosome formation (3,4). In addition, it has been found that Ambra1 binds to mitochondrial Bcl-2 and that this interaction is regulated by either apoptosis or autophagy (5,6). Ambra1 also interacts with Parkin, an E3 ubiquitin ligase important for mitophagy, a selective autophagic process of mitochondrial clearance (7,8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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