Calnexin Protein, Mouse (HEK293, His)

Calnexin protein, a calcium-binding chaperone located in the endoplasmic reticulum (ER), plays a pivotal role in interacting with newly synthesized monoglucosylated glycoproteins, contributing to protein assembly and retention of unassembled protein subunits within the ER. With a key function in the ER's quality control apparatus, calnexin participates in the retention of incorrectly folded proteins. Notably, it associates with partial T-cell antigen receptor complexes in immature thymocytes, suggesting a role in signaling and regulation of thymocyte maturation. Additionally, calnexin may be involved in receptor-mediated endocytosis at the synapse. Its interactions extend to various proteins, including MAPK3/ERK1, KCNH2, SERPINA2P/SERPINA2, SGIP1, PPIB, SMIM22, TMX2, TMEM35A/NACHO, CHRNA7, RETREG2, RETREG3, DNM1L, and ADAM7, highlighting its versatility in forming complexes and participating in diverse cellular processes. The palmitoylated form specifically interacts with the ribosome-translocon complex component SSR1, promoting efficient folding of glycoproteins and emphasizing its role in protein maturation within the ER.