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Anti-Acetyl-Histone H3 (Lys14) Mouse mAb

PTM-157
PTM BIO
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityHuman, Mouse, Rat
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Overview

  • Supplier
    PTM BIO
  • Product Name
    Anti-Acetyl-Histone H3 (Lys14) Mouse mAb
  • Delivery Days Customer
    5
  • Applications
    ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry, ImmunoHistoChemistry Paraffin
  • Applications Supplier
    WB, IHC-P, ICC/IF, IP, ChIP
  • Category Supplier
    Antibody
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    1A4
  • Conjugate
    Unconjugated
  • Host
    Mouse
  • Isotype
    IgG
  • Protein IDP68431
  • Protein Name
    Histone H3.1
  • Scientific Description
    Histone 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 instruction
    Stable for 12 months from date of receipt/reconstitution.
  • Reactivity
    Human, Mouse, Rat
  • Reactivity Supplier
    Human, Mouse, Rat
  • Reactivity Supplier Note
    Protein G and immunogen affinity purified
  • Storage Instruction
    Store at -20°C. Avoid freeze/thaw cycles.
  • UNSPSC
    12352203

References

  • Pu Chen, et al. 'An Integrated Approach for Combinatorial Readout of Dual Histone Modifications by Epigenetic Tandem Domains' ANALYTICAL CHEMISTRY (2020)
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  • Shasha Shi, et al. 'Competitive Inhibition of Lysine Acetyltransferase 2B by a Small Motif of the Adenoviral Oncoprotein E1A *' JOURNAL OF BIOLOGICAL CHEMISTRY (2016)
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  • Zhang Ning, et al. 'BcRPD3-Mediated Histone Deacetylation Is Involved in Growth and Pathogenicity of Botrytis cinerea' Frontiers in Microbiology (2020)
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  • Lan Huahui, et al. 'The Aspergillus flavus Histone Acetyltransferase AflGcnE Regulates Morphogenesis, Aflatoxin Biosynthesis, and Pathogenicity' Frontiers in Microbiology (2016)
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  • Xia Liu, et al. 'Human borna disease virus infection impacts host proteome and histone lysine acetylation in human oligodendroglia cells' VIROLOGY (2014)
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  • Qiangzhen Yang, et al. 'Cadmium inhibits lysine acetylation and succinylation inducing testicular injury of mouse during development' TOXICOLOGY LETTERS (2018)
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  • Guan Haipeng, et al. 'Diverse modes of H3K36me3-guided nucleosomal deacetylation by Rpd3S' NATURE (2023)
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  • Bing Zhou, et al. 'Amelioration of nonalcoholic fatty liver disease by inhibiting the deubiquitylating enzyme RPN11' Cell Metabolism (2024)
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