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Biological Description
| Specificity | Acetyl-Histone H4 (Lys5) Rabbit mAb detects endogenous levels of Histone H4 only when Acetylated at Lys5. |
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| Background | Acetyl-Histone H4 (Lys5) refers to the post-translationally modified form of histone H4 in which the lysine residue at position 5 on its N-terminal tail is acetylated. Histone H4 is a core component of the nucleosome, the fundamental unit of chromatin in eukaryotic cells, and consists of a globular histone fold domain for nucleosome assembly and an N-terminal tail rich in lysine residues (including Lys5, Lys8, Lys12, and Lys16) that are targets for dynamic acetylation. Acetylation at Lys5, one of the earliest histone H4 modifications, neutralizes the positive charge of the lysine side chain, reducing the histone's affinity for negatively charged DNA. This leads to a relaxation of chromatin structure, facilitating key nuclear processes such as transcription, DNA replication, and DNA repair. Lys5 acetylation is associated with active chromatin states, partly through its role in recruiting bromodomain-containing proteins and chromatin remodeling complexes. This mark frequently occurs alongside Lys12 acetylation during nucleosome assembly, suggesting a coordinated mechanism for regulating chromatin maturation and epigenetic memory. Dysregulation of histone H4 Lys5 acetylation is linked to developmental disorders and cancer. |
Usage Information
| Application | WB, IP, IHC, IF, ChIP, ELISA | Dilution |
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| Reactivity | Mouse, Rat, Human | ||||||||||
| Source | Rabbit | MW | 11 kDa | ||||||||
| Storage Buffer | PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3 | Storage (from the date of receipt) |
-20°C (avoid freeze-thaw cycles), 2 years | ||||||||
References
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