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Calnexin antibody (CANX) (C-Term)

Details for Product anti-CANX Antibody No. ABIN361783, Supplier: Log in to see
Antigen
  • zgc:63524
  • wu:fe06b12
  • clgn
  • clnx
  • cnx
  • CANX
  • CNX
  • IP90
  • P90
  • canx
  • 1110069N15Rik
  • AI988026
  • Cnx
  • D11Ertd153e
  • PP90
  • CG11958
  • Dmel\CG11958
  • calnexin
  • Calnexin 99A
  • canx
  • CANX
  • CNX
  • LOC100283947
  • LOC100304606
  • canx-a
  • Canx
  • Cnx99A
Alternatives
anti-Human Calnexin antibody for Immunofluorescence
Epitope
C-Term
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47
20
14
13
11
5
4
4
3
3
3
2
2
2
2
1
1
1
1
1
1
1
1
1
Reactivity
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
344
186
178
100
93
87
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53
37
22
13
9
5
4
4
4
4
4
2
2
1
1
1
Host
Rabbit
228
110
26
Clonality
Polyclonal
Conjugate
This Calnexin antibody is un-conjugated
13
11
11
10
8
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7
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6
6
6
6
5
5
5
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4
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4
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4
4
2
1
1
1
1
1
1
1
Application
Immunocytochemistry (ICC), Flow Cytometry (FACS), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
326
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146
123
89
75
11
9
6
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3
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2
1
1
Options
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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 Protein A Purified
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 Membrane | Melanosome
Gene ID 403908
NCBI Accession NP_001003232
UniProt P24643
Pathways MAPK Signaling
Application Notes Recommended Dilution: WB (1:2000), ICC/IF (1:100), IHC (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-Calnexin antibody (CANX) (C-Term) (ABIN361783) Calnexin CT, rat tissue mix.
Background publications Janiszewski, Lopes, Carmo, Pedro, Brandes, Santos, Laurindo: "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, Borisova, Hahn, Thomas, Cygler: "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, Rokeach: "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, Byers, Shows, Calderon, Schreiber, Gray: "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, Frohlich, Cummings, Carlson, Wands, Isselbacher, Pillai, Ozturk: "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).