Cat: PA2000-8002

Recombinant Human GNE Protein,His

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Analytical Data

  • Gene name

    GNE

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    UDP-GlcNAc-2-epimerase/ManAc kinase;hydrolyzing;UDP-GlcNAc-2-epimerase;Uridine diphosphate-N-acetylglucosamine-2-epimerase;ManAc kinase

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9Y223

  • Expression Region

    1-722aa

  • AA Sequence

    MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIY

  • Molecular Weight

    86.2 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

GNE (glucosamine-6-phosphate N-acetyltransferase) is an essential enzyme involved in the biosynthetic pathway of sialic acids, which are crucial for various biological processes, including cell signaling and immune response. Mutations in the GNE gene are associated with a rare genetic disorder known as GNE myopathy, characterized by progressive muscle weakness and atrophy. Understanding the structure and function of GNE, along with the mechanisms by which mutations disrupt its activity, is critical for developing potential therapeutic strategies. Researchers have increasingly turned to recombinant protein techniques to produce GNE for biochemical and biophysical studies, allowing for detailed investigation of its enzymatic activity, interaction with substrates, and the effects of pathogenic mutations. By characterizing the recombinant GNE protein, scientists aim to elucidate the molecular basis of GNE myopathy, paving the way for targeted interventions and improved management of the disease. Additionally, studying the recombinant protein can provide insights into the regulatory mechanisms governing sialic acid biosynthesis, which may have broader implications in understanding other metabolic disorders where sialic acids play a significant role. The ongoing research in this field emphasizes the importance of GNE not only in the context of muscle diseases but also in the broader landscape of glycobiology and its impact on human health.

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