Anti-Histone H3.3 (G34V) antibody
Description
Application Data
Description
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Recognises glycine to valine substitution mutation of histone variant H3.3 in Western blots and immunohistochemistry with strong signal and low background noise
Application Data
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Anti-Histone H3 (G34V) antibody (crb2005186) Western blot analysis of cell purified recombinant GST-histone H3 proteins.
Lane 1: GST-histone H3.3 wildtype
Lane 2: GST-histone H3.3 K27M
Lane 3: GST-histone H3.3 G34R
Lane 4: GST-histone H3.3 G34V
| Catalogue number | crb2005186 |
|---|---|
| Antibody | Anti-Histone H3.3 (G34V) antibody |
| Antigen Peptide | KLH conjugated synthetic peptide crb1200377e |
| Protein ID | UniProtKB - P84243 |
| Aliases | H3 Histone Family Member 3A, H3 Histone, H3.3A H3F3, Histone H3.3, H3F3A |
| Cross-Reactivity | Human, Rabbit, Mouse |
| Target Protein Species | Human, Rabbit, Mouse |
| Host Species | Rabbit |
| Antibody Type | Polyclonal |
| Concentration | 1mg/ml |
| Validation | 1:1000 (WB), 1:1000 (ELISA), IF, IHC |
| Target | Histone H3 (H3.3) |
| Storage Stabilisers | This material is supplied in PBS containing 0.01% sodium azide and 1% trehalose. The product should be stored at +4°C for short term storage and -20°C for long term storage. Avoid repeated freeze/ thaw cycles. |
| Family | Histones |
| Disease Area | Histones, Tumourigenesis |
| Specificity | Protein |
| Storage | This material is supplied in PBS containing 0.01% sodium azide and 1% trehalose. The product should be stored at +4°C for short term storage and -20°C for long term storage. Avoid repeated freeze/ thaw cycles. |
| Citations | Haque et al. (2017) Acta Neuropathol Commun.5(1):45. PMID: 28587626 |
| 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 G34V (glycine to valine) substitution mutation is found in paediatric high-grade glioblastoma (HGG).
