Anti-Acetyl-Histone H3 (Lys4) Mouse mAb
PTM-168
ApplicationsImmunoFluorescence, Western Blot, ImmunoCytoChemistry
Product group Antibodies
ReactivityHuman, Mouse, Rat
Overview
- SupplierPTM BIO
- Product NameAnti-Acetyl-Histone H3 (Lys4) Mouse mAb
- Delivery Days Customer5
- ApplicationsImmunoFluorescence, Western Blot, ImmunoCytoChemistry
- Applications SupplierWB, ICC/IF
- Category SupplierAntibody
- CertificationResearch Use Only
- ClonalityMonoclonal
- Clone ID10G1
- ConjugateUnconjugated
- HostMouse
- IsotypeIgG
- Protein IDP68431
- Protein NameHistone H3.1
- 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
- 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
- Lin Huiyun, et al. 'Inhibition of Heat Shock-Induced H3K9ac Reduction Sensitizes Cancer Cells to Hyperthermia' International Journal of Biological Sciences (2023)Read more