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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

Synonym(s):

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

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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 solution

mol wt

antigen ~55 kDa

species reactivity

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Biochem/physiol Actions

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.

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.

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Storage Class Code

10 - Combustible liquids

WGK

nwg

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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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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