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Goat Anti-Calnexin Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, IF, Pep-ELISA |
|---|---|
| Primary Accession | P27824 |
| Other Accession | NP_001737, 821, 12330 (mouse), 29144 (rat) |
| Reactivity | Human, Mouse |
| Predicted | Rat, Pig, Dog |
| Host | Goat |
| Clonality | Polyclonal |
| Concentration | 100ug/200ul |
| Isotype | IgG |
| Calculated MW | 67568 Da |
| Gene ID | 821 |
|---|---|
| Other Names | Calnexin, IP90, Major histocompatibility complex class I antigen-binding protein p88, p90, CANX |
| Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
| 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 | Goat Anti-Calnexin Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | CANX |
|---|---|
| Function | Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse. |
| Cellular Location | Endoplasmic reticulum membrane; Single-pass type I membrane protein. Mitochondrion membrane {ECO:0000250|UniProtKB:P24643}; Single-pass type I membrane protein. Melanosome membrane; Single-pass type I membrane protein. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545, PubMed:17081065). The palmitoylated form preferentially localizes to the perinuclear rough ER (PubMed:22314232) Localizes to endoplasmic reticulum mitochondria-associated membrane (MAMs) that connect the endoplasmic reticulum and the mitochondria (By similarity). {ECO:0000250|UniProtKB:P24643, ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:22314232} |
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
This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. It may also play a central role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Alternatively spliced transcript variants encoding the same protein have been described.
References
Human delta opioid receptor biogenesis is regulated via interactions with SERCA2b and calnexin. Tuusa JT, et al. FEBS J, 2010 Jul. PMID 20528919.
Mapping of domains on HIV envelope protein mediating association with calnexin and protein-disulfide isomerase. Papandr茅ou MJ, et al. J Biol Chem, 2010 Apr 30. PMID 20202930.
Calnexin phosphorylation attenuates the release of partially misfolded alpha1-antitrypsin to the secretory pathway. Cameron PH, et al. J Biol Chem, 2009 Dec 11. PMID 19815548.
Calnexin improves the folding efficiency of mutant rhodopsin in the presence of pharmacological chaperone 11-cis-retinal. Noorwez SM, et al. J Biol Chem, 2009 Nov 27. PMID 19801547.
Altered expression of glycoproteins on the cell surface of Jurkat cells during etoposide-induced apoptosis: shedding and intracellular translocation of glycoproteins. Sato H, et al. Biochim Biophys Acta, 2009 Oct. PMID 19524015.
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