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TRIM16 (F3S3I) Rabbit Monoclonal Antibody #38910

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  • IP
  • IF

    Product Specifications

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 70
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50
    Immunofluorescence (Immunocytochemistry) 1:800

    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

    TRIM16 (F3S3I) Rabbit mAb recognizes endogenous levels of total TRIM16 protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala69 of human TRIM16 protein.

    Background

    Misfolded proteins are cleared in cells by ubiquitination and degradation using the proteasome and autophagy pathways (1-5). Various factors, including mutations, oxidative stress, and environmental conditions, can trigger increased protein misfolding and overwhelm cells, resulting in aggregation, accumulation, and disease (2,3). Tripartite Motif-Containing Protein 16 (TRIM16) was first discovered to regulate the NRF2 pathway (3) along with other autophagy proteins, such as Beclin-1, ULK1, and ATG16L, helping to facilitate protein aggregate clearing (1-3,6). TRIM16 plays an important role in cellular defense against oxidative stress and autophagy (4-6). The TRIM family of proteins is highly conserved and has been implicated in a diverse range of biological processes, including development, cell growth, differentiation, innate immune functions, and cancer (4). TRIMs most commonly have a RING finger domain, B-box domains, a coiled-coil domain, and a variable C-terminal domain (4). Specifically, TRIM16 lacks a RING domain but possesses two B-box domains and a C-terminal SPRY domain. TRIM16 has recently been shown to function as an E3 ubiquitin ligase (1,4). TRIM16 is also studied as a tumor suppressor, influencing cell differentiation and migration, and has been implicated in various cancers (7-9), including pancreatic, bladder (9), and breast cancer (7).

    Alternate Names

    E3 ubiquitin-protein ligase TRIM16; EBBP; Estrogen-responsive B box protein; TRI16; TRIM16; tripartite motif containing 16; tripartite motif-containing 16; Tripartite motif-containing protein 16

    For Research Use Only. Not for Use in Diagnostic Procedures.
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