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Human, Mouse (Murine), Rat (Rattus), Cow (Bovine), Chicken, Dog (Canine), Guinea Pig, Hamster, Pig (Porcine), Monkey, Rabbit, Sheep (Ovine), Xenopus laevis
Western Blotting (WB), Immunoprecipitation (IP), Immunocytochemistry (ICC)
|9 references available|
|Price||202.40 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 3 to 4 Business Days|
|Immunogen||A 19 residue synthetic peptide based on canine calnexin and the peptide coupled to KLH.|
Calnexin, an abundant ~90kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90. It consists of a large 50kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail. Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention, calnexin has positively charged cytosolic residues that do the same thing. 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 monoglycosylated glycans. 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.
Synonyms: CANX, CNX, IP90, P90
|Characteristics||Accession Number: NP_001003232.1|
|Application Notes||1:5000-10000 (ECL) (WB), 1:100 (IP)|
|Storage||Store at -20° C. Shipping Temperature: Blue Ice or 4° C|
|Storage Shipping Temp Max||Blue Ice or 4 °C|
|Research Area||Cell Signaling, Organelles|
|Restrictions||For Research Use only|
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).
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).
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).
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).
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).