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|Application / Reactivity||Human||Cow (Bovine)||Chicken||Guinea Pig||Mouse (Murine)||Pig (Porcine)||Rabbit||Rat (Rattus)||Sheep (Ovine)||Xenopus laevis||Dog (Canine)||Hamster||Monkey|
|Western Blotting (WB)||200 Antibodies||72 Antibodies||66 Antibodies||63 Antibodies||113 Antibodies||67 Antibodies||65 Antibodies||108 Antibodies||63 Antibodies||60 Antibodies||90 Antibodies||64 Antibodies||68 Antibodies|
|Proximity Ligation Assay (PLA)||1 Antibodies|
|Immunoprecipitation (IP)||70 Antibodies||40 Antibodies||40 Antibodies||38 Antibodies||45 Antibodies||38 Antibodies|
|Antigen||Calnexin (CANX) Antibodies|
|Reactivity||Chicken, Cow (Bovine), Dog (Canine), Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Pig (Porcine), Rabbit, Rat (Rattus), Sheep (Ovine), Xenopus laevis Alternatives|
|Conjugate||This Calnexin antibody is un-conjugated Alternatives|
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
|10 references available|
|Supplier||Log in to see|
Product Details anti-Calnexin AntibodyTarget Details Calnexin Application Details Handling References for anti-Calnexin Antibody (ABIN361839) Images
|Specificity||Detects the N-terminal domain of Calnexin ~90 kDa.|
|Immunogen||A 19 residue synthetic peptide based on dog calnexin and the peptide coupled to KLH|
Target Details CalnexinProduct Details anti-Calnexin Antibody Application Details Handling References for anti-Calnexin Antibody (ABIN361839) Images back to top
|Alternative Name||Calnexin (CANX Antibody Abstract)|
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 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).
Cellular Localization: Endoplasmic Reticulum | Endoplasmic Reticulum Membrane | Melanosome
Application DetailsProduct Details anti-Calnexin Antibody Target Details Calnexin Handling References for anti-Calnexin Antibody (ABIN361839) Images back to top
|Application Notes||Recommended Dilution: WB (1:5000), IHC (1:100), ICC/IF (1:100), IP (1:100), optimal dilutions for assays should be determined by the user.|
|Restrictions||For Research Use only|
HandlingProduct Details anti-Calnexin Antibody Target Details Calnexin Application Details References for anti-Calnexin Antibody (ABIN361839) Images back to top
References for anti-Calnexin Antibody (ABIN361839)Product Details anti-Calnexin Antibody Target Details Calnexin Application Details Handling Images back to top
|Product cited in:||
Liu, Milner, Boppart et al.: "β1D chain increases α7β1 integrin and laminin and protects against sarcolemmal damage in mdx mice." in: Human molecular genetics, Vol. 21, Issue 7, pp. 1592-603, 2012 (PubMed).
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).
Raggo, Rapin, Stirling et al.: "Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis." in: Molecular and cellular biology, Vol. 22, Issue 16, pp. 5639-49, 2002 (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).
Rubio, Wenthold: "Calnexin and the immunoglobulin binding protein (BiP) coimmunoprecipitate with AMPA receptors." in: Journal of neurochemistry, Vol. 73, Issue 3, pp. 942-8, 1999 (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).
ImagesProduct Details anti-Calnexin Antibody Target Details Calnexin Application Details Handling References for anti-Calnexin Antibody (ABIN361839) back to top