Anti-PDIA5 antibody

Supplementary info

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

Activity summary

The protein disulfide-isomerase A5 (PDIA5) also known as PDIR serves as an enzyme that catalyzes the formation breakage and rearrangement of disulfide bonds. It weighs approximately 58 kDa. Researchers find PDIA5 expressed in the endoplasmic reticulum especially in tissues with high secretory activity like the pancreas and liver. It participates in protein folding and maintaining cell function by ensuring proper protein structure through disulfide bond formation.

Biological function summary

PDIA5 has important roles in regulating redox homeostasis and protein quality control within the endoplasmic reticulum. It does not operate alone; it functions as part of multi-protein complexes engaging with other chaperones to assist in folding newly synthesized proteins. These interactions prevent protein aggregation and accumulation of misfolded proteins protecting cells from stress.

Pathways

PDIA5 integrates into the unfolded protein response (UPR) and endoplasmic reticulum-associated degradation (ERAD) pathways. It interfaces with other proteins like BiP/GRP78 which enhances its chaperone activity during cellular stress and EDEM1 a protein involved in recognizing misfolded glycoproteins. These pathways work together to maintain cellular homeostasis by managing protein load and degradation processes.

Associated diseases and disorders

Research associates PDIA5 with various conditions including neurodegenerative diseases and cancer. Misfolding and aggregation of proteins linked to PDIA5 malfunction can contribute to disorders like Alzheimer's disease. Moreover PDIA5 may influence cancer progression by interacting with proteins like CALR which also participates in cell stress responses. Understanding PDIA5 functions helps in developing potential therapeutic strategies for these conditions.