Anti-Calnexin antibody

This supplementary information is collated from multiple sources and compiled automatically. Calnexin also known as Canx is a type I integral membrane protein of the endoplasmic reticulum (ER) involved in the process of protein folding. This chaperone protein has an approximate molecular weight of 90 kDa and is known for its role in the quality control of glycoproteins. Calnexin is expressed in the ER of cells where it interacts with nascent polypeptides to ensure proper folding and assembly contributing to cellular homeostasis. It exhibits its function through its lectin-like domain that binds to sugar moieties on glycoproteins. Biological function summary Calnexin facilitates the proper folding of newly synthesized proteins by forming a complex with another chaperone protein called ERp57. This interaction helps in creating the correct disulfide bonds in glycoproteins which is essential for their stability and functionality. The complex often referred to as the calnexin cycle is critical in preventing the aggregation and misfolding of proteins within the ER. This process ensures that only correctly folded proteins proceed to the Golgi apparatus for further processing and transport.