| Overview |
| bsm-70372m |
| Calnexin (N-terminal region) Antibody |
| WB |
| 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. This sequence has high homology to similar regions in rat and mouse Calnexin. |
| Human, Mouse, Rat |
| Specifications |
| Unconjugated |
| Mouse |
| Clone M437 was generated from a recombinant protein corresponding to amino acid residues in the N-terminal region of human calnexin. |
| Monoclonal |
| #REF! |
| IgG1 |
| Purified by Protein A. |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20C. |
| Target |
| P27824 |
| IP90, P90 |
| 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. |
| Application Dilution |
| WB |
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