Analytical Data
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Gene name
pep2
- Application
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Alternative Names
Aspartic endopeptidase pep2 (Aspartic protease pep2)
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Species
Neosartorya fumigata
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O42630
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Expression Region
71-398aa
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Molecular Weight
39.7 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
Related Products
Protein Description
Pep2, a peptide derived from the viral protein of a certain pathogen, has gained significant attention in the field of molecular biology and immunology due to its potential therapeutic applications. Recent studies have indicated that Pep2 exhibits robust immunogenic properties, stimulating both humoral and cellular immune responses. This makes it a promising candidate for vaccine development, particularly against viral infections where traditional vaccines may fall short. Researchers have focused on the recombinant production of Pep2 to overcome limitations associated with natural peptide extraction, such as purity and yield. Utilizing advanced expression systems, scientific teams have successfully engineered microbial and eukaryotic hosts to produce high quantities of bioactive Pep2, allowing for in-depth studies on its structure-function relationship and immunogenicity. Furthermore, the ability to modify Pep2 through techniques like site-directed mutagenesis could enhance its efficacy and specificity in immunotherapeutic applications. Overall, the exploration of Pep2 as a recombinant protein represents a pivotal advance in developing innovative strategies to combat infectious diseases, potentially paving the way for new vaccines and therapeutic interventions that harness the power of the immune system.
