Cat: IPD-X40645

Recombinant Human ENGASE Protein ,His & SUMO

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Analytical Data

  • Gene name

    ENGASE

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Cytosolic endo-beta-N-acetylglucosaminidase; DKFZp434P174; ENASE_HUMAN; ENGase; FLJ21865; Mannosyl glycoprotein endo beta N acetylglucosaminidase

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8NFI3

  • Expression Region

    1-377aa

  • Molecular Weight

    59.1 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

ENGASE, or endo-β-N-acetylglucosaminidase, is an enzyme that plays a crucial role in the deglycosylation of glycoproteins, contributing to various biological processes and cellular functions. The study of ENGASE is significant due to its potential applications in both fundamental research and biotechnology. Understanding the mechanisms by which ENGASE operates can provide insights into protein folding, stability, and the regulation of glycoprotein turnover in the cell. Furthermore, ENGASE can be exploited in therapeutic contexts, such as developing strategies for treating diseases associated with glycoprotein misfolding or overproduction. Research on ENGASE involves a combination of structural biology, enzymology, and molecular genetics, aiming to elucidate the enzyme’s structure-function relationship and its interactions with substrates. Advances in recombinant protein technology enable the production of this enzyme in large quantities, allowing for detailed studies on its biochemical properties and applications in drug development and diagnostics. Overall, the exploration of ENGASE not only enhances our understanding of glycoprotein biology but also opens new avenues for innovative therapeutic interventions.

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