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Key Documents

SAB5200097

Sigma-Aldrich

Anti-CANX antibody produced in rabbit

affinity isolated antibody

Synonyme(s) :

Anti-CANX, Anti-CNX, Anti-Calnexin-CT (Purified), Anti-IP90, Anti-P90

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous glycerol solution

Poids mol.

antigen predicted mol wt 90 kDa

Espèces réactives

bovine, Drosophila (weak), monkey, chicken, guinea pig, human, hamster, Xenopus (weak), dog, quail, rat, mouse, sheep, pig, rabbit

Technique(s)

flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

Catégories apparentées

Description générale

Calnexin (CANX) is a 67kDa transmembrane protein expressed in the endoplasmic reticulum. It is part of the lectin chaperone group. The gene ID of the protein is 821.

Spécificité

Detects ~90 kDa.

Immunogène

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

Actions biochimiques/physiologiques

Calnexin (CANX) takes care of protein folding. It binds to the target proteins which have only one glucose residue and aids in their folding. When the protein is released from CANX it is then trafficked to the Golgi apparatus for further modifications.

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Forme physique

PBS, pH 7..2, 50% glycerol, and 0.09% sodium azide

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Tetyana Drozdova et al.
Physiological reports, 1(4), e00086-e00086 (2013-12-05)
Nephrin, an important component of the podocyte filtration slit diaphragm, plays a key role in the maintenance of glomerular permselectivity. Mutations in nephrin lead to proteinuria and congenital nephrotic syndrome. Nephrin undergoes posttranslational modifications in the endoplasmic reticulum (ER) prior
Dorthe T Olsen et al.
Protein expression and purification, 92(1), 105-111 (2013-09-24)
Calreticulin (Crt) and calnexin (Cnx) are homologous endoplasmic reticulum (ER) chaperones involved in protein folding and quality control. Crt is a soluble ER luminal Mr 46 kDa protein and Cnx is a Mr 67kDa ER membrane protein. During purification of
Praseetha Kizhakkedath et al.
Biochimica et biophysica acta, 1843(12), 2871-2877 (2014-09-01)
Dysequilibrium syndrome (DES, OMIM 224050) is a genetically heterogeneous condition that combines autosomal recessive non-progressive cerebellar ataxia with mental retardation. The subclass dysequilibrium syndrome type 1 (CAMRQ1) has been attributed to mutations in the VLDLR gene encoding the very low
Yaeli Lebel-Haziv et al.
Neoplasia (New York, N.Y.), 16(9), 723-740 (2014-09-24)
The chemokine CCL2 (MCP-1) has been identified as a prominent tumor-promoting factor in breast cancer. The major source for CCL2 is in the tumor cells; thus, identifying the mechanisms regulating CCL2 release by these cells may enable the future design
C Norez et al.
British journal of pharmacology, 171(21), 4831-4849 (2014-07-30)
The most common mutation in cystic fibrosis (CF), F508del, causes defects in trafficking, channel gating and endocytosis of the CF transmembrane conductance regulator (CFTR) protein. Because CF is an orphan disease, therapeutic strategies aimed at improving mutant CFTR functions are

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