Analytical Data
-
Gene name
XPNPEP3
- Application
-
Alternative Names
APP3; NPHPL1; Aminopeptidase P3
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NQH7
-
Expression Region
Glu253~Gln482
-
Molecular Weight
32kDa
-
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
XPNPEP3, a member of the neprilysin family of metallopeptidases, plays a crucial role in the regulation of peptide digestion and metabolism. As a cytoplasmic enzyme, it is involved in the degradation of various bioactive peptides, including neuropeptides and regulatory peptides, thereby participating in critical physiological processes such as neurotransmission, blood pressure regulation, and immune response. Dysregulation of XPNPEP3 has been implicated in several diseases, including neurodegenerative disorders and cardiovascular conditions. Recent research has focused on the structural and functional characterization of recombinant XPNPEP3 to better understand its catalytic mechanisms and substrate specificity. The production of recombinant XPNPEP3 allows for detailed biochemical studies, enabling researchers to explore its interactions with inhibitors and potential therapeutic applications. The urgency to develop specific inhibitors arises from the enzyme's involvement in pathological conditions, with the goal of creating targeted treatments. Understanding the protein's structure-function relationship is essential for the design of novel pharmacological agents aimed at modulating its activity in various clinical settings. Consequently, research on XPNPEP3 not only enhances our knowledge of protein biochemistry but also contributes to the broader field of drug discovery and development focused on neuropeptide-mediated pathways.
