Calnexin (N-terminal region) (clone M437), anti-human, mouse, rat

Background:
Calnexin is a 90 kDa integral membrane protein located primarily in the endoplasmic reticulum (ER). The structure of calnexin includes a long N-terminal calcium-binding domain that extends into the lumen of the ER and a short, acidic cytosolic domain. Calnexin associates with several cell surface proteins as they pass through the ER, and may be involved in the Ca2+-dependent retention of proteins in the ER. The amino acid sequence of calnexin is highly conserved among various species and is similar in sequence to calreticulin, another Ca2+-binding protein found in the ER. Phosphorylation may regulate the activity of the C-terminal region of Calnexin. Both proline-dependent kinase and casein kinase sites have been identified, and the phosphorylation of these sites may regulate calnexin functions involved with detection of ER protein quality control and transport.

Immunogen: Clone M437 was generated from a recombinant protein corresponding to amino acid residues in the N-terminal region of human calnexin. This sequence has high homology to similar regions in rat and mouse Calnexin.

Specificity: This antibody detects a 90 kDa* protein corresponding to the apparent molecular mass of Calnexin on SDS-PAGE immunoblots of human HeLa and rat A7r5 cells. In immunocytochemistry, anti-Calnexin specifically stains endoplasmic reticulum and related vesicular structures in paraformaldehyde fixed and NP-40 permeabilized cells.

Buffer/Storage:
Mouse monoclonal purified with protein A chromatography is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.