Render Target: STATIC
Render Timestamp: 2024-11-08T09:51:52.462Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-08-01 15:27:06.226
Product last modified at: 2024-10-17T12:45:11.222Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Ribosomal Protein L13a Antibody #2765

Filter:
  • WB

    Supporting Data

    REACTIVITY H Mk
    SENSITIVITY Endogenous
    MW (kDa) 23
    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

    Ribosomal Protein L13a Antibody detects endogenous levels of total ribosomal protein L13a.

    Species Reactivity:

    Human, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence of human ribosomal protein L13a. Antibodies are purified by peptide affinity chromatography.

    Background

    Ribosomal protein L13a (RPL13a, 60S ribosomal protein L13a) is a member of the L13 ribosomal protein family and a structural component of the 60S ribosomal subunit (1). RPL13a appears to play an important role in transcript-specific translational silencing. Interferon-γ induces the phosphorylation of RPL13a and triggers the release of this protein from the 60S ribosomal subunit (2). Free RPL13a protein binds to the GAIT (interferon-γ-activated inhibitor of translation) complex at the 3'-UTR of ceruloplasmin (Cp) mRNA to repress Cp expression (2). RPL13a bound to the GAIT complex interacts with eIF4G, which prevents the recruitment of 43S ribosomal subunit and results in transcript-specific translation suppression (3).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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