Anti-Acetyl-Histone H3 (Lys23) Rabbit pAb
PTM-115
ApplicationsWestern Blot
Product group Antibodies
ReactivityHuman, Mouse, Rat
Overview
- SupplierPTM BIO
- Product NameAnti-Acetyl-Histone H3 (Lys23) Rabbit pAb
- Delivery Days Customer5
- Antibody SpecificityAnti-Acetyl-Histone H3 (Lys23) Rabbit pAb detects histone H3 only when it is acetylated at Lys23. This antibody has been shown to selectively recognize acetylated H3 peptide at Lys23, but not the structurally similar butyrylated H3 peptides at Lys23.
- ApplicationsWestern Blot
- Applications SupplierWB
- Category SupplierAntibody
- CertificationResearch Use Only
- ClonalityPolyclonal
- ConjugateUnconjugated
- HostRabbit
- IsotypeIgG
- Protein IDP68431
- Protein NameHistone H3.1
- Scientific DescriptionHistone post-translational modifications (PTMs), known as the “histone code”, are key mechanisms of epigenetics that modulate chromatin structures. The PTMs on histone including acetylation, methylation, Phosphorylatedrylation, and novel acylations directly affect the accessibility of chromatin to transcription factors and other epigenetic regulators, altering genome stability and gene transcription. Histone acetylation, tightly controlled by the opposing action of histone acetyltransferases (HATs) and histone deacetylases (HDACs), occurs primarily at lysine residues on the N-terminal tails of histones H2A (Lys5, 9, and 15), H2B (Lys5,12, 15, 16, and 20), H3 (Lys4, 9, 14, 18, 23, 27, and 36), and H4 (Lys5, 8, 12, 16, and 20), and plays vital roles in the regulation of gene expression, DNA damage repair, chromatin dynamics, etc.
- Shelf life instructionStable for 12 months from date of receipt/reconstitution.
- ReactivityHuman, Mouse, Rat
- Reactivity SupplierHuman, Mouse, Rat
- Reactivity Supplier NoteProtein A and immunogen affinity purified
- Storage InstructionStore at -20°C. Avoid freeze/thaw cycles.
- UNSPSC12352203
References
- Wang Xuemei, et al. 'Proteomic Analysis of Serum Lysine Acetylation in Uyghur Patients With T2DM' Frontiers in Molecular Biosciences (2022)Read more
- Guan Haipeng, et al. 'Diverse modes of H3K36me3-guided nucleosomal deacetylation by Rpd3S' NATURE (2023)Read more
- Bing Zhou, et al. 'Amelioration of nonalcoholic fatty liver disease by inhibiting the deubiquitylating enzyme RPN11' Cell Metabolism (2024)Read more