Mono-methyl-Histone H3.1 (R128) Recombinant Monoclonal Antibody

The production process of the mono-methyl-histone H3.1 (R128) recombinant monoclonal antibody begins with the cloning of genes that encode the HIST1H3A antibody, encompassing both heavy and light chains. These cloned genes are incorporated into expression vectors, which are then introduced into host cells through transfection. The host cells are then responsible for producing and secreting the antibody. Following purification through affinity chromatography to ensure purity, the antibody undergoes comprehensive functionality testing in ELISA and WB applications, guaranteeing accurate detection of the human and mouse HIST1H3A proteins mono-methylated at R128.

Histone H3.1 mono-methylation at arginine 128 (R128) can promote either transcriptional activation or repression, depending on the specific cellular context and the proteins involved. H3.1 R128 mono-methylation serves as an epigenetic signal, indicating specific chromatin states and influencing essential cellular processes like differentiation, development, and cellular identity.

Histone H3.1 is a core component of nucleosomes. Nucleosomes play a crucial role in wrapping and compacting DNA into chromatin, thereby limiting DNA accessibility to cellular machinery that requires DNA as a template. Consequently, histones are central to the regulation of transcription, DNA repair, DNA replication, and chromosomal stability. DNA accessibility is regulated through a complex set of post-translational modifications of histones, collectively known as the histone code, and nucleosome remodeling.

Relevant Research Studies:

1. Data indicates the mechanism for epigenetic regulation in cancer by inducing E3 ubiquitin ligase NEDD4-dependent histone H3 ubiquitination. PMID: 28300060
2. The identification of increased expression of H3K27me3 during a patient's clinical course can be helpful for determining whether the tumors are heterochronous. PMID: 29482987
3. This research reports that JMJD5, a Jumonji C (JmjC) domain-containing protein, is a Cathepsin L-type protease that mediates histone H3 N-tail proteolytic cleavage under stress conditions that cause a DNA damage response. PMID: 28982940
4. Data suggests that Ki-67 antigen proliferative index has important limitations and phosphohistone H3 (PHH3) is an alternative proliferative marker. PMID: 29040195
5. These results identify cytokine-induced histone 3 lysine 27 trimethylation as a mechanism that stabilizes gene silencing in macrophages. PMID: 27653678
6. This data indicates that, in the early developing human brain, HIST1H3B constitutes the largest proportion of H3.1 transcripts among H3.1 isoforms. PMID: 27251074
7. This series of 47 diffuse midline gliomas, histone H3-K27M mutation was mutually exclusive with IDH1-R132H mutation and EGFR amplification, rarely co-occurred with BRAF-V600E mutation, and was commonly associated with p53 overexpression, ATRX loss, and monosomy 10. Among these K27M+ diffuse midline gliomas. PMID: 26517431
8. Data show that histone chaperone HIRA co-localizes with viral genomes, binds to incoming viral and deposits histone H3.3 onto these. PMID: 28981850
9. These experiments showed that PHF13 binds specifically to DNA and to two types of histone H3 methyl tags (lysine 4-tri-methyl or lysine 4-di-methyl) where it functions as a transcriptional co-regulator. PMID: 27223324
10. Hemi-methylated CpGs DNA recognition activates UHRF1 ubiquitylation towards multiple lysines on the H3 tail adjacent to the UHRF1 histone-binding site. PMID: 27595565
11. We describe, for the first time, the MR imaging features of pediatric diffuse midline gliomas with histone H3 K27M mutation. PMID: 28183840
12. Approximately 30% of pediatric high-grade gliomas (pedHGG) including GBM and DIPG harbor a lysine 27 mutation (K27M) in histone 3.3 (H3.3) which is correlated with poor outcome and was shown to influence EZH2 function. PMID: 27135271
13. H3F3A K27M mutation in adult cerebellar HGG is not rare. PMID: 28547652
14. Data show that lysyl oxidase-like 2 (LOXL2) is a histone modifier enzyme that removes trimethylated lysine 4 (K4) in histone H3 (H3K4me3) through an amino-oxidase reaction. PMID: 27735137
15. Histone H3 lysine 9 (H3K9) acetylation was most prevalent when the Dbf4 transcription level was highest whereas the H3K9me3 level was greatest during and just after replication. PMID: 27341472
16. SPOP-containing complex regulates SETD2 stability and H3K36me3-coupled alternative splicing. PMID: 27614073
17. Data suggest that binding of the helical tail of histone 3 (H3) with PHD ('plant homeodomain') fingers of BAZ2A or BAZ2B (bromodomain adjacent to zinc finger domain 2A or 2B) requires molecular recognition of secondary structure motifs within the H3 tail and could represent an additional layer of regulation in epigenetic processes. PMID: 28341809
18. The results demonstrate a novel mechanism by which Kdm4d regulates DNA replication by reducing the H3K9me3 level to facilitate formation of the preinitiation complex. PMID: 27679476
19. Histone H3 modifications caused by traffic-derived airborne particulate matter exposures in leukocytes. PMID: 27918982
20. A key role of persistent histone H3 serine 10 or serine 28 phosphorylation in chemical carcinogenesis through regulating gene transcription of DNA damage response genes. PMID: 27996159
21. hTERT promoter mutations are frequent in medulloblastoma and are associated with older patients, prone to recurrence and located in the right cerebellar hemisphere. On the other hand, histone 3 mutations do not seem to be present in medulloblastoma. PMID: 27694758
22. AS1eRNA-driven DNA looping and activating histone modifications promote the expression of DHRS4-AS1 to economically control the DHRS4 gene cluster. PMID: 26864944
23. Data suggest that nuclear antigen Sp100C is a multifaceted histone H3 methylation and phosphorylation sensor. PMID: 27129259
24. The authors propose that histone H3 threonine 118 phosphorylation via Aurora-A alters the chromatin structure during specific phases of mitosis to promote timely condensin I and cohesin disassociation, which is essential for effective chromosome segregation. PMID: 26878753
25. Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its H3 histone recognition. PMID: 27045799
26. Functional importance of H3K9me3 in hypoxia, apoptosis and repression of APAK. PMID: 25961932
27. Taken together, the authors verified that histone H3 is a real substrate for GzmA in vivo in the Raji cells treated by staurosporin. PMID: 26032366
28. We conclude that circulating H3 levels correlate with mortality in sepsis patients and inversely correlate with antithrombin levels and platelet counts. PMID: 26232351
29. Data show that double mutations on the residues in the interface (L325A/D328A) decreases the histone H3 H3K4me2/3 demethylation activity of lysine (K)-specific demethylase 5B (KDM5B). PMID: 24952722
30. Data indicate that minichromosome maintenance protein 2 (MCM2) binding is not required for incorporation of histone H3.1-H4 into chromatin but is important for stability of H3.1-H4. PMID: 26167883
31. Data suggest that histone H3 lysine methylation (H3K4me3) serves a crucial mechanistic role in leukemia stem cell (LSC) maintenance. PMID: 26190263
32. PIP5K1A modulates ribosomal RNA gene silencing through its interaction with histone H3 lysine 9 trimethylation and heterochromatin protein HP1-alpha. PMID: 26157143
33. Data indicate that the lower-resolution mass spectrometry instruments can be utilized for histone post-translational modifications (PTMs) analysis. PMID: 25325711
34. Data indicate that inhibition of lysine-specific demethylase 1 activity prevented IL-1beta-induced histone H3 lysine 9 (H3K9) demethylation at microsomal prostaglandin E synthase 1 (mPGES-1) promoter. PMID: 24886859
35. The authors report that de novo CENP-A assembly and kinetochore formation on human centromeric alphoid DNA arrays is regulated by a histone H3K9 acetyl/methyl balance. PMID: 22473132

HGNC: 4766

OMIM: 137800

KEGG: hsa:8350

STRING: 9606.ENSP00000444823

UniGene: Hs.132854