Cat: IPD-X37450

Recombinant Human POMGNT1 Protein (HEK293),His

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Analytical Data

  • Gene name

    POMGNT1

  • 简介

    The POMGNT1 protein crucially directs O-mannosyl glycosylation, which adds N-acetylglucosamine to O-linked mannose residues on glycoproteins. It catalyzes GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr on α-dystroglycan and other O-mannosylated proteins, laying the foundation for subsequent carbohydrate addition. POMGNT1 Protein, Human (HEK293, His) is the recombinant human-derived POMGNT1 protein, expressed by HEK293 , with C-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Protein O-Linked-Mannose Beta-1; 2-N-Acetylglucosaminyltransferase 1; POMGnT1; UDP-GlcNAc:Alpha-D-Mannoside Beta-1; 2-N-Acetylglucosaminyltransferase I.2; POMGNT1; MGAT1.2

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8WZA1-1

  • Expression Region

    L59-T660

  • AA Sequence

    LDTRRAISEANEDPEPEQDYDEALGRLEPPRRRGSGPRRVLDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGEKHSKSPALSSWGDPVLLKTDVPLSSAEEAECHWADTELNRRRRRFCSKVEGYGSVCSCKDPTPIEFSPDPLPDNKVLNVPVAVIAGNRPNYLYRMLRSLLSAQGVSPQMITVFIDGYYEEPMDVVALFGLRGIQHTPISIKNARVSQHYKASLTATFNLFPEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAEDPALLYRVETMPGLGWVLRRSLYKEELEPKWPTPEKLWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMNGYFHEAYFKKHKFNTVPGVQLRNVDSLKKEAYEVEVHRLLSEAEVLDHSKNPCEDSFLPDTEGHTYVAFIRMEKDDDFTTWTQLAKCLHIWDLDVRGNHRGLWRLFRKKNHFLMVGVPASPYSVKKPPSVTPIFLEPPPKEEGAPGAPEQT

  • Protein Length

    Lumenal Domain

  • Molecular Weight

    79 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

POMGNT1, or Protein O-Mannosyltransferase 1, is an enzyme that plays a critical role in glycosylation, specifically in the modification of proteins through the addition of mannose residues. This enzyme is essential for the proper function and stability of various glycoproteins, particularly those involved in muscle structure and function. Mutations in the POMGNT1 gene have been linked to a variety of congenital muscular dystrophies, notably those characterized by congenital myopathy and cognitive impairments, such as muscle-eye-brain disease. Understanding the structure and function of POMGNT1 is vital for elucidating the molecular mechanisms underlying these diseases and facilitating the development of potential therapeutic strategies. Researchers are increasingly focused on producing recombinant POMGNT1 proteins to study their biochemical properties, interactions with substrates, and the pathways of glycosylation. This research could provide insights into the pathogenesis of POMGNT1-related disorders and contribute to advancements in treatment options, including gene therapy and enzyme replacement therapy. The production and characterization of POMGNT1 recombinant proteins also enhance our understanding of glycoprotein biosynthesis and open new avenues for biotechnological applications in both the pharmaceutical and biomedical fields. By integrating structural biology, enzymology, and molecular genetics, ongoing studies aim to map out the functional landscape of POMGNT1 and its potential roles in health and disease, paving the way for innovative solutions to combat associated conditions.

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