Calnexin is responsible for the assembly of histocompatibility molecules in murine class I. Calnexin, a calcium-binding protein embedded within the ER membrane, retains newly synthesized glycoproteins in the ER to ensure quality control and proper folding.
Calnexin's specificity for a particular subset of glycoproteins can be determined by the presence of a lectin, which binds an intermediate early oligosaccharide on the folding glycoprotein. You can know more about Calnexin antibody via www.bosterbio.com/anti-calnexin-antibody-a03372-boster.html.
Calnexin (also known as IP90 or p88), is an integral membrane protein that measures approximately 90 kDa in the endoplasmic reticulum. Many resident ER proteins serve as molecular chaperones, and help in the proper folding and assembly of polypeptides into multisubunit proteins.
Calnexin is associated with the major histocompatibility complicated (MHC) class 1 heavy chains, partial complexes, and the B cell membrane immunoglobulin but not with complete receptor complexes. Calnexin, a chaperone, is known to retain incompletely or incorrectly folded proteins in ER.
Lys-AspGlu-Leu (KDEL), or a closely related sequence is found at the carboxyterminus of soluble ER resident protein such as GRP78, GRP94, and protein disulfide Iomerase. Calnexin is an integral membrane ER resident protein that lacks the KDEL sequence, but has positively charged cytosolic residues that allow for ER retention.
Calnexin has a large ER luminal region (461 amino acid), a transmembrane segment (22.2 amino acids) and a cytoplasmic trail (89 amino acids).