Anti-ERp72 antibody

Supplementary info

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

Activity summary

ERp72 also known as PDIA4 is a protein with a molecular weight of approximately 72 kDa. It belongs to the protein disulfide isomerase (PDI) family and functions as an enzyme within the endoplasmic reticulum (ER). The protein helps with folding by catalyzing the formation rearrangement and breakage of disulfide bonds in nascent proteins. ERp72 is expressed in a variety of tissues with high abundance in the liver pancreas and other secretory organs reflecting its role in protein synthesis and processing.

Biological function summary

The protein disulfide isomerase family member ERp72 plays a significant part in maintaining ER function. It participates in the unfolded protein response (UPR) which ensures proper protein folding and manages ER stress. ERp72 operates as part of a larger multiprotein complex that aids in the quality control of newly synthesized proteins. The protein interacts with calnexin and BiP to perform these functions. This makes ERp72 essential for cellular homeostasis and adaptation to changing physiological conditions.

Pathways

ERp72 is closely involved in the protein folding and ER stress response pathways. The unfolded protein response pathway recognizes misfolded proteins in the ER and initiates mechanisms to restore normal function. It connects with other proteins such as ATF6 and IRE1 to modulate gene expression and improve protein folding capacity. Additionally ERp72 participates in the pathway related to oxidative protein folding working alongside proteins like ERO1. This confirms its key contribution to cellular function by maintaining the balance between protein folding and degradation.

Associated diseases and disorders

Alterations in ERp72 expression or function link to conditions such as neurodegenerative diseases and cancer. Alzheimer's disease shows aberrant ER stress and misfolded protein accumulation where ERp72's interaction with amyloid precursor protein might play a role. In the case of cancer ER stress and UPR pathway alterations contribute to cancer cell survival associating ERp72 with this adaptation process particularly its interaction with BiP and other PDIs. These connections highlight the relevance of ERp72 in disease progression and as a potential therapeutic target.