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Calnexin-NT Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, ICC, IP |
|---|---|
| Primary Accession | P24643 |
| Other Accession | NP_001003232.1 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat, Rabbit, Hamster, Monkey, Pig, Chicken, Bovine, Dog, Guinea Pig, Sheep |
| Clonality | Polyclonal |
| Description | Rabbit Anti-Human Calnexin-NT Polyclonal |
| Target/Specificity | Detects the N-terminal domain of Calnexin ~90kDa. |
| Other Names | Calnexin antibody, CALX_HUMAN antibody, CANX antibody, CNX antibody, FLJ26570 antibody, Histocompatibility complex class I antigen binding protein p88 antibody, IP90 antibody, Major histocompatibility complex class I antigen-binding protein p88 antibody, P90 antibody |
| Immunogen | A 19 residue synthetic peptide based on dog calnexin and the peptide coupled to KLH |
| Purification | Rabbit Antiserum |
| Storage | -20ºC |
| Storage Buffer | Rabbit Antiserum |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | A 1:5000 dilution of SPC-127 was sufficient for detection of Calnexin in 20 µg of HeLa cell lysate by ECL immunoblot analysis. |
| Cellular Localization | Endoplasmic Reticulum | Endoplasmic Reticulum Membrane | Melanosome |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Calnexin, an abundant ~90kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90 (1). It consists of a large 50kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail (2, 3). Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention (4), calnexin has positively charged cytosolic residues that do the same thing (3). Most ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into mulit-subunit proteins. Calnexin together with calreticulin, plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their mono-glycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatibility complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7).
References
1. Rajagopalan S., Xu Y., and Brenner M.B. (1994) Science 263(5145): 387-90.
2. Tjoelker L.W., et al. (1994) Biochemistry 33:3229.
3. Schrag J. et al. (2001) Molecular Cell 8(3): 633-644.
4. Janiszewski M. (2005) J. Biol Chem. 280(49):40813-40819.
5. Elagoz A., Callejo M., Armstrong J., and Rokeach L. A. (1999) J. Cell Sci. 112: 4449-4460.
6. Otteken A. and Moss B. (1996) J Bio Chem. 271(1): 97-103.
7. Galvin K. et al. (1992) Proc Natl Acad Sci USA. 89(18): 8452-6.
8. Raggo C., et al. (2002) Mol Cell Biol. 22: 5639-5649.
9. Rubio M.E., and Wenthold R.J. (1999) J Neurochem. 73: 942-948.
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