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Ribosomal Protein L26 Antibody [L15C18]

Cat.No.: F5830

    Application: Reactivity:

    Usage Information

    Dilution
    1:1000
    Application
    WB
    Reactivity
    Human, Mouse, Rat, Monkey
    Source
    Rabbit Monoclonal Antibody
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years
    Predicted MW
    17 kDa
    Positive Control LN18 cells;293 cells;HeLa cells;PC-12 cells;COS-7 cells
    Negative Control

    Datasheet & SDS

    Biological Description

    Specificity
    Ribosomal Protein L26 Antibody [L15C18] detects endogenous levels of total Ribosomal Protein L26 protein.
    Clone
    L15C18
    Synonym(s)
    Large ribosomal subunit protein uL24; 60S ribosomal protein L26; RPL26
    Background
    Ribosomal protein L26 (RPL26) is a conserved component of the 60S large ribosomal subunit within the eukaryotic ribosome, which comprises around eighty distinct proteins. RPL26 is positioned near the nascent polypeptide exit tunnel in domain I of the 25S/5.8S rRNA and shares structural similarity with the bacterial L24 protein. RPL26 adopts a compact fold featuring sequence repeats and rRNA-binding motifs that are important for stabilizing early pre-60S assembly intermediates in the nucleolus, although its absence leads to only minor rRNA conformational changes without destabilizing adjacent ribosomal proteins such as L39. RPL26 also plays a pivotal role in p53 mRNA-specific translation: following DNA damage, such as that induced by ultraviolet light or chemotherapeutic agents, RPL26 binds the 5' untranslated region of p53 mRNA with high affinity, facilitating ribosomal recruitment, increasing p53 protein synthesis several-fold, and promoting cell cycle arrest and apoptosis through p21 induction. Overexpression of RPL26 can mimic the effects of MDM2 inhibition by selectively elevating p53 levels. RPL26 contributes to optimal maturation of 27S pre-rRNA and efficient export of pre-60S subunits, ensuring wild-type translational accuracy even in the presence of half-mer polysomes, and acting as a sensor that links nucleolar integrity to p53-mediated tumor suppression. Dysregulation of RPL26 is implicated in ribosomopathies resembling Diamond-Blackfan anemia, primarily due to its extra-ribosomal role in controlling p53.
    References
    • https://pubmed.ncbi.nlm.nih.gov/22688513/
    • https://pubmed.ncbi.nlm.nih.gov/25735597/

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