Analytical Data
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Gene name
PREP
- Application
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Alternative Names
PEP
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P48147
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Expression Region
M1-P710
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Protein Length
Full Length
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Molecular Weight
80.8 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
PREP (Prolyl Endopeptidase) is an endogenous serine protease that plays a significant role in the regulation of various physiological processes, including neuropeptide metabolism and the modulation of neurotransmitter activity. Its relevance has gained attention in the context of neurodegenerative diseases, such as Alzheimer's disease, where the accumulation of amyloid-beta peptides is implicated. Research has demonstrated that PREP can degrade prolyl-containing neuropeptides, thereby influencing synaptic plasticity and cognitive functions. Furthermore, the modulation of PREP activity has emerged as a potential therapeutic target due to its involvement in pathological conditions, including mood disorders and schizophrenia. The characterization of PREP's structure and enzymatic activity is crucial for understanding its biological functions and developing PREP inhibitors as novel therapeutic agents. Recent advances in recombinant protein technology have enabled the production of PREP for detailed study, facilitating the exploration of its mechanisms of action and potential applications in drug development. As the research on PREP continues to evolve, it holds promise for uncovering new insights into the treatment of complex neurological conditions and improving therapeutic approaches.
