Analytical Data
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Gene name
DNPEP
- Application
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Alternative Names
Aspartyl aminopeptidase; ASPEP; DAP; DNPEP; DNPEP_HUMAN
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Species
Human
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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
Q9ULA0
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Expression Region
11-485aa
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Molecular Weight
68.4 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
DNPEP, or Dipeptidase E, is an enzyme that plays a crucial role in the hydrolysis of dipeptides, contributing significantly to various physiological functions including amino acid metabolism and neurotransmitter regulation. Emerging research highlights its involvement in pathological conditions, particularly in cancer and neurodegenerative diseases, where altered dipeptide levels may influence disease progression and symptomatology. As a membrane-bound protein, DNPEP's expression is tightly regulated in different tissues, suggesting a potential role in tissue-specific metabolic processes. The recombinant production of DNPEP offers a valuable tool for studying its molecular mechanisms and designing targeted therapies. Advances in protein engineering and expression systems have facilitated the generation of functional DNPEP variants, enabling detailed characterization of its enzymatic activity and interactions. Comprehensive studies on the structure-function relationship of this enzyme could yield insights into its specificity towards substrates and potential inhibitors. Consequently, understanding DNPEP at the molecular level is pivotal for developing innovative therapeutic strategies that could manipulate its activity in disease contexts, underscoring the necessity for continued research and exploration of this promising biomolecule.
