Analytical Data
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Gene name
pepP
- Application
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Alternative Names
Short name: X-Pro aminopeptidase Alternative name(s): Aminoacylproline aminopeptidase Aminopeptidase P Short name: APP
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Species
Mycoplasma pneumoniae
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P75313
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Expression Region
1-354aa
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Molecular Weight
55.6 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
Related Products
Protein Description
Peptide P (pepP) is a protein commonly studied due to its significant role in various biological processes, including cellular signaling, immune responses, and protein-protein interactions. The study of pepP recombinant proteins has gained momentum in the fields of biotechnology and pharmaceuticals, as they offer valuable insights into the structural and functional characteristics of peptides in specific physiological contexts. Researchers have focused on the heterologous expression of pepP in prokaryotic and eukaryotic systems, allowing for the production of high yields of functional peptide for further analysis. The ability to manipulate the genetic sequences coding for pepP paves the way for engineering novel variants with enhanced properties. Moreover, understanding the mechanisms through which pepP interacts with other biomolecules could lead to the development of targeted therapies and diagnostic tools. As the demand for biopharmaceuticals continues to rise, the exploration of pepP recombinant proteins becomes increasingly relevant, promising advancements in drug design and therapeutic interventions. Overall, the comprehensive study of pepP not only illustrates its biological importance but also highlights its potential in improving healthcare outcomes.
