Cat: IPD-X24777

Recombinant Human SMYD3 Protein (Yeast),His & Myc

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Analytical Data

  • Gene name

    SMYD3

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (SET and MYND domain-containing protein 3)(Zinc finger MYND domain-containing protein 1)

  • Species

    Human

  • Source

    Yeast

  • Tag

    N- Flag & C- His-Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9H7B4

  • Expression Region

    1-428aa

  • Molecular Weight

    53.5 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

SMYD3 (SET and MYND domain-containing protein 3) is a histone methyltransferase primarily recognized for its role in epigenetic regulation by modifying lysine residues on histone proteins, particularly H3K4me3 and H3K9me3. Recent studies have linked SMYD3 to various biological processes, including gene expression regulation, cell proliferation, and differentiation. Dysregulation of SMYD3 has been implicated in several cancers, such as hepatocellular carcinoma and breast cancer, making it a potential therapeutic target. The need for SMYD3 recombinant protein arises from its significance in understanding the molecular mechanisms driving cancer progression and developing novel treatments. By producing and purifying SMYD3 as a recombinant protein, researchers can conduct detailed studies on its enzymatic activity, substrate specificity, and interaction with other epigenetic regulators. Furthermore, recombinant SMYD3 can be utilized in high-throughput screening assays to identify small-molecule inhibitors that could serve as candidates for cancer therapy. Overall, the investigation of SMYD3 through recombinant protein research holds promise for uncovering new insights into epigenetic regulation and potential therapeutic avenues in oncology.

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