research use only

SMYD3 Antibody [P23D23]

Cat.No.: F8492

    Application: Reactivity:
    • F8492-wb
      Lane 1: HCT116, Lane 2: MCF7, Lane 3: Vero

    Usage Information

    Dilution
    1:1000
    Application
    WB
    Reactivity
    Human, 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
    42 kDa

    Datasheet & SDS

    Biological Description

    Specificity
    SMYD3 Antibody [P23D23] detects endogenous levels of total SMYD3 protein.
    Clone
    P23D23
    Synonym(s)
    Histone-lysine N-methyltransferase SMYD3;SET and MYND domain-containing protein 3;Zinc finger MYND domain-containing protein 1;SMYD3;ZMYND1;ZNFN3A1
    Background
    SET and MYND domain–containing protein 3 (SMYD3) is a lysine methyltransferase of the SET‑domain family that shuttles between the nucleus and the cytoplasm and functions as a transcriptional potentiator of cancer‑promoting genes. SMYD3 binds chromatin at promoters and enhancers through its MYND domain and can methylate histone H3 at lysine 4 (H3K4), histone H4 at lysine 5 (H4K5), and possibly histone H4 at lysine 20 (H4K20), deposits that are associated both with transcriptional activation and, in some contexts, with repression through recruitment of factors such as nuclear receptor corepressor complexes, depending on the promoter architecture and interacting partners. SMYD3 methylates non‑histone proteins such as the vascular endothelial growth factor receptor 1 (VEGFR1) on lysine‑831, thereby enhancing its kinase activity and downstream signaling, and can also methylate AKT1 to promote its membrane localization and phosphoactivation, integrating methyltransferase activity with growth‑factor and metabolic‑signaling pathways. SMYD3 is frequently overexpressed in liver, breast, colorectal, and other carcinomas, and enhanced SMYD3 expression drives proliferation, adhesion, and migration of cancer cells, while knockdown or catalytic inactivation of SMYD3 suppresses growth and neoplastic phenotypes. SMYD3 exists as both a full‑length protein and a cleaved isoform lacking the N‑terminal 34 amino acids, and the truncated form shows increased methyltransferase activity toward histone H3.
    References
    • https://pubmed.ncbi.nlm.nih.gov/17998933/
    • https://pubmed.ncbi.nlm.nih.gov/26908355/

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