Cat: IPD-X31772

Recombinant Others PNGase F Protein,His

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Analytical Data

  • Gene name

    PNGase F

  • 简介

    The PNGase F protein acts as an enzyme catalyst that specifically cleaves entire glycans from glycoproteins. This process depends on the replacement of the glycosylated asparagine moiety by a polypeptide chain at both its amino (R1) and carboxyl (R2) termini, as shown in Reaction 1. PNGase F Protein, F. meningosepticum (His) is the recombinant PNGase F protein, expressed by E. coli , with N-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PNGase F; PNGF; Peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine Amidase F

  • Species

    Others

  • Source

    E. coli

  • Tag

    N-6*His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P21163

  • Expression Region

    A41-N354

  • AA Sequence

    APADNTVNIKTFDKVKNAFGDGLSQSAEGTFTFPADVTTVKTIKMFIKNECPNKTCDEWDRYANVYVKNKTTGEWYEIGRFITPYWVGTEKLPRGLEIDVTDFKSLLSGNTELKIYTETWLAKGREYSVDFDIVYGTPDYKYSAVVPVIQYNKSSIDGVPYGKAHTLGLKKNIQLPTNTEKAYLRTTISGWGHAKPYDAGSRGCAEWCFRTHTIAINNANTFQHQLGALGCSANPINNQSPGNWAPDRAGWCPGMAVPTRIDVLNNSLTGSTFSYEYKFQSWTNNGTNGDAFYAISSFVIAKSNTPISAPVVTN

  • Protein Length

    Full Length of Mature Protein

  • Molecular Weight

    35 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

PNGase F, or Peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidase F, is an important glycosidase enzyme derived from the bacterium Elizabethkingia miricola. Its primary function is to cleave the N-glycans from glycoproteins, specifically targeting the bond between the asparagine residue and the N-acetylglucosamine moiety. The relevance of PNGase F has grown significantly in biomedicine and biotechnology due to its potential applications in glycoprotein analysis and therapeutic glycoprotein production. As the demand for biopharmaceuticals continues to rise, understanding the structural and functional properties of recombinant PNGase F enables researchers to utilize it effectively for the deglycosylation of proteins. This is crucial for both the characterization of glycoproteins and the enhancement of their therapeutic efficacy by improving drug stability and bioavailability. Recent advancements in recombinant DNA technology have facilitated the production of PNGase F in large quantities, allowing for detailed studies on its mechanism and specificity. Moreover, the enzyme's ability to function optimally under various conditions makes it a versatile tool in glycoproteomics. Ongoing research aims to explore the enzyme's potential for industrial applications, such as biocatalysis and bioprocessing in the production of glycosylated products. The continued investigation into PNGase F is expected to contribute significantly to advancements in glycoscience, aiding in the development of novel therapeutic strategies and improving existing biopharmaceuticals by leveraging its unique enzymatic properties.

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