Calnexin-CT (C-Term) antibody

Details for Product No. ABIN361782
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Antigen
Epitope
C-Term
(3)
Reactivity
Human, Monkey, Mouse (Murine), Rat (Rattus), Cow (Bovine), Chicken, Dog (Canine), Guinea Pig, Hamster, Pig (Porcine), Quail, Rabbit, Sheep (Ovine), Fruit Fly (Drosophila melanogaster), Xenopus laevis
(3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3)
Host
Rabbit
(3)
Clonality
Polyclonal
Application
Western Blotting (WB), Immunoprecipitation (IP), Immunocytochemistry (ICC), Immunohistochemistry (IHC), Flow Cytometry (FACS)
(3), (2), (1), (1), (1), (1)
Pubmed 7 references available
Catalog no. ABIN361782
Quantity 50 µg
Price
212.30 $   Plus shipping costs $45.00
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Immunogen Dog Calnexin C-terminal synthetic peptide conjugated to KLH. Identical to human mouse and rat calnexin sequences over these AA .
Specificity Detects approx. 90 kDa.
Purification Protein A Purified
Background Synonyms:
CANX, CNX, IP90, P90
Calnexin, an abundant approx. 90 kDa integral protein of the endoplasmic reticulum, is also referred to as IP90, p88 and p90. It consists of a large 50 kDa 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 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. 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.
Gene ID 403908
NCBI Accession NP_001003232.1
UniProt P24643
Application Notes Recommended Dilution: 1:2000 (WB)
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
Storage -20 °C
Supplier Images
anti-Calnexin-CT (C-Term) antibody Calnexin CT, rat tissue mix.
Background 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).

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).

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).

Hosts (3)
Reactivities (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3)
Applications (3), (2), (1), (1), (1), (1)
Epitopes (3)
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