Render Target: STATIC
Render Timestamp: 2025-01-24T11:54:27.266Z
Commit: 8d9f38232df81570bbc23eaa560b31cb39dd8776
XML generation date: 2024-08-01 15:27:53.317
Product last modified at: 2024-05-30T07:12:44.507Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

TRIM25 Antibody #12315

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Inquiry Info. # 12315

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    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 72
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    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

    TRIM25 Antibody recognizes endogenous levels of total TRIM25 protein.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln146 of human TRIM25 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    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).
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