Overview
- Peptide (C)KAEEDEILNRSPRNRK, corresponding to amino acid residues 572-587 of rat Canx (Accession P35565). Intracellular, C-terminus.
Western blot analysis of rat heart membrane (lanes 1 and 5), mouse heart membrane (lanes 2 and 6), human breast adenocarcinoma (MCF7) lysate (lanes 3 and 7) and human ovary adenocarcinoma (OVCAR-3) cell line lysate (lanes 4 and 8):1-4. Anti-Calnexin Antibody (#ACS-009), (1:400).
5-8. Anti-Calnexin Antibody, preincubated with Calnexin Blocking Peptide (#BLP-CS009).
Expression of Calnexin in BV-2 cells (lane 1) and in BV-2-derived exosomes (lane 2).Western blot was done using Anti-Calnexin Antibody (#ACS-009), (1:400).
Note: Calnexin is a negative control marker of exosomes. It is used to assess the purity of exosome isolation.
Western blot analysis of human U-87 MG glioblastoma cell line lysate (lane 1) and U-87 MG-derived purified exosomes (lane 2)50µg of cells and purified exosomes lysates were analyzed using Anti-Calnexin Antibody (#ACS-009), (1:600).
Note: Calnexin is a negative control marker of exosomes. It is used to assess the purity of exosome isolation.
Expression of Calnexin in mouse hippocampusImmunohistochemical staining of mouse hippocampal CA1 region using Anti-Calnexin Antibody (#ACS-009), (1:200). A. Canx staining (green) appears in neurons (horizontal arrow) and astrocytes (vertical arrow). B. GFAP staining of astrocytic fibers (red). C. Merge of panels A and B demonstrates co-localization in some astrocytes. DAPI is used to stain nuclei (blue).
- Ho, S.C. et al. (1999) Mol. Immunol. 36, 1.
- Nagaya, N. et al. (1999) Receptors Channels. 6, 229.
- Manganas, L.N. and Trimmer, J.S. (2004) Biochem. Biophys. Res. Commun. 322, 577.
- Pind, S. et al. (1994) J. Biol. Chem. 269, 12784.
Calnexin is a type I transmembrane endoplasmic reticulum chaperone protein involved in the folding and assembly of numerous proteins. Calnexin is comprised of 537 amino acids with a large luminal domain consisting of 462 amino acids. Calnexin does not possess N-linked glycosylation sites and is localized to the endoplasmic reticulum by a –RKPRRE motif at its carboxyl terminus. Calnexin is one of the few ER membrane proteins that can be phosphorylated in a GTP-dependent manner1.
Calnexin interacts with a number of ER membrane channels. It interacts transiently with wild-type Shaker K+ channel in the ER but fails to associate with an unglycosylated Shaker mutant that makes active, cell surface channels. This suggest that glycosylation of Shaker protein is required for interaction with calnexin but calnexin is not required for the proper assembly and folding of Shaker channels2.
Coexpression of calnexin with the voltage-gated potassium channel KV1.2α was found to produce a substantial dose-dependent increase in cell surface KV1.2α channels in transfected mammalian COS-1 cells. In contrast, calnexin coexpression showed no effect on trafficking of intracellularly retained KV1.1 or KV1.6α subunits3.
Calnexin has been implicated in the pathophysiology of cystic fibrosis disease (CF). Wild type and ΔF508 mutant cystic-fibrosis conductance regulator (CFTR) associate with calnexin in a Chinese hamster ovary (CHO) cell model. Although both wild-type and ΔF508 CFTRs are present in complexes with calnexin, only wild-type CFTR is able to escape this association and exit the ER. This suggests that calnexin retains misfolded proteins in the ER and contributes to the mislocalization of mutant CFTRs.
Anti-Calnexin Antibody (#ACS-009) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot and immunohistochemistry applications. It has been designed to recognize Canx from human, mouse, and rat samples.
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