Anti-Calnexin antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hybridoma TO-5 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice. Calnexin contains a long (461 amino acids) N-terminal Ca2+
-binding domain extending into the lumen of the endoplasmic reticulum (ER), a short (22 amino acids) trans-membrane segment and an acidic cytosolic domain (96 amino acids).
Calnexin (p88, IP90) is a calcium-binding, type I integral membrane protein, localized primarily in the endoplasmic reticulum (ER). Calnexin binds newly synthesized glycoproteins and misfolded proteins and is believed to play a critical role in quality control processes during protein synthesis and folding. Calnexin acts as a lectin like chaperone that binds oligosaccharide residues of newly synthesized N-linked glycoproteins. The lectin specificity of calnexin and its soluble homologue calreticulin has been identified as high mannose oligosaccharides terminating in monoglucosyl residues linked through α1-3. Calnexin has been shown to be associated with several cell surface proteins, including MHC class I heavy chain, T-cell receptor (TCR), and B cell membrane immunoglobulin during translocation through the ER. It also forms complexes with other resident ER proteins involved in Ca2+-dependent retention of proteins.