Analytical Data
-
Gene name
DPP2
- Application
-
Alternative Names
DPP2; DPPII; QPP; Dipeptidylpeptidase 7
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UHL4
-
Expression Region
Asp28~Gly486
-
Molecular Weight
55kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Dipeptidyl peptidase 2 (DPP2) is a serine protease that plays a crucial role in various biological processes, including the regulation of protein turnover, immune responses, and cellular signaling. Its enzymatic activity is involved in the cleavage of dipeptides from the N-terminus of polypeptides, which can influence the stability and availability of signaling peptides such as neuropeptides and cytokines. The study of DPP2 has gained significant attention due to its potential implications in various diseases, including cancer, diabetes, and neurodegenerative disorders. The interest in DPP2 as a therapeutic target has prompted researchers to produce recombinant forms of the protein for detailed biochemical characterization and functional studies. Understanding its structural and functional properties can provide insights into its mechanism of action and pave the way for the development of DPP2 inhibitors as novel therapeutic agents. Additionally, the production of recombinant DPP2 allows for the exploration of its roles in pathophysiological conditions, enhancing our understanding of its biological significance. By advancing our knowledge of DPP2 through recombinant protein studies, researchers aim to uncover new avenues for targeted therapies and improve our strategies for managing diseases linked to aberrant DPP2 activity. Overall, the research on DPP2 recombinant protein is vital for elucidating its biological roles and therapeutic potential, signifying its importance in the field of biomedical research.











