Cat: PA1000-6357

Recombinant Human KMT5A Protein,His

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Analytical Data

  • Gene name

    KMT5A

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    KMT5A;PRSET7;SET07;SET8;N-lysine methyltransferase KMT5A

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9NQR1-2

  • Expression Region

    195-352aa

  • AA Sequence

    KAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVE YHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLG RLINHSKCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASI EAHPWLKH

  • Molecular Weight

    44 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.

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Protein Description

KMT5A, or Lysine Methyltransferase 5A, is a member of the lysine methyltransferase family known for its role in epigenetic regulation through the methylation of lysine residues on histone proteins. This modification plays a critical part in various cellular processes, including gene expression regulation, DNA repair, and cellular differentiation. Research on KMT5A has gained attention due to its potential implications in cancer biology, where aberrant methylation patterns are often associated with tumorigenesis and cancer progression. Dysregulation of KMT5A expression has been linked to several types of cancer, suggesting that it may serve as a therapeutic target or a biomarker for cancer diagnosis and prognosis. In addition, KMT5A's involvement in stem cell biology and developmental processes highlights its significance beyond cancer, making it a key focus for studies exploring epigenetic modifications in health and disease. Understanding KMT5A function and regulation can provide insights into the mechanisms of epigenetic control and lead to the development of novel strategies for disease intervention. Researchers are employing various techniques, including recombinant protein expression, to study KMT5A’s enzymatic activity, substrate specificity, and interaction with other proteins, paving the way for potential applications in targeted therapies and precision medicine.

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