Analytical Data
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Gene name
PNGaseF
- Application
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Alternative Names
PNGaseF；png；Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21163
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Expression Region
1-354aa
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AA Sequence
MRKLLIFSISAYLMAGIVSCKGVDSATPVTEDRLALNAVNAPADNTVNIKTFDKVKNAFGDGLSQSAEGTFTFPADVTTVKTIKMFIKNECPNKTCDEWDRYANVYVKNKTTGEWYEIGRFITPYWVGTEKLPRGLEIDVTDFKSLLSGNTELKIYTETWLAKGREYSVDFDIVYGTPDYKYSAVVPVIQYNKSSIDGVPYGKAHTLGLKKNIQLPTNTEKAYLRTTISGWGHAKPYDAGSRGCAEWCFRTHTIAINNANTFQHQLGALGCSANPINNQSPGNWAPDRAGWCPGMAVPTRIDVLNNSLTGSTFSYEYKFQSWTNNGTNGDAFYAISSFVIAKSNTPISAPVVTN
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Molecular Weight
39 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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-N-Glycosidase F, is an enzyme that plays a crucial role in the deglycosylation of glycoproteins, specifically by hydrolyzing the asparagine-linked glycan residues. This enzyme has garnered significant attention in the fields of biotechnology and biomedicine due to its ability to remove oligosaccharides from glycoproteins, thereby facilitating studies on protein structure and function. The research surrounding recombinant PNGase F focuses on optimizing its expression in various host systems, including bacteria, yeast, and mammalian cells, to produce sufficient quantities for industrial and research applications. The ability to produce PNGase F recombinantly enhances its availability, as it can be tailored for specific experimental needs, such as studying glycoprotein interactions, structures, and immunogenic properties. Additionally, PNGase F research is critical for developing therapeutic glycoproteins, as glycosylation patterns significantly influence protein stability, efficacy, and immune response. As glycosylation is a pivotal modification affecting the pharmacokinetics and pharmacodynamics of biologics, understanding the enzymatic action of PNGase F can aid in the design of more effective glycoprotein-based therapies. Hence, ongoing research aims to elucidate the mechanism of action, improve enzyme efficiency, and explore novel applications of PNGase F in glycoprotein analysis and therapeutic advances. The integration of recombinant DNA technology and protein engineering is expected to further enhance the utility of PNGase F in various scientific and industrial fields, driving forward the understanding of glycoprotein biology.
