ab10287-100ul，Anti-ERp57 antib

This supplementary information is collated from multiple sources and compiled automatically. ERp57 also known as 4f9 is a protein responsible for catalyzing disulfide bond formations and isomerizations in the endoplasmic reticulum. ERp57 has a molecular mass of approximately 57 kDa and belongs to the protein disulfide isomerase (PDI) family. Its main expression occurs in the endoplasmic reticulum of cells where it plays a role in ensuring proper protein folding and quality control. Biological function summary ERp57 interacts with calnexin and calreticulin to form a complex involved in glycoprotein folding. This complex assists in the proper assembly and maturation of nascent glycoproteins by ensuring correct folding pathways within the cell. ERp57 has a specialized role in managing oxidative protein folding which makes it essential for cell function and homeostasis. Pathways ERp57 participates in the calnexin/calreticulin cycle which is critical for protein triage in the endoplasmic reticulum. This cycle ensures that only properly folded proteins progress to their final destinations. ERp57 also interacts with ERp72 another member of the PDI family to facilitate thiol-disulfide exchange reactions. These interactions position ERp57 as a central player in the maintenance of cellular redox balance and protein homeostasis. Alterations in ERp57 function can relate to neurodegenerative diseases such as Alzheimer's and certain types of cancer. Misfolded proteins often accumulate in these conditions highlighting ERp57's role in preventing cellular stress. Moreover ERp57 associates with the protein tau in Alzheimer's disease where it assists in tau’s proper folding and diminishes its aggregation tendency. Additionally disruptions in the ERp57 pathway may interact with cancer-related proteins like p53 modulating apoptosis and cell cycle regulation.