Lane 1: CRC cell lysate
Lane 2: Hela cell lysate
Lane 3: SH-SY5Y cell lysate
Recombinant Rabbit monoclonal primary
Recombinant Acetyl Histone H4 (acetyl K5) Monoclonal Antibody (ET1602-40)
Synthetic peptide within human histone h4 aa 2-12 (acetyl k5).
CRC cell lysate, Hela cell lysate, SH-SY5Y cell lysate, Hela, CRC, SH-SY5Y, rat brain tissue, human tonsil tissue, human colon carcinoma tissue, mouse testis tissue, mouse colon tissue, mouse brain tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
Histone H4(acetyl K5)
Histone gene cluster 1, H4A antibody; Histone gene cluster 2, H4 antibody; dJ160A22.1 antibody; dJ160A22.2 antibody; dJ221C16.1 antibody; dJ221C16.9 antibody; FO108 antibody; H4 antibody; H4 histone family, member A antibody; H4 histone family, member B antibody; H4 histone family, member C antibody; H4 histone family, member D antibody; H4 histone family, member E antibody; H4 histone family, member G antibody; H4 histone family, member H antibody; H4 histone family, member I antibody; H4 histone family, member J antibody; H4 histone family, member K antibody; H4 histone family, member M antibody; H4 histone family, member N antibody; H4 histone, family 2 antibody; H4/A antibody; H4/B antibody; H4/C antibody; H4/D antibody; H4/E antibody; H4/G antibody; H4/H antibody; H4/I antibody; H4/J antibody; H4/K antibody; H4/M antibody; H4/N antibody; H4/O antibody; H4/p antibody; H4_HUMAN antibody; H4F2 antibody; H4F2iii antibody; H4F2iv antibody; H4FA antibody; H4FB antibody; H4FC antibody; H4FD antibody; H4FE antibody; H4FG antibody; H4FH antibody; H4FI antibody; H4FJ antibody; H4FK antibody; HIST1 cluster, H4A antibody; HIST1 cluster, H4B antibody; HIST1 cluster, H4D antibody; HIST2H4 antibody; Hist4 cluster, H4 antibody; Hist4h4 antibody; histone 1, H4a antibody; histone 1, H4c antibody; histone 1, H4d antibody; histone 1, H4f antibody; histone 1, H4h antibody; histone 1, H4i antibody; histone 1, H4j antibody; histone 1, H4k antibody; histone 1, H4l antibody; histone 2, H4a antibody; histone 2, H4b antibody; Histone 4 family, member M antibody; histone 4, H4 antibody; histone cluster 1, H4 antibody; histone cluster 1, H4a antibody; histone cluster 1, H4b antibody; histone cluster 1, H4c antibody; histone cluster 1, H4d antibody; histone cluster 1, H4e antibody; histone cluster 1, H4f antibody; histone cluster 1, H4h antibody; histone cluster 1, H4i antibody; histone cluster 1, H4j antibody; histone cluster 1, H4k antibody; histone cluster 1, H4l antibody; histone cluster 2, H4a antibody; histone cluster 2, H4b antibody; histone cluster 4, H4 antibody; Histone family, member A antibody; Histone family, member B antibody; Histone family, member D antibody; Histone family, member H antibody; Histone family, member I antibody; Histone family, member L antibody; Histone gene cluster 1, H4 antibody; Histone gene cluster 1, H4D antibody; Histone gene cluster 1, H4E antibody; Histone gene cluster 1, H4K antibody; Histone gene cluster 4, H4 antibody; Histone gene cluster 4, H4 histone antibody; Histone H4 antibody; histone IV, family 2 antibody
Belongs to the histone H4 family.
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). Monomethylation is performed by SET8. Dimethylation and trimethylation is performed by KMT5B and KMT5C and induces gene silencing (By similarity).; 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).; 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.
Eukaryotic histones are basic and water soluble nuclear proteins that form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene, that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.
Qin, Ge et al.
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