Render Target: STATIC
Render Timestamp: 2024-12-20T11:35:04.060Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:53:55.332
Product last modified at: 2024-12-17T18:48:19.568Z
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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.

TRIM25 (D9T7G) Rabbit mAb #13773

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 72
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • 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, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    TRIM25 (D9T7G) Rabbit mAb recognizes endogenous levels of total TRIM25 protein.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln146 of human TRIM25 protein.

    Background

    TRIM25, also termed Estrogen-responsive Finger Protein (EFP), is a member of the tripartite motif-containing (TRIM) family of proteins, characterized by the presence of a RING domain, one or two B-box motifs, and a coiled-coil region (1). TRIM25 was first identified in a search for estrogen-responsive genes (2), and studies have subsequently shown TRIM25 to be overexpressed in many breast cancer tumors (3). A potentially oncogenic role for TRIM25 was suggested by studies showing that suppression of TRIM25 expression inhibited growth of MCF7 cells in vitro and in mouse xenograft models (4). Functional studies largely suggest that TRIM25 functions as a ubiquitin E3 or ISG15 E3 ligase. For example, TRIM25 was shown to induce K63-linked ubiquitination of Rig-I, resulting in Rig-I-mediated activation of downstream signaling cascades that drive the host antiviral innate immune response (5). Notably, it was reported that the influenza A virus non-structural protein 1 inhibits TRIM25-mediated ubiquitination of Rig-I, which may have evolved as a mechanism to evade the host innate immune response (6).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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