Calnexin-CT Antibody: APC

Calnexin is a ~90 kDa integral membrane protein of the endoplasmic reticulum (ER), also known as IP90, p88, or p90. Structurally, it comprises a large N-terminal calcium-binding luminal domain (~50 kDa), a single transmembrane helix, and a short, acidic cytoplasmic tail (CT) . Unlike many ER-resident proteins that rely on a C-terminal KDEL motif for retention, Calnexin is retained in the ER via positively charged residues in its cytosolic tail. Functionally, Calnexin is a central component of the ER quality control system. It acts as a molecular chaperone, facilitating the proper folding and assembly of nascent glycoproteins. In concert with calreticulin, Calnexin binds to monoglucosylated N-linked glycans on folding intermediates, ensuring fidelity in glycoprotein maturation. It also interacts with key immune molecules, including MHC class I heavy chains, T cell receptor subunits, and B cell immunoglobulins. In neuroscience, Calnexin-CT is gaining attention for its role in neurodegenerative disease. ER stress and impaired protein folding are hallmarks of disorders such as Alzheimer’s, Parkinson’s, and ALS. Dysregulation of Calnexin function can exacerbate proteostasis imbalance, leading to accumulation of misfolded proteins and neuronal dysfunction. Given its dual role in protein folding and ER homeostasis, Calnexin—particularly its cytoplasmic tail—represents a promising target for therapeutic strategies aimed at restoring proteostasis in neurodegenerative diseases.

Calnexin, CALX_HUMAN, CANX, CNX, FLJ26570, IP90, p88, p90, Histocompatibility complex class I antigen binding protein p88, Major histocompatibility complex class I antigen-binding protein p88

1. Rajagopalan S., Xu Y., and Brenner M.B. (1994) Science. 263 (5145) : 387-90. 2. Tjoelker L.W., et al. (1994) Biochemistry. 33: 3229. 3. Schrag J. et al. (2001) Molecular Cell. 8 (3) : 633-644. 4. Janiszewski M. (2005) J. Biol Chem. 280 (49) : 40813-40819. 5. Elagoz A., Callejo M., Armstrong J., and Rokeach L. A. (1999) J. Cell Sci. 112: 4449-4460. 6. Otteken A. and Moss B. (1996) J Bio Chem. 271 (1) : 97-103. 7. Galvin K. et al. (1992) Proc Natl Acad Sci USA. 89 (18) : 8452-6.

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