Analytical Data
-
Gene name
Aminopeptidase P2
- Application
-
Alternative Names
Xaa-Pro aminopeptidase 2; Membrane-bound aminopeptidase P; Membrane-bound APP; mAPP; X-prolyl aminopeptidase 2; Xpnpep2;
-
Species
Mouse
-
Source
HEK293
-
Tag
C-8*His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
B1AVD1
-
Expression Region
P23-A650
-
Protein Length
Full Length of Mature Protein
-
Molecular Weight
75-105 kDa
-
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
Aminopeptidase P2 (APP2) is an enzyme that plays a critical role in the hydrolysis of peptide bonds at the amino terminus of proteins, specifically targeting proline residues. This enzyme is particularly significant in various physiological processes, including protein metabolism and regulation of bioactive peptides. Recent studies have highlighted the potential role of APP2 in various pathological conditions, such as cardiovascular diseases, where it may be involved in the modulation of vasoactive peptides. The recombinant expression of APP2 has been a focus of research to facilitate the study of its structure-function relationship and to understand its biochemical properties. By producing recombinant APP2 in a controlled environment, researchers can analyze its enzymatic activity, investigate its substrate specificity, and explore its potential as a therapeutic target. Furthermore, the availability of recombinant APP2 supports the development of inhibitors that could serve as valuable tools in treating diseases linked to dysregulated peptide metabolism. Understanding the functional mechanisms of APP2 could yield insights into new biomedical applications and enhance our knowledge of various enzymatic processes in the human body. Overall, the study of recombinant APP2 is pivotal in advancing our comprehension of this enzyme’s role in health and disease.
