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Documentos Principais

C7617

Sigma-Aldrich

Anti-Calnexin antibody, Mouse monoclonal

enhanced validation

clone TO-5, purified from hybridoma cell culture

Sinônimo(s):

Anti-CANX, Anti-CNX

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.44

fonte biológica

mouse

conjugado

unconjugated

forma do anticorpo

purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

TO-5, monoclonal

Formulário

buffered aqueous solution

peso molecular

antigen ~90 kDa

reatividade de espécies

human

validação aprimorada

independent
Learn more about Antibody Enhanced Validation

concentração

~2 mg/mL

técnica(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.

Isotipo

IgG1

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... CANX(821)

Descrição geral

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.

Especificidade

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

Aplicação

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

forma física

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Induction of a massive endoplasmic reticulum and perinuclear space expansion by expression of lamin B receptor mutants and the related sterol reductases TM7SF2 and DHCR7
Zwerger M, et al.
Molecular Biology of the Cell, 21(2), 354-368 (2010)
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
Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
Michalak M, et al.
The Biochemical Journal, 417(3), 651-666 (2009)
Identification of RUVBL1 and RUVBL2 as Novel Cellular Interactors of the Ebola Virus Nucleoprotein
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