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SAB5200097

Sigma-Aldrich

Anti-CANX antibody produced in rabbit

affinity isolated antibody

Synonym(s):

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

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

mol wt

antigen predicted mol wt 90 kDa

species reactivity

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

NCBI accession no.

NP_001003232.1

UniProt accession no.

P27824

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

dog ... CANX(403908)

General description

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.

Specificity

Detects ~90 kDa.

Immunogen

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

Biochem/physiol Actions

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.

Features and Benefits

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.

Physical form

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

Disclaimer

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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Pricing

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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