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- Peptide (C)KAEEDEILNRSPRNRK, corresponding to amino acid residues 572-587 of rat Canx (Accession P35565). Intracellular, C-terminus.
- Immuno-colocalization of Calnexin and Presenilin-1 in mouse cortexImmunohistochemical staining of perfusion-fixed frozen mouse parietal cortex sections using Anti-Presenilin-1-ATTO-488 Antibody (#AIP-011-AG), (1:60) and Anti-Calnexin-ATTO-594 Antibody (#ACS-009-AR), (1:60). A. Calnexin staining (red) appears in neuronal profiles. B. Presenilin-1 staining (green) in the same section appears in neuronal profiles and apical dendrites (arrows). C. Merger of A and B demonstrates colocalization in several neurons (arrows). Cell nuclei are stained using DAPI (blue) as the counterstain. Images were acquired with 25x objective.Immuno-colocalization of Calnexin and Presenilin-1 in mouse hippocampusImmunohistochemical staining of perfusion-fixed frozen mouse hippocampal sections using Anti-Presenilin-1-ATTO-488 Antibody (#AIP-011-AG), (1:60) and Anti-Calnexin-ATTO-594 Antibody (#ACS-009-AR), (1:60). A. Calnexin staining (red) appears in neuronal profiles. B. Presenilin-1 staining (green) in the same section appears in neuronal profiles and apical dendrites (arrows). C. Merger of A and B demonstrates colocalization in several neurons (arrows). Cell nuclei are stained using DAPI (blue) as the counterstain. Images were acquired with 25x objective.
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 KV1.2 was found to produce a substantial dose-dependent increase in cell surface KV1.2 channels in transfected mammalian COS-1 cells. In contrast, Calnexin coexpression showed no effect on trafficking of intracellularly retained KV1.1 or KV1.6 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.
Species reactivity key:
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.
Anti-Calnexin-ATTO-594 Antibody (#ACS-009-AR) is directly labeled with an ATTO-594 fluorescent dye. ATTO dyes are characterized by strong absorption (high extinction coefficient), high fluorescence quantum yield, and high photo-stability. The ATTO-594 fluorescent label belongs to the class of Rhodamine dyes and can be used with fluorescent equipment typically optimized to detect Texas Red and Alexa-594. Anti-Calnexin-ATTO-594 Antibody is specially suited to experiments requiring simultaneous labeling of different markers.