Calnexin (CANX) antibody

Antigen: Calnexin (CANX)

Synonyms: CNX, P90, IP90, FLJ26570, Cnx, AI988026, D11Ertd153e, 1110069N15Rik, DmelCG11958, CG11958, canx, MGC52927, CANX, PP90, zgc:63524, wu:fe06b12, MGC166317, MGC69400, fj49d10, MGC153946, wu:fj24b04, wu:fj49d10, zgc:153946, DKFZp459P042, LOC100283947

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human, Monkey, Mouse (Murine), Rat (Rattus), Cow (Bovine), Dog (Canine), Guinea Pig, Hamster, Pig (Porcine), Quail, Rabbit, Sheep (Ovine)

Application: Western Blotting (WB)

Catalog no.: ABIN361826

Additional Information

Alternative name: Calnexin

Immunogen: Dog calnexin C-terminal synthetic peptide conjugated to KLH. Identical to human, mouse and rat calnexin sequences over these residues.

Format: Antiserum

Description: 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 mulitsubunit 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 monoglycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatability complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7).

Specificity: Detects ~90kDa. Species cross-reactivity: Human, Monkey, Mouse, Rat, Bovine, Chicken (weak), Dog, guinea Pig, Hamster, Pig, Quail, Rabbit, Sheep, Drosophila (weak), Xenopus (weak).

Synonyms: CNX, P90, IP90, FLJ26570, Cnx, AI988026, D11Ertd153e, 1110069N15Rik, DmelCG11958, CG11958, canx, MGC52927, CANX, PP90, zgc:63524, wu:fe06b12, MGC166317, MGC69400, fj49d10, MGC153946, wu:fj24b04, wu:fj49d10, zgc:153946, DKFZp459P042, LOC100283947

Application Details

Application Notes: Recommended dilution for WB 1:2000

Buffer: Antiserum

Storage: -20°C, 1 year+, shipped on cold packs or ambient

Restrictions: For Research Use only

Images

Calnexin CT, rat tissue mix

CalnexinCT, mouse colitis, Amplifier

SPC108 Anti Calnexin CT, mouse backskin.jpg

Publications

Publications: 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).

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).

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).

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).

Elagoez, 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).

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).

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).