Nu.Q® Discover
A complete solution to profiling nucleosomes.
Explore the exciting role of epigenetics through accessing our proprietary Nucleosomics™ platform, Nu.Q® Discover.
What is Nu.Q® Discover?
Nu.Q® Discover gives you access to a range of state-of-the-art assays, built on our proprietary Nucleosomics™ platform, for rapid epigenetic profiling in disease model development, preclinical testing and clinical studies.
What are the benefits?
You can use our assays to answer your clinical questions, such as measuring treatment efficacy, or on-target and off-target effects in drug development.
Applications include biomarker discovery in oncology, inflammatory conditions, and more.
Who can benefit?
If you are a pharmaceutical company or an academic research institution, we can work with you to support your development needs and help you execute your vision.
What does it cost?
To purchase our H3.1 assay or receive a quote for any of the assays within our Nu.Q® Discover portfolio, please contact our commercial team today by emailing asknu.qdiscover@volition.com
Where are the assays processed?
Our Silver One site in Belgium offers cutting edge, purpose-built manufacturing and processing facilities. We manufacture our own plates and large scale batches of our antibodies on beads.
Our expert team will be on hand throughout, to offer guidance and support and to fulfil your needs. Volition’s objective is to establish long-term mutually beneficial commercial relationships (subject to IP).
How can I find out more?
If you would like more information about Nu.Q® Discover, download our clinical paper, read our leaflet, or get in touch with our commercial team directly by emailing asknu.qdiscover@volition.com
You can also access our technical documentation here.
Nu.Q® Discover Assays
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Nu.Q®
H3.1
The nucleosome core particle is composed of an octamer of histone proteins comprising a tetramer of histone H3 and H4 and two dimers H2A-H2B, around which 147bp of DNA is wrapped. In addition to the post-translational modifications occurring on the N-terminal tails of the histone, histone variants (for histone H3, H2A and H2B but not H4) could be incorporated. The canonical H3.1 histone variant, incorporated during S-phase, is maintained at high levels in cells dividing at a high rate but is massively evicted in cells undergoing their last cell cycle before exit to differentiation.
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Nu.Q® - Methylation
H3K27Me3
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the tri-methylation of lysine 27 on H3 protein. This modification is mainly associated with genes repression and often found in heterochromatin regions. H3K27Me3 is regulated by Enhancer of Zeste (EZH2) of Polycomb Repressive Complex PRC2. H3K27me3 has been implicated in numerous of diseases including cancer and it has also been linked to the repair of DNA damage.
H3K36Me3
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the tri-methylation of lysine 36 on H3 protein. This modification is often found in gene body of transcriptionally active genes. The trimethylation is mainly catalysed by SETD2 methyltransferase.
H3K4Me2
Epigenetic modification on the Histone 3 (H3). This mark indicates the di-methylation of lysine 4 on H3 protein and is enriched in cis-regulatory regions in particular, promoters of transcriptionally active genes.
H3K9Me3
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the tri-methylation of lysine 9 on H3 protein and is associated with gene repression and silent hetero- chromatin. H3K9me3 plays a major role in the cell integrity, genomic stability, and heterochromatin maintenance.
H3K9Me1
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the (mono-)methylation of lysine 9 on H3 protein. H3K9Me1 is a critical marker for transcriptional silencing. This mark is a target of HP1 proteins and primes the formation of functional heterochromatin, a critical chromatin landmark for genome stability.
H3K4Me1
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the (mono-)methylation of lysine 4 on H3 protein. Histone H3 lysine 4 (H3K4) methylation is widely regarded as a mark of transcriptional activation. In particular, H3K4Me1 is commonly considered a chromatin hallmark of enhancers (while high level of tri-methylation of lysine 4 on the histone H3 -H3K4Me3- predominantly mark promoters). However, not all H3K4Me1-enriched regions correspond to enhancers, this mark is also present at promoters. This implies that H3K4me1 modification has a context-dependent role in regulating transcription.
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Nu.Q® - Acetylation
H3K18Ac
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the acetylation of lysine 18 on H3 protein. Histone acetylation is commonly linked to active transcription. Indeed, such modifications lead to chromatin relaxation that enables the activation of gene transcription. Moreover, this modification can serve as docking sites for proteins involved in gene activation, such as transcriptional activators and chromatin remodeling complexes.
H3K9Ac
Epigenetic modification on the Histone 3 (H3). This mark indicates the acetylation of lysine 9 on H3 protein. This mark, as H3K14Ac, is linked to gene activation and active promoters.
H3K27Ac
Epigenetic modification on the Histone 3 (H3). This mark indicates the acetylation of lysine 27 on H3 protein. This mark is associated with the higher activation of transcription, and primarily defined as an active enhancer mark. H3K27Ac is also found surrounding transcriptional start sites (TSS).
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Nu.Q®- Other PTMS
H3S10Ph
Epigenetic modification of Nucleosome on the Histone 3 (H3). This mark indicates the phosphorylation of serine 10 on H3 protein. This modification, done by Aurora kinase, plays a role in mitosis.
pH2AX
Epigenetic modification on the isoform X of Histone 2A (H2AX). This mark indicates the phosphorylation of serine 139 on H2AX protein. This modification correlates with double-strand DNA damage.
H3R8Cit
Epigenetic modification on the Histone 3 (H3). This mark indicates the citrullination of arginine 8 on H3 protein. Protein arginine deiminase 4 (PAD4) mediates citrullination of histone tail residues.
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Nu.Q® Mutation
H3K27M
Mutation in the Histone 3 (H3) on the lysine 27 replaced by a Methionine and is found in aggressive pediatric gliomas.
Nu.Q® Discover Assays
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Nu.Q®
H3.1
The nucleosome core particle is composed of an octamer of histone proteins comprising a tetramer of histone H3 and H4 and two dimers H2A-H2B, around which 147bp of DNA is wrapped. In addition to the post-translational modifications occurring on the N-terminal tails of the histone, histone variants (for histone H3, H2A and H2B but not H4) could be incorporated. The canonical H3.1 histone variant, incorporated during S-phase, is maintained at high levels in cells dividing at a high rate but is massively evicted in cells undergoing their last cell cycle before exit to differentiation.
-
Nu.Q® - Methylation
H3K27Me3
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the tri-methylation of lysine 27 on H3 protein. This modification is mainly associated with genes repression and often found in heterochromatin regions. H3K27Me3 is regulated by Enhancer of Zeste (EZH2) of Polycomb Repressive Complex PRC2. H3K27me3 has been implicated in numerous of diseases including cancer and it has also been linked to the repair of DNA damage.
H3K36Me3
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the tri-methylation of lysine 36 on H3 protein. This modification is often found in gene body of transcriptionally active genes. The trimethylation is mainly catalysed by SETD2 methyltransferase.
H3K4Me2
Epigenetic modification on the Histone 3 (H3). This mark indicates the di-methylation of lysine 4 on H3 protein and is enriched in cis-regulatory regions in particular, promoters of transcriptionally active genes.
H3K9Me3
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the tri-methylation of lysine 9 on H3 protein and is associated with gene repression and silent hetero- chromatin. H3K9me3 plays a major role in the cell integrity, genomic stability, and heterochromatin maintenance.
H3K9Me1
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the (mono-)methylation of lysine 9 on H3 protein. H3K9Me1 is a critical marker for transcriptional silencing. This mark is a target of HP1 proteins and primes the formation of functional heterochromatin, a critical chromatin landmark for genome stability.
H3K4Me1
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the (mono-)methylation of lysine 4 on H3 protein. Histone H3 lysine 4 (H3K4) methylation is widely regarded as a mark of transcriptional activation. In particular, H3K4Me1 is commonly considered a chromatin hallmark of enhancers (while high level of tri-methylation of lysine 4 on the histone H3 -H3K4Me3- predominantly mark promoters). However, not all H3K4Me1-enriched regions correspond to enhancers, this mark is also present at promoters. This implies that H3K4me1 modification has a context-dependent role in regulating transcription.
-
Nu.Q® - Acetylation
H3K18Ac
Epigenetic modification on the Histone 3 (H3). This epigenetic mark indicates the acetylation of lysine 18 on H3 protein. Histone acetylation is commonly linked to active transcription. Indeed, such modifications lead to chromatin relaxation that enables the activation of gene transcription. Moreover, this modification can serve as docking sites for proteins involved in gene activation, such as transcriptional activators and chromatin remodeling complexes.
H3K9Ac
Epigenetic modification on the Histone 3 (H3). This mark indicates the acetylation of lysine 9 on H3 protein. This mark, as H3K14Ac, is linked to gene activation and active promoters.
H3K27Ac
Epigenetic modification on the Histone 3 (H3). This mark indicates the acetylation of lysine 27 on H3 protein. This mark is associated with the higher activation of transcription, and primarily defined as an active enhancer mark. H3K27Ac is also found surrounding transcriptional start sites (TSS).
-
Nu.Q®- Other PTMS
H3S10Ph
Epigenetic modification of Nucleosome on the Histone 3 (H3). This mark indicates the phosphorylation of serine 10 on H3 protein. This modification, done by Aurora kinase, plays a role in mitosis.
pH2AX
Epigenetic modification on the isoform X of Histone 2A (H2AX). This mark indicates the phosphorylation of serine 139 on H2AX protein. This modification correlates with double-strand DNA damage.
H3R8Cit
Epigenetic modification on the Histone 3 (H3). This mark indicates the citrullination of arginine 8 on H3 protein. Protein arginine deiminase 4 (PAD4) mediates citrullination of histone tail residues.
-
Nu.Q® Mutation
H3K27M
Mutation in the Histone 3 (H3) on the lysine 27 replaced by a Methionine and is found in aggressive pediatric gliomas.