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Key Documents

N8789

Sigma-Aldrich

Anti-NONO (N-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-NMT55, Anti-NRB54, Anti-Non-pou domain-containing octamer-binding protein, Anti-p54nrb

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~55 kDa

Espèces réactives

human

Concentration

~1.0 mg/mL

Technique(s)

immunoprecipitation (IP): 2.5-5 μg using HeLa cell lysates
indirect immunofluorescence: 2-5 μg/mL using paraformaldehyde fixed HeLa cells
western blot: 1-2 μg/mL using NIH-3T3 lysate

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 ... NONO(4841)
mouse ... Nono(53610)
rat ... Nono(317259)

Description générale

Non-POU Domain-Containing Octamer-Binding Protein (NONO) is ubiquitously expressed and is composed of two tandem RNP-type RNA-recognition motifs and a putative helix-turn-helix domain followed by a highly charged region. It is enriched in paraspeckles, a nucleoplasmic compartment, and relocalizes to cap structures at the nucleolar periphery when transcription is inhibited.
Non-POU domain containing octamer binding protein (NONO) is part of the Drosophila behavior/human splicing (DBHS) protein family. It has a molecular weight of 54kDa and the gene encoding it is localized on human chromosome Xq13.1.

Application

Anti-NONO (N-terminal) antibody produced in rabbit has been used in immunoprecipitation, immunoblotting. It may be used for immunofluorescence.

Actions biochimiques/physiologiques

Non-POU Domain-Containing Octamer-Binding Protein (NONO) is a nuclear protein implicated in numerous processes including transcription, pre-mRNA processing, nuclear retention of edited RNA, and DNA relaxation. NONO is phosphorylated on multiple sites during mitosis and is a target of the peptidylprolyl isomerase (Pin1).
Non-POU domain containing octamer binding protein (NONO) modulates transcription. Loss-of-function of the protein has been linked to human intellectual disability. The protein also has a role in synaptic transcription and regulation of the circadian clock. NONO also has a function in DNA damage response.

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

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

RNA-binding protein PSPC1 promotes the differentiation-dependent nuclear export of adipocyte RNAs.
Wang J, et al.
The Journal of Clinical Investigation, 127(3), 987-1004 (2017)
Promoter-dependent translation controlled by p54nrb and hnRNPM during myoblast differentiation.
Ainaoui N, et al.
Testing, 10(9), e0136466-e0136466 (2015)
Prefrontal cortex shotgun proteome analysis reveals
altered calcium homeostasis and immune system
imbalance in schizophrenia
Daniel Martins-de-Souza
European Archives of Psychiatry and Clinical Neuroscience (2009)
The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1.
Proteau A, et al.
Journal of molecular biology, 346(4), 1163-1172 (2005)
Promoter-Dependent Translation Controlled by p54nrb and hnRNPM during Myoblast Differentiation
Nadera Ainaoui
PLoS ONE (2015)

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