Anti-Acetyl-Histone H3 (Lys14) Mouse mAb
PTM-157
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityHuman, Mouse, Rat
Overview
- SupplierPTM BIO
- Product NameAnti-Acetyl-Histone H3 (Lys14) Mouse mAb
- Delivery Days Customer5
- ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry, ImmunoHistoChemistry Paraffin
- Applications SupplierWB, IHC-P, ICC/IF, IP, ChIP
- Category SupplierAntibody
- CertificationResearch Use Only
- ClonalityMonoclonal
- Clone ID1A4
- ConjugateUnconjugated
- HostMouse
- 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 G and immunogen affinity purified
- Storage InstructionStore at -20°C. Avoid freeze/thaw cycles.
- UNSPSC12352203
References
- Pu Chen, et al. 'An Integrated Approach for Combinatorial Readout of Dual Histone Modifications by Epigenetic Tandem Domains' ANALYTICAL CHEMISTRY (2020)Read more
- Shasha Shi, et al. 'Competitive Inhibition of Lysine Acetyltransferase 2B by a Small Motif of the Adenoviral Oncoprotein E1A *' JOURNAL OF BIOLOGICAL CHEMISTRY (2016)Read more
- Zhang Ning, et al. 'BcRPD3-Mediated Histone Deacetylation Is Involved in Growth and Pathogenicity of Botrytis cinerea' Frontiers in Microbiology (2020)Read more
- Lan Huahui, et al. 'The Aspergillus flavus Histone Acetyltransferase AflGcnE Regulates Morphogenesis, Aflatoxin Biosynthesis, and Pathogenicity' Frontiers in Microbiology (2016)Read more
- Xia Liu, et al. 'Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells' VIROLOGY (2014)Read more
- Qiangzhen Yang, et al. 'Cadmium inhibits lysine acetylation and succinylation inducing testicular injury of mouse during development' TOXICOLOGY LETTERS (2018)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