Analytical Data
-
Gene name
PPC-DC
- Application
-
Alternative Names
COAC; PPC-DC
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96CD2
-
Expression Region
Met1~Ser204
-
Molecular Weight
26kDa
-
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
PPC-DC, or Prolyl-Dependent Carboxypeptidase Dipeptidase, is a protein of considerable interest in the field of biochemistry due to its role in protein maturation and cellular function. The enzyme is primarily involved in post-translational modifications, which are crucial for the biological activity of various proteins. Understanding PPC-DC is essential for unraveling its mechanism in metabolic processes, as it is believed to influence significant pathways related to protein degradation, processing of neuropeptides, and modulation of signaling molecules. Research into PPC-DC has been spurred by its potential links to various diseases, including neurodegenerative disorders and cancer, where disruption of protein processing plays a crucial role. By examining its structure, enzymatic function, and regulatory mechanisms, scientists aim to develop targeted therapies that could mitigate the impacts of diseases associated with PPC-DC dysfunction. Furthermore, advances in recombinant DNA technology have allowed for the production of PPC-DC in laboratory settings, enabling in-depth studies of its biochemical properties and interactions, thereby facilitating the exploration of its therapeutic potentials and implications in biomedical research. This comprehensive understanding of PPC-DC is critical for pioneering novel approaches in drug development and improving therapeutic strategies in clinical applications.
