Analytical Data
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Gene name
DPEP2
- Application
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9H4A9
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Expression Region
Leu303~Leu486
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Molecular Weight
24kDa
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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
DPEP2, or Dipeptidase 2, is a membrane-bound enzyme that plays a significant role in the metabolism of dipeptides in various biological processes. Its interest in research has increased notably due to its involvement in critical physiological functions, such as the regulation of blood pressure, immune response, and neurotransmission. Recent studies have highlighted the enzyme's potential as a therapeutic target in treating diseases related to metabolic disorders and certain cancers, where altered peptidase activity may contribute to pathophysiology. Moreover, DPEP2's role in the degradation of bioactive peptides suggests its significance in modulating signaling pathways and maintaining homeostasis. The recombinant expression of DPEP2 provides an opportunity for detailed biochemical and structural characterization, facilitating a better understanding of its function and regulation. This research is vital for exploring the enzyme's potential in drug design and development, offering insights into novel therapeutic strategies targeting DPEP2-related pathways. Consequently, the investigation of DPEP2 as a recombinant protein serves not only to elucidate its biological properties but also to assess its application in clinical settings, potentially advancing the field of molecular medicine.
