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Merck

N8664

Sigma-Aldrich

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

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

Sinónimos:

Anti-NMT55, Anti-NRB54, Anti-Non-pou domain-containing octamer-binding protein, Anti-Nuclear RNA-binding protein, 54-KD, Anti-p54nrb

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rabbit

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

formulario

buffered aqueous solution

mol peso

antigen ~55 kDa

reactividad de especies

human

concentración

~1.0 mg/mL

técnicas

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 cell lysates

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... NONO(4841)

Descripción general

Non-POU domain containing octamer binding (NONO) is ubiquitously expressed and comprises 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.

Aplicación

Anti-NONO (C-terminal) antibody produced in rabbit has been used in immunoblotting and immunofluorescence.
Anti-NONO (N-terminal) antibody produced in rabbit has been used in immunoprecipitation.

Acciones bioquímicas o fisiológicas

NONO (also termed as p54nrb) is a nuclear protein implicated in numerous processes including transcription, pre-mRNA processing, nuclear retention of edited RNA and DNA relaxation. NONO was suspected to be involved in pre-mRNA splicing. Later it was found that NONO and PSF mediate different functions depending on their intracellular location.
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.

Forma física

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

Cláusula de descargo de responsabilidad

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 clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

nwg

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

A crystallographic study of human NONO (p54nrb): overcoming pathological problems with purification, data collection and noncrystallographic symmetry
Knott GJ, et al.
Acta crystallographica. Section D, Structural biology, 761-761 (2016)
Prefrontal cortex shotgun proteome analysis reveals
altered calcium homeostasis and immune system
imbalance in schizophrenia
Daniel Martins-de-Souza
European Journal of Anaesthesiology. Supplement (2009)
Promoter-Dependent Translation Controlled by p54nrb and hnRNPM during Myoblast Differentiation
Nader A
PLoS ONE (2015)
Luisa Gabriel et al.
Journal of cell science, 134(10) (2021-05-27)
Zα domains recognize the left-handed helical Z conformation of double-stranded nucleic acids. They are found in proteins involved in the nucleic acid sensory pathway of the vertebrate innate immune system and host evasion by viral pathogens. Previously, it has been
Paraspeckles: a novel nuclear domain.
Fox AH, et al.
Current Biology, 12(1), 13-25 (2002)

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