Histone H3.3 (G34R) peptide
Description
Application Data
Description
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Antigenic histone variant H3.3 peptide containing glycine to arginine substitution mutation
Application Data
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Data Sheet Material Safety Data Sheet (MSDS)Catalogue number crb1200376 Antibody Histone H3.3 (G34R) peptide Antigen Peptide Histone H3 (G34R) peptide Protein ID UniProtKB - P84243 Aliases H3 Histone Family Member 3A, H3 Histone, H3.3A H3F3, Histone H3.3, H3F3A Cross-Reactivity Human, Rat, Mouse Target Protein Species Human, Rat, Mouse Storage Stabilisers -20°C Family Histones Disease Area Histones, Tumourigenesis Storage -20°C Citations Voon, H., Udugama, M., Lin, W., Hii, L., Law, R., Steer, D., Das, P., Mann, J. and Wong, L. (2018). Inhibition of a K9/K36 demethylase by an H3.3 point mutation found in paediatric glioblastoma. Nature Commun, 9(1). PMID: 30087349
Wu, G., Broniscer, A., McEachron, T., Lu, C., Paugh, B., Becksfort, J., Qu, C., Ding, L., Huether, R., Parker, M., Zhang, J., Gajjar, A., Dyer, M., Mullighan, C., Gilbertson, R., Mardis, E., Wilson, R., Downing, J., Ellison, D., Zhang, J. and Baker, S. (2012). Somatic histone H3 alterations in pediatric diffuse intrinsic pontine gliomas and non-brainstem glioblastomas. Nature Genet, 44(3), 251-253. PMID: 22286216
References Voon, H., Udugama, M., Lin, W., Hii, L., Law, R., Steer, D., Das, P., Mann, J. and Wong, L. (2018). Inhibition of a K9/K36 demethylase by an H3.3 point mutation found in paediatric glioblastoma. Nature Commun, 9(1). PMID: 30087349
Wu, G., Broniscer, A., McEachron, T., Lu, C., Paugh, B., Becksfort, J., Qu, C., Ding, L., Huether, R., Parker, M., Zhang, J., Gajjar, A., Dyer, M., Mullighan, C., Gilbertson, R., Mardis, E., Wilson, R., Downing, J., Ellison, D., Zhang, J. and Baker, S. (2012). Somatic histone H3 alterations in pediatric diffuse intrinsic pontine gliomas and non-brainstem glioblastomas. Nature Genet, 44(3), 251-253. PMID: 22286216
Histone H3.3 is a replication-independent histone variant, which replaces canonical histone H3.1/2 outside of S phase. H3.3 is expressed throughout the cell cycle, as well as in quiescent cells and is referred to as the “replacement histone”. H3.3 is largely deposited in a DNA synthesis-independent fashion by a distinct set of chaperones proteins. H3.3 accumulates in post mitotic cells, such as cerebral cortical neurons and is incorporated at sites of UV damage where it protects against sensitivity to UV light.
H3.3 deposition occurs on DNA sequences that are transiently nucleosome-free, such as during transcription and DNA repair, therefore serving as a marker for regions of high transcriptional activity. H3.3 is also enriched in heterochromatic subtelomeric and pericentromeric regions. H3.3 plays important roles in many developmental contexts such as in stem cells, during fertilization and reproduction and during reprogramming of genomes following fertilization or somatic cell nuclear transfer.
Mutations in histone H3.3 are common events in certain cancers. H3.3 G34R (glycine to arginine) substitution mutation is found in high prevalence in paediatric high-grade glioblastoma (HGG), chondroblastoma, and giant cell tumours of the bone.