Cat: IPD-X41831

Recombinant Magnaporthe oryzae CUT1 Protein,His & SUMO

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Analytical Data

  • Gene name

    CUT1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (Cutin hydrolase)

  • Species

    Magnaporthe oryzae

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P30272

  • Expression Region

    17-228aa

  • 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.

Quality inspection process

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Protein Description

The study of recombinant proteins, particularly CUT1, has gained traction due to its potential implications in biotechnology and medicine. CUT1, a protein derived from specific organisms, plays a crucial role in various biological processes, including cell signaling, metabolic pathways, and stress responses. Researchers have been particularly interested in CUT1 due to its unique structural motifs and functional properties that may offer insights into protein interactions and mechanisms of action. The ability to produce CUT1 through recombinant DNA technology allows for its detailed study and application in various fields, including therapeutic development, enzyme engineering, and synthetic biology. Moreover, understanding CUT1's function could lead to innovations in agricultural biotechnology, enhancing crop resilience and productivity. As the scientific community continues to explore the intricacies of CUT1, the ongoing research aims to unravel its molecular structure, elucidate its biological functions, and identify potential applications that can address global challenges in health and sustainability.

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