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Anti-Acetyllysine Mouse mAb

PTM-101
PTM BIO
ApplicationsWestern Blot, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityAll Species
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Overview

  • Supplier
    PTM BIO
  • Product Name
    Anti-Acetyllysine Mouse mAb
  • Delivery Days Customer
    5
  • Antibody Specificity
    Anti-Acetyllysine Mouse mAb detects proteins with acetylated lysine residues. This pan antibody recognizes acetylated lysine independent of its surrounding sequences.
  • Applications
    Western Blot, ImmunoHistoChemistry Paraffin
  • Applications Supplier
    WB, IHC-P
  • Category Supplier
    Antibody
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    Kac-01
  • Conjugate
    Unconjugated
  • Host
    Mouse
  • Isotype
    IgG
  • Scientific Description
    The 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 instruction
    Stable for 12 months from date of receipt/reconstitution.
  • Reactivity
    All Species
  • Reactivity Supplier
    All
  • Reactivity Supplier Note
    Protein G and immunogen affinity purified
  • Storage Instruction
    Store at -20°C. Avoid freeze/thaw cycles.
  • UNSPSC
    12352203

References

  • Zhang Di, et al. 'Metabolic regulation of gene expression by histone lactylation' NATURE (2019)
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  • Ren Xiangle, et al. 'Histone benzoylation serves as an epigenetic mark for DPF and YEATS family proteins' NUCLEIC ACIDS RESEARCH (2020)
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  • Zhu Zhesi, et al. 'Identification of lysine isobutyrylation as a new histone modification mark' NUCLEIC ACIDS RESEARCH (2020)
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  • Huang He, et al. 'Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway' CELL RESEARCH (2017)
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  • 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)
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  • Carlos Moreno-Yruela, et al. 'Class I histone deacetylases (HDAC1–3) are histone lysine delactylases' Science Advances (2022)
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  • He Huang, et al. 'p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis' MOLECULAR CELL (2018)
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  • Liu Zuojun, et al. 'SIRT7 couples light-driven body temperature cues to hepatic circadian phase coherence and gluconeogenesis' Nature Metabolism (2019)
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  • Dai Lunzhi, et al. 'Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark' Nature Chemical Biology (2014)
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  • Yang Tangpo, et al. 'Photo-lysine captures proteins that bind lysine post-translational modifications' Nature Chemical Biology (2015)
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