Anti-Acetyllysine Mouse mAb
PTM-101
ApplicationsWestern Blot, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityAll Species
Overview
- SupplierPTM BIO
- Product NameAnti-Acetyllysine Mouse mAb
- Delivery Days Customer5
- Antibody SpecificityAnti-Acetyllysine Mouse mAb detects proteins with acetylated lysine residues. This pan antibody recognizes acetylated lysine independent of its surrounding sequences.
- ApplicationsWestern Blot, ImmunoHistoChemistry Paraffin
- Applications SupplierWB, IHC-P
- Category SupplierAntibody
- CertificationResearch Use Only
- ClonalityMonoclonal
- Clone IDKac-01
- ConjugateUnconjugated
- HostMouse
- IsotypeIgG
- Scientific DescriptionThe reversible lysine acetylation of histones and non-histone proteins is a crucial post-translational modification that regulates diverse cellular processes, including chromatin dynamics, gene expression, cell cycle progression, apoptosis, differentiation, DNA replication, DNA repair, nuclear import, and neuronal repression. More than 20 acetyltransferases and 18 histone deacetylases (HDACs) have been identified, but the mechanisms governing substrate selection and site specificity of these enzymes remain unclear. Dysregulation of protein acetylation has been implicated in the development of cancers and other diseases, and HDACs have become likely targets for anti-cancer drugs.
- Shelf life instructionStable for 12 months from date of receipt/reconstitution.
- ReactivityAll Species
- Reactivity SupplierAll
- Reactivity Supplier NoteProtein G and immunogen affinity purified
- Storage InstructionStore at -20°C. Avoid freeze/thaw cycles.
- UNSPSC12352203
References
- Zhang Di, et al. 'Metabolic regulation of gene expression by histone lactylation' NATURE (2019)Read more
- Ren Xiangle, et al. 'Histone benzoylation serves as an epigenetic mark for DPF and YEATS family proteins' NUCLEIC ACIDS RESEARCH (2020)Read more
- Zhu Zhesi, et al. 'Identification of lysine isobutyrylation as a new histone modification mark' NUCLEIC ACIDS RESEARCH (2020)Read more
- Huang He, et al. 'Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway' CELL RESEARCH (2017)Read more
- Wei Wei, et al. 'Class I histone deacetylases are major histone decrotonylases: evidence for critical and broad function of histone crotonylation in transcription' CELL RESEARCH (2017)Read more
- Carlos Moreno-Yruela, et al. 'Class I histone deacetylases (HDAC1–3) are histone lysine delactylases' Science Advances (2022)Read more
- He Huang, et al. 'p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis' MOLECULAR CELL (2018)Read more
- Liu Zuojun, et al. 'SIRT7 couples light-driven body temperature cues to hepatic circadian phase coherence and gluconeogenesis' Nature Metabolism (2019)Read more
- Dai Lunzhi, et al. 'Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark' Nature Chemical Biology (2014)Read more
- Yang Tangpo, et al. 'Photo-lysine captures proteins that bind lysine post-translational modifications' Nature Chemical Biology (2015)Read more