Cat: PA1000-1368

Recombinant Human NATD1 Protein,His

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Analytical Data

  • Gene name

    NATD1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    NATD1;C17orf103;GTLF3B;Protein NATD1

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8N6N6

  • Expression Region

    1-113aa

  • AA Sequence

    MAHSAAAVPL GALEQGCPIR VEHDRRRRQF TVRLNGCHDR AVLLYEYVGK RIVDLQHTEV PDAYRGRGIA KHLAKAALDF VVEEDLKAHL TCWYIQKYVK ENPLPQYLER LQP

  • 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

NATD1, a member of the N-terminal acetyltransferase family, plays a crucial role in the post-translational modification of proteins through N-terminal acetylation, which is key in regulating protein stability, localization, and function. The study of NATD1 and its recombinant protein has gained attention due to its potential implications in various biological processes and diseases, including cancer and neurodegenerative disorders. Recent advancements in proteomics have highlighted the importance of acetylation in cellular signaling pathways and gene expression regulation. Furthermore, NATD1 is implicated in modulating the activity of essential transcription factors and signaling molecules, thereby influencing cell proliferation and differentiation. Investigating the structural and functional properties of NATD1 recombinant protein allows researchers to delve deeper into its enzymatic mechanisms and substrate specificity. Understanding NATD1’s role in cellular homeostasis and its involvement in disease pathology can pave the way for targeted therapeutic strategies, particularly as altered N-terminal acetylation patterns have been observed in various malignancies. Consequently, ongoing research efforts aim to elucidate the comprehensive functions of NATD1 in vivo and its therapeutic potential, utilizing techniques such as site-directed mutagenesis, mass spectrometry, and in vivo models to explore its biological relevance. With the increasing recognition of protein acetylation as a vital regulatory mechanism, the exploration of NATD1 continues to be a promising frontier in molecular biology and biomedicine.

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