Anti-Acetyl-Histone H4 (Lys8) Mouse mAb
PTM-164
ApplicationsImmunoFluorescence, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityHuman, Mouse, Rat
Overview
- SupplierPTM BIO
- Product NameAnti-Acetyl-Histone H4 (Lys8) Mouse mAb
- Delivery Days Customer5
- ApplicationsImmunoFluorescence, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry, ImmunoHistoChemistry Paraffin
- Applications SupplierWB, IHC-P, ICC/IF, ChIP
- Category SupplierAntibody
- CertificationResearch Use Only
- ClonalityMonoclonal
- Clone ID12F10
- ConjugateUnconjugated
- HostMouse
- IsotypeIgG
- Protein IDP62805
- Protein NameHistone H4
- Scientific DescriptionHistone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. 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, gene transcription, etc. Histone acetylation occurs primarily at multiple lysine residues on the amino-terminal of core histones, in response to various stimuli and plays vital roles in the regulation of gene expression, DNA damage repair, chromatin dynamics, etc. Mostly, histone H2A is primarily acetylated at Lys5, 9, 15, and 36; H2B is primarily acetylated at Lys5, 12, 15, 16, and 20. Histone H3 is primarily acetylated at Lys4, 9, 14, 18, 23, 27, 56, and 79. Histone H4 is primarily acetylated at Lys5, 8, 12, 16, and 20. Histone acetyltransferases (HATs) and histone deacetylases (HDACs) are major regulating factors.
- 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
- He Huang, et al. 'The regulatory enzymes and protein substrates for the lysine bèta-hydroxybutyrylation pathway' Science Advances (2021)Read more
- Zijun Peng, et al. 'Multi-omics analyses reveal the mechanisms of Arsenic-induced male reproductive toxicity in mice' JOURNAL OF HAZARDOUS MATERIALS (2021)Read more
- Weimin Zhang, et al. 'Probing the Function of Metazoan Histones with a Systematic Library of H3 and H4 Mutants' DEVELOPMENTAL CELL (2018)Read more
- Zhengchang Wu, et al. 'Insight into mechanisms of pig lncRNA FUT3-AS1 regulating E. coli F18-bacterial diarrhea' PLoS Pathogens (2022)Read more
- Yinyun Ni, et al. 'miR-15a-5p inhibits metastasis and lipid metabolism by suppressing histone acetylation in lung cancer' FREE RADICAL BIOLOGY AND MEDICINE (2020)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
- Runhua Du, et al. 'Sirtuin 1/sirtuin 3 are robust lysine delactylases and sirtuin 1-mediated delactylation regulates glycolysis' iScience (2024)Read more