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Calnexin antibody (CANX) (C-Term)

Details for Product anti-CANX Antibody No. ABIN361827, Supplier: Login to see New
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Synonyms zgc:63524, wu:fe06b12, clgn, clnx, cnx, CANX, CNX, IP90, P90, canx, 1110069N15Rik, AI988026, Cnx, D11Ertd153e, PP90, CG11958, Dmel\CG11958
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(84), (25), (10), (8), (6), (4), (4), (4), (3), (3), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Chicken, Cow (Bovine), Dog (Canine), Fruit Fly (Drosophila melanogaster), Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Pig (Porcine), Quail, Rabbit, Rat (Rattus), Sheep (Ovine), Xenopus laevis
(230), (127), (120), (91), (72), (67), (66), (65), (64), (63), (62), (62), (59), (36), (36), (5), (4), (4), (4), (4), (4), (4), (2), (1), (1), (1), (1)
(197), (29), (25)
This Calnexin antibody is un-conjugated
(7), (7), (5), (5), (5), (5), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blotting (WB)
(228), (137), (111), (96), (83), (73), (47), (44), (11), (9), (5), (5), (2), (1), (1)
Pubmed 11 references available
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Quantity 200 μL
Shipping to United States ( )
Availability Will be delivered in 3 to 4 Business Days
Immunogen Dog calnexin C-terminal synthetic peptide conjugated to KLH. Identical to human, mouse and rat calnexin sequences over these residues.
Specificity Detects the C-terminal domain of Calnexin ~90 kDa. Weak detection in Chicken, Drosophila, and Xenopus tissues
Purification Rabbit Antiserum
Alternative Name Calnexin (CANX Antibody Abstract)
Background Calnexin, an abundant ~90 kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90 (1). It consists of a large 50 kDa 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 multi-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).
Cellular Localization: Endoplasmic Reticulum | Endoplasmic Reticulum Lumen | Melanosome | Cytoplasm
Gene ID 403908
NCBI Accession NP_001003232
UniProt P24643
Pathways MAPK Signaling
Application Notes Recommended Dilution: WB (1:2000), IHC (1:100), ICC/IF (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Buffer Rabbit Antiserum
Storage -20 °C
Supplier Images
Image no. 1 for anti-Calnexin antibody (CANX) (C-Term) (ABIN361827) Calnexin CT, rat tissue mix
Image no. 2 for anti-Calnexin antibody (CANX) (C-Term) (ABIN361827) CalnexinCT, mouse colitis, Amplifier
Image no. 3 for anti-Calnexin antibody (CANX) (C-Term) (ABIN361827) SPC108 Anti Calnexin CT, mouse backskin.jpg
Product cited in: Gordo-Gilart, Hierro, Andueza et al.: "Heterozygous ABCB4 mutations in children with cholestatic liver disease." in: Liver international : official journal of the International Association for the Study of the Liver, 2015 (PubMed).

Martín-Acebes, Merino-Ramos, Blázquez et al.: "The composition of West Nile virus lipid envelope unveils a role of sphingolipid metabolism in flavivirus biogenesis." in: Journal of virology, Vol. 88, Issue 20, pp. 12041-54, 2014 (PubMed).

Williams, Tulke, Ilegems et al.: "Expression of nucleobindin 1 (NUCB1) in pancreatic islets and other endocrine tissues." in: Cell and tissue research, Vol. 358, Issue 2, pp. 331-42, 2014 (PubMed).

Gordo-Gilart, Andueza, Hierro et al.: "Functional analysis of ABCB4 mutations relates clinical outcomes of progressive familial intrahepatic cholestasis type 3 to the degree of MDR3 floppase activity." in: Gut, Vol. 64, Issue 1, pp. 147-55, 2014 (PubMed).

Background publications Janiszewski, Lopes, Carmo et al.: "Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells." in: The Journal of biological chemistry, Vol. 280, Issue 49, pp. 40813-9, 2005 (PubMed).

Schrag, Bergeron, Li et al.: "The Structure of calnexin, an ER chaperone involved in quality control of protein folding." in: Molecular cell, Vol. 8, Issue 3, pp. 633-44, 2001 (PubMed).

Elagöz, Callejo, Armstrong et al.: "Although calnexin is essential in S. pombe, its highly conserved central domain is dispensable for viability." in: Journal of cell science, Vol. 112 ( Pt 23), pp. 4449-60, 2000 (PubMed).

Otteken, Moss: "Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin." in: The Journal of biological chemistry, Vol. 271, Issue 1, pp. 97-103, 1996 (PubMed).

Rajagopalan, Xu, Brenner: "Retention of unassembled components of integral membrane proteins by calnexin." in: Science (New York, N.Y.), Vol. 263, Issue 5145, pp. 387-90, 1994 (PubMed).

Tjoelker, Seyfried, Eddy et al.: "Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5." in: Biochemistry, Vol. 33, Issue 11, pp. 3229-36, 1994 (PubMed).

Galvin, Krishna, Ponchel et al.: "The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 18, pp. 8452-6, 1992 (PubMed).

Catalog No. ABIN361827
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