Anti-ERO1L antibody [EPR12474]

Supplementary info

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

Activity summary

ERO1L also known as ERO1-alpha is a protein involved in the formation of disulfide bonds in the endoplasmic reticulum important for protein folding. The molecular mass of ERO1L is approximately 54 kDa. ERO1L primarily expresses in tissues with high secretory activities such as the liver and pancreas. It plays a vital role in maintaining redox homeostasis within the cell by transferring electrons from protein disulfide isomerase to molecular oxygen.

Biological function summary

ERO1L contributes to oxidative protein folding within the endoplasmic reticulum. As part of a complex it interacts with protein disulfide isomerases to facilitate the introduction of disulfide bonds into nascent proteins. This function is essential for the proper maturation of secreted proteins influencing cellular protein management processes. ERO1L activity impacts cellular responses to stress and influences the capacity of cells to handle unfolded proteins.

Pathways

ERO1L significantly influences the protein folding and endoplasmic reticulum-associated degradation pathway. It has strong associations with protein disulfide isomerase and interacts within the unfolded protein response to manage cellular stress caused by misfolded proteins. The protein contributes to the maintenance of a stable internal environment during conditions where protein folding demands increase.

Associated diseases and disorders

ERO1L shows connections to cancer and neurodegenerative disorders. Aberrant expression of ERO1L can influence tumor growth due to its role in modulating cellular stress responses and managing protein folding in cancer cells. The protein also shows a relationship with neurodegenerative conditions through its involvement in protein misfolding pathways which are critical in diseases like Alzheimer's. ERO1L collaborates with proteins like protein disulfide isomerase and participates in cellular mechanisms underlying these conditions.