Cat: IPD-X36899

Recombinant Human KAT5 Protein,His

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Analytical Data

  • Gene name

    KAT5

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HTATIP; ESA1; HTATIP1; PLIP; TIP; TIP60; cPLA2; HIV-1 Tat Interacting Protein,60kDa; 60 kDa Tat-interactive protein; Lysine acetyltransferase 5; Histone acetyltransferase HTATIP

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    Q92993

  • Expression Region

    Tyr294~Trp513

  • Molecular Weight

    30kDa

  • 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

KAT5, also known as Lysine Acetyltransferase 5, is an essential enzyme involved in various cellular processes, including gene regulation, DNA repair, and cell cycle progression. Its primary function is to acetylate lysine residues on histones and non-histone proteins, thereby modulating chromatin structure and influencing gene expression. Dysregulation of KAT5 has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. The interest in KAT5 research has surged in recent years due to its potential as a therapeutic target. Knowing its role in both pathological and physiological contexts, researchers have focused on unraveling its specific mechanisms of action, substrate specificity, and regulatory pathways. Investigating KAT5 and its interactions with other key molecular players could lead to the development of innovative strategies for disease intervention, including the design of selective inhibitors that could restore normal acetylation patterns in disease states. This makes KAT5 a prominent focus in the fields of epigenetics and drug discovery, as understanding its function could pave the way for novel treatments aimed at correcting acetylation imbalances associated with various health conditions.

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