Cat: PA2000-5233

Recombinant Human CUT1 Protein,His

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Analytical Data

  • Gene name

    CUT1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CUT1;CUTL1;Homeobox Protein cut-like 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P30272

  • Expression Region

    17-228aa

  • AA Sequence

    SPIATNVEKPSELEARQLNSVRNDLISGNAAACPSVILIFARASGEVGNMGLSAGTNVASALEREFRNDIWVQGVGDPYDAALSPNFLPAGTTQGAIDEAKRMFTLANTKCPNAAVVAGGYSQGTAVMFNAVSEMPAAVQDQIKGVVLFGYTKNLQNRGRIPDFPTEKTEVYCNASDAVCFGTLFLLPAHFLYTTESSIAAPNWLIRQIRAA

  • Molecular Weight

    35.5 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.

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Protein Description

CUT1, a crucial protein in the field of biochemistry and molecular biology, has garnered attention due to its role in cellular processes such as gene regulation, RNA processing, and stress response. Its functional significance is evident in various organisms, where it contributes to the regulation of metabolic pathways and developmental processes. Researchers have been intrigued by CUT1’s structural characteristics, which reveal potential binding sites for other molecules, thereby implicating it in numerous signaling pathways. Studies have highlighted its involvement in stress response mechanisms, particularly in plants and fungi, where it aids in adaptation to environmental challenges. Additionally, CUT1's evolutionary conservation across species underscores its fundamental biological importance. Investigating CUT1 not only enhances our understanding of its specific functions but also offers insights into broader biological phenomena, potentially paving the way for biotechnological applications in agriculture and medicine. These studies aim to unravel the molecular mechanisms governing CUT1's activity, further elucidating its role in cellular homeostasis and its potential as a target for therapeutic intervention in various diseases.

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