Anti-Acetyl-Histone H4 (Lys12) Rabbit mAb
PTM-121RM
ApplicationsWestern Blot, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityHuman, Mouse, Rat
Overview
- SupplierPTM BIO
- Product NameAnti-Acetyl-Histone H4 (Lys12) Rabbit mAb
- Delivery Days Customer5
- Antibody SpecificityAnti-Acetyl-Histone H4 (Lys12) Rabbit mAb detects histone H4 only when it is acetylated at Lys12. This antibody has been shown to selectively recognize acetylated H4 peptide at Lys12, but not the structurally similar crotonylated, butyrylated, propionylated, bèta-hydroxybutyrylated, or 2-hydroxyisobutyrylated H4 peptide at Lys12.
- ApplicationsWestern Blot, ImmunoHistoChemistry Paraffin
- Applications SupplierWB, IHC-P
- Category SupplierAntibody
- CertificationResearch Use Only
- ClonalityMonoclonal
- Clone ID11-H1L2
- ConjugateUnconjugated
- HostRabbit
- IsotypeIgG
- Protein IDP62805
- Protein NameHistone H4
- 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 purified
- Storage InstructionStore at -20°C. Avoid freeze/thaw cycles.
- UNSPSC12352203