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Rabbit Anti-Di-Methyl-Histone H4 (Lys20) Recombinant Antibody (D2D9P) (CBMAB-CP1025-LY)

The product is antibody recognizes Di-Methyl-Histone H4 (Lys20). The antibody D2D9P immunoassay techniques such as: WB.
See all Di-Methyl-Histone H4 (Lys20) antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat, Monkey
Clone
D2D9P
Antibody Isotype
IgG
Application
WB

Basic Information

Immunogen
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the amino terminus of histone H4 in which Lys20 is di-methylated.
Specificity
Human, Mouse, Rat, Monkey
Antibody Isotype
IgG
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
100 µg/ml BSA, 50% glycerol
Preservative
0.02% sodium azide
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Di-Methyl-Histone H4 (Lys20)
Function
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Biological Process
DNA replication-dependent nucleosome assembly Source: UniProtKB
DNA replication-independent nucleosome assembly Source: UniProtKB
DNA-templated transcription, initiation Source: InterPro
Negative regulation of megakaryocyte differentiation Source: UniProtKB
Nucleosome assembly Source: UniProtKB
Telomere organization Source: BHF-UCL
Cellular Location
Nucleus; Chromosome
Involvement in disease
Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.
PTM
Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin.
Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.
Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3) (PubMed:12086618, PubMed:15964846, PubMed:17967882). Monomethylation is performed by KMT5A/SET8 (PubMed:15964846). Dimethylation and trimethylation is performed by KMT5B and KMT5C and induces gene silencing (By similarity). Monomethylated at Lys-13 (H4K12me1) by N6AMT1; H4K12me1 modification is present at the promoters of numerous genes encoding cell cycle regulators (PubMed:31061526).
Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4.
Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me).
Ufmylated; monofmylated by UFL1 at Lys-32 (H4K31Ufm1) in response to DNA damage.
Sumoylated, which is associated with transcriptional repression.
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.
Butyrylation of histones marks active promoters and competes with histone acetylation.
Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.
Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.

Rabdano, S. O., Shannon, M. D., Izmailov, S. A., Gonzalez Salguero, N., Zandian, M., Purusottam, R. N., ... & Jaroniec, C. P. (2021). Histone H4 tails in nucleosomes: a fuzzy interaction with DNA. Angewandte Chemie International Edition, 60(12), 6480-6487.

Lin, C., Li, H., Liu, J., Hu, Q., Zhang, S., Zhang, N., ... & Zhang, Y. (2020). Arginine hypomethylation-mediated proteasomal degradation of histone H4—an early biomarker of cellular senescence. Cell Death & Differentiation, 27(9), 2697-2709.

Samata, M., Alexiadis, A., Richard, G., Georgiev, P., Nuebler, J., Kulkarni, T., ... & Akhtar, A. (2020). Intergenerationally maintained histone H4 lysine 16 acetylation is instructive for future gene activation. Cell, 182(1), 127-144.

Vulliamy, P., Gillespie, S., Armstrong, P. C., Allan, H. E., Warner, T. D., & Brohi, K. (2019). Histone H4 induces platelet ballooning and microparticle release during trauma hemorrhage. Proceedings of the National Academy of Sciences, 116(35), 17444-17449.

Silvestre-Roig, C., Braster, Q., Wichapong, K., Lee, E. Y., Teulon, J. M., Berrebeh, N., ... & Soehnlein, O. (2019). Externalized histone H4 orchestrates chronic inflammation by inducing lytic cell death. Nature, 569(7755), 236-240.

Bao, X., Liu, Z., Zhang, W., Gladysz, K., Fung, Y. M. E., Tian, G., ... & Li, X. D. (2019). Glutarylation of histone H4 lysine 91 regulates chromatin dynamics. Molecular cell, 76(4), 660-675.

Qin, B., Yu, J., Nowsheen, S., Wang, M., Tu, X., Liu, T., ... & Lou, Z. (2019). UFL1 promotes histone H4 ufmylation and ATM activation. Nature communications, 10(1), 1-13.

Long, M., Sun, X., Shi, W., Yanru, A., Leung, S. T., Ding, D., ... & Ishibashi, T. (2019). A novel histone H4 variant H4G regulates rDNA transcription in breast cancer. Nucleic Acids Research, 47(16), 8399-8409.

Holt, M. V., Wang, T., & Young, N. L. (2019). High-throughput quantitative top-down proteomics: histone H4. Journal of The American Society for Mass Spectrometry, 30(12), 2548-2560.

Dhar, S., Gursoy-Yuzugullu, O., Parasuram, R., & Price, B. D. (2017). The tale of a tail: histone H4 acetylation and the repair of DNA breaks. Philosophical Transactions of the Royal Society B: Biological Sciences, 372(1731), 20160284.

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For research use only. Not intended for any clinical use.

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