Analytical Data
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Gene name
pepF
- Application
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Alternative Names
pepF；Pepf；Pepsin A-5
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Species
E.coli
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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
P54125
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Expression Region
1-210aa
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AA Sequence
MNNQYNWNLEVLLNGKSLADNFTELKQLSEQEKALYDGGACFQTKAKFTEFLQLQEKIEVLENRYSNFLSNKHAENSLDKTINDALFQYEMFKSEHALVFVDFEKNLFKHEKVIRAYLQDPALKQYQRDFELVWRNKKHQIDPASQKLLAQISPAWNQADKIFNVLSTADLNLQPVVYKGKTYVINAVSDYQSLLENKDRGLREAAYKVW
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Molecular Weight
40.6 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
PepF is a protein that plays a crucial role in the metabolism of various peptides and has garnered significant interest in the field of biochemistry and molecular biology. It is a member of the peptidase family, characterized by its ability to catalyze the hydrolysis of peptide bonds, which is vital for protein processing and turnover in cells. Research on PepF has expanded due to its potential applications in biotechnology and medicine, particularly in the production of bioactive peptides that could serve as therapeutic agents. Understanding the structure and function of PepF can provide insights into its enzymatic mechanisms and regulation, paving the way for innovative strategies in drug design and development. As scientists explore the reconstitution and engineering of PepF through recombinant DNA technology, there is a growing interest in optimizing its activity and stability for industrial applications, such as in food processing, pharmaceuticals, and environmental bioremediation. Characterizing PepF's specificity, kinetics, and interaction with substrates can illuminate its biological significance and utility. Overall, the study of PepF and its recombinant versions presents exciting opportunities to harness the power of enzymes in various fields, highlighting the importance of such research in advancing our understanding of biological processes and developing new technologies.
