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C7617

Sigma-Aldrich

Anti-Calnexin antibody, Mouse monoclonal

enhanced validation

clone TO-5, purified from hybridoma cell culture

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Synonym(s):
Anti-CANX, Anti-CNX
MDL number:

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

TO-5, monoclonal

form

buffered aqueous solution

mol wt

antigen ~90 kDa

species reactivity

human

enhanced validation

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... CANX(821)

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Gene Information

human ... CANX(821)

Gene Information

human ... CANX(821)
mouse ... Canx(12330)
rat ... Canx(29144)

Gene Information

human ... CANX(821)

Gene Information

human ... CANX(821)

clone

TO-5, monoclonal

clone

polyclonal

clone

polyclonal

clone

AF8, monoclonal

biological source

mouse

biological source

rabbit

biological source

rabbit

biological source

mouse

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

-

antibody form

purified immunoglobulin

antibody form

IgG fraction of antiserum

antibody form

affinity isolated antibody

antibody form

purified immunoglobulin

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General description

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.

Specificity

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

Physical form

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
Begomoviral Movement Protein Effects in Human and Plant Cells: Towards New Potential Interaction Partners
Krapp S, et al.
Viruses, 9(11), 334-334 (2017)
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)

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