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) transmembrane segment and an acidic cytosolic domain (96 amino acids).
Calnexin, is a calcium binding type I integral membrane protein present mainly in the endoplasmic reticulum. It plays a pivotal role in quality control processes during protein synthesis and folding. Anti-calnexin antibody (diluted 1: 300) can be used in dual immunofluorescence staining to visualize TG2 transport.
Rabbit anti-calnexin antibody reacts specifically with calnexin (90 kDa) of dog, mouse, rat and human.
Synthetic peptide corresponding to the c-terminus of human calnexin (amino acids 573-592) conjugated to KLH.
Anti-Calnexin antibody produced in rabbit has been used in:
- western blot analysis
- dual immunofluorescence staining
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. Calnexin has been shown to be associated with several cell surface proteins, including major histocompatibility complex (MHC) class I heavy chain, T-cell receptor (TCR), and B cell membrane immunoglobulin during translocation through the endoplasmic reticulum (ER). It also forms complexes with other resident ER proteins involved in Ca2+ -dependent retention of proteins.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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