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Anti-Calnexin (N-terminal region) Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | P27824 |
| Reactivity | Bovine |
| Host | Mouse |
| Clonality | Mouse Monoclonal |
| Isotype | IgG1 |
| Clone Names | M437 |
| Calculated MW | 67568 Da |
| Gene ID | 821 |
|---|---|
| Other Names | IP90, P90 |
| Target/Specificity | 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. |
| Format | Protein A Purified |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Anti-Calnexin (N-terminal region) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
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.
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