Anti-Aspartyl Aminopeptidase antibody [EPR10300]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Aspartyl Aminopeptidase also known as DNPEP is a metallopeptidase enzyme that mechanically cleaves N-terminal aspartic acid residues from peptides. This enzyme has a molecular mass of about 52 kDa. Aspartyl Aminopeptidase is expressed in various tissues with high abundance in liver and kidney. Its subcellular location is mainly the cytosol where it is involved in protein processing and turnover.

Biological function summary

Aspastyl aminopeptidase plays a role in peptide metabolism by trimming aspartic acid residues aiding in protein degradation and maturation. It functions independently and is not known to be part of a larger protein complex. Its activity facilitates the maintenance of normal peptide levels which is essential for various cellular processes.

Pathways

Aspartyl aminopeptidase is involved in the renin-angiotensin system an important regulator of blood pressure and fluid balance. Within this pathway it modulates levels of angiotensin peptides. It also interacts with other proteins such as angiotensin-converting enzyme (ACE) and neprilysin highlighting its importance in cardiovascular homeostasis.

Associated diseases and disorders

Research links aspartyl aminopeptidase to essential hypertension due to its role in the renin-angiotensin system. Abnormal activity of this enzyme might contribute to alterations in angiotensin metabolism therefore impacting blood pressure regulation. Additionally dysregulation may have implications in kidney diseases where interaction with ACE affects renal function and blood pressure control.