Calnexin antibody (CANX) (C-Term)

Details for Product anti-CANX Antibody No. ABIN361783, Supplier: Log in to see
Antigen
  • CNX
  • IP90
  • P90
  • 1110069N15Rik
  • AI988026
  • Cnx
  • D11Ertd153e
  • canx
  • clgn
  • clnx
  • cnx
  • PP90
  • zgc:63524
  • wu:fe06b12
  • CANX
  • calnexin
  • CalNeXin
  • calnexin L homeolog
  • CANX
  • Canx
  • cnx-1
  • canx.L
  • canx
  • LOC100283947
Alternatives
anti-Mammalian Calnexin antibody for Immunoprecipitation
Epitope
C-Term
137
62
20
14
13
13
12
7
5
5
5
4
4
4
3
3
3
3
2
2
2
2
1
1
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
473
300
287
184
177
171
169
165
165
159
159
158
104
95
58
54
54
16
13
7
6
6
4
4
3
2
2
1
1
1
1
1
Host
Rabbit
311
152
31
Clonality
Polyclonal
Conjugate
This Calnexin antibody is un-conjugated
20
18
17
14
13
12
9
8
8
7
7
7
7
7
7
7
7
7
7
7
7
7
7
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6
5
5
5
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Application
Immunocytochemistry (ICC), Flow Cytometry (FACS), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
452
339
237
190
161
159
129
88
67
21
14
9
9
8
3
2
1
1
1
1
Options
Supplier
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Supplier Product No.
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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
Plasmids, Primers & others Plasmids, Primers & others Calnexin products on genomics-online (e.g. as negative or positive controls)
Antigen
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).
Gene ID 403908
NCBI Accession NP_001003232
UniProt P24643
Pathways MAPK Signaling, Thyroid Hormone Synthesis
Application Notes
  • WB (1:2000)
  • ICC/IF (1:100)
  • IHC (1:100)
  • optimal dilutions for assays should be determined by the user.
Comment

A 1:2000 dilution of SPC-182 was sufficient for detection of Calnexin in 10 μg of HeLa cell lysate by ECL immunoblot analysis.

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 (CANX) (C-Term) antibody (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).

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