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Key Documents

SAB5200097

Sigma-Aldrich

Anti-CANX antibody produced in rabbit

affinity isolated antibody

Sinonimo/i:

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

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous glycerol solution

PM

antigen predicted mol wt 90 kDa

Reattività contro le specie

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

tecniche

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

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

Descrizione generale

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.

Specificità

Detects ~90 kDa.

Immunogeno

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

Azioni biochim/fisiol

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.

Caratteristiche e vantaggi

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.

Stato fisico

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

Esclusione di responsabilità

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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Raccomandato

N° Catalogo
Descrizione
Determinazione del prezzo

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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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