Cat: IPD-X28667

Recombinant Human DCAF12-DDB1 Protein (Baculovirus),Strep & His

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Analytical Data

  • Gene name

    DCAF12-DDB1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    KIAA1892; TCC52; WDR40A

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    Strep;His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q5T6F0 (A2-S453)&Q16531-1

  • Expression Region

    Q5T6F0 (A2-S453)&Q16531-1 (M1-H1140)

  • 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

KMT9a and KMT9b are two closely related proteins that belong to the Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain family, known for their roles in histone methylation and chromatin remodeling. These proteins are involved in the regulation of gene expression through their enzymatic activity, specifically catalyzing the methylation of lysine residues on histone H3, which can lead to transcriptional activation or repression depending on the context. Emerging research has highlighted their vital functions in various biological processes, including development, cell differentiation, and the response to environmental signals. Dysregulation of KMT9a/KMT9b has been implicated in several diseases, including cancer, making these proteins attractive targets for therapeutic interventions. The recombinant expression of KMT9a and KMT9b provides a basis for detailed structural and functional studies, allowing researchers to elucidate their mechanisms of action, substrate specificity, and interaction with other chromatin-modifying complexes. Understanding these aspects is crucial for exploring potential roles of KMT9a/KMT9b in disease progression and for the development of novel epigenetic therapies.

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