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C7617

Sigma-Aldrich

Anti-Calnexin antibody, Mouse monoclonal

enhanced validation

clone TO-5, purified from hybridoma cell culture

Synonyme(s) :

Anti-CANX, Anti-CNX

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.44

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

TO-5, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~90 kDa

Espèces réactives

human

Validation améliorée

independent
Learn more about Antibody Enhanced Validation

Concentration

~2 mg/mL

Technique(s)

flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: 0.5-1.0 μg/mL using total cell extract of HeLa cells.

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... CANX(821)

Description générale

Anti-Calnexin antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hybridoma TO-5 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice. Calnexin contains a long (461 amino acids) N-terminal Ca2+-binding domain extending into the lumen of the endoplasmic reticulum (ER), a short (22 amino acids) trans-membrane segment and an acidic cytosolic domain (96 amino acids).
Calnexin (p88, IP90) is a calcium-binding, type I integral membrane protein, localized primarily in the endoplasmic reticulum (ER). Calnexin binds newly synthesized glycoproteins and misfolded proteins and is believed to play a critical role in quality control processes during protein synthesis and folding. Calnexin acts as a lectin like chaperone that binds oligosaccharide residues of newly synthesized N-linked glycoproteins. The lectin specificity of calnexin and its soluble homologue calreticulin has been identified as high mannose oligosaccharides terminating in monoglucosyl residues linked through α1-3. Calnexin has been shown to be associated with several cell surface proteins, including MHC class I heavy chain, T-cell receptor (TCR), and B cell membrane immunoglobulin during translocation through the ER. It also forms complexes with other resident ER proteins involved in Ca2+-dependent retention of proteins.

Spécificité

Mouse monoclonal clone TO-5 anti-Calnexin antibody recognizes human Calnexin, ~90 kDa.

Application

Anti-Calnexin antibody, Mouse monoclonal has been used in:
  • enzyme-linked immunosorbent assay (ELISA)
  • immunoblotting
  • flow cytometry
  • immunocytochemistry
  • immunohistochemistry
  • immunofluorescence analysis

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM 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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Produit(s) apparenté(s)

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

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

Identification of RUVBL1 and RUVBL2 as Novel Cellular Interactors of the Ebola Virus Nucleoprotein
Morwitzer MJ, et al.
Viruses, 11(4), 372-372 (2019)
Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
Michalak M, et al.
The Biochemical Journal, 417(3), 651-666 (2009)
Aleksandr Treyer et al.
Molecular biology of the cell, 27(14), 2259-2271 (2016-05-27)
For several decades, the trans-Golgi network (TGN) was considered the most distal stop and hence the ultimate protein-sorting station for distinct apical and basolateral transport carriers that reach their respective surface domains in the direct trafficking pathway. However, recent reports
E Giacomini et al.
Human reproduction (Oxford, England), 36(8), 2249-2274 (2021-07-01)
Are uterine fluid-derived extracellular vesicles (UF-EVs) a 'liquid biopsy' reservoir of biomarkers for real-time monitoring of endometrial status? The transcriptomic cargo of UF-EVs reflects the RNA profile of the endometrial tissue as well as changes between the non-receptive and the
Begomoviral Movement Protein Effects in Human and Plant Cells: Towards New Potential Interaction Partners
Krapp S, et al.
Viruses, 9(11), 334-334 (2017)

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