Anti-Calnexin-ATTO Fluor-594

Antibodies

ATTO-594. Maximum absorption 601 nm; Maximum fluorescence 627 nm. The fluorescence is excited most efficiently in the 580 - 615 nm range. This label belongs to the class of Rhodamine dyes and can be used with fluorescent equipment typically optimized to detect Texas Red and Alexa-594.

Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C

Lyophilized powder

Canx, Calx, CNX, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90 - A Rabbit Polyclonal Antibody to Calnexin Conjugated to the Fluorescent Dye ATTO-594

Mouse, human - identical

Confirmed by amino acid analysis and mass spectrometry

1 mg/ml

Intracellular, C-terminus

Rat

41116161

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.