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Anti-Butyryllysine Rabbit pAb

PTM-301
PTM BIO
ApplicationsWestern Blot
Product group Antibodies
ReactivityAll Species
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Overview

  • Supplier
    PTM BIO
  • Product Name
    Anti-Butyryllysine Rabbit pAb
  • Delivery Days Customer
    5
  • Antibody Specificity
    Anti-Butyryllysine Rabbit pAb detects proteins post-translationally modified by butyrylation on lysine residues. This pan antibody recognizes butyrylated lysine independent of its surrounding sequences.
  • Applications
    Western Blot
  • Applications Supplier
    WB
  • Category Supplier
    Antibody
  • Certification
    Research Use Only
  • Clonality
    Polyclonal
  • Conjugate
    Unconjugated
  • Host
    Rabbit
  • Isotype
    IgG
  • Scientific Description
    Butyrylation of lysine, structurally similar to lysine acetylation and lysine propionylation, is a newly identified reversible modification controlling protein activity. With integrated proteomic approaches and biochemistry analysis, lysine butyrylation are widely distributed in wide ranges of prokaryotic and eukaryotic histones and non-histone substrates. Lysine butyrylation may play a vital role in the regulation of transcriptional regulation, tumorigenesis, chromatin dynamics, and plasticity.
  • Shelf life instruction
    Stable for 12 months from date of receipt/reconstitution.
  • Reactivity
    All Species
  • Reactivity Supplier
    All
  • Reactivity Supplier Note
    Protein A and immunogen affinity purified
  • Storage Instruction
    Store at -20°C. Avoid freeze/thaw cycles.
  • UNSPSC
    12352203

References

  • Yi Fang, et al. 'Histone crotonylation promotes mesoendodermal commitment of human embryonic stem cells' Cell Stem Cell (2021)
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  • Gregory R. Wagner, et al. 'A Class of Reactive Acyl-CoA Species Reveals the Non-enzymatic Origins of Protein Acylation' Cell Metabolism (2017)
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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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  • Smestad John, et al. 'Protein Hyperacylation Links Mitochondrial Dysfunction with Nuclear Organization' MOLECULAR CELL (2020)
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  • Dang Lin, et al. 'Nuclear Condensation of CDYL Links Histone Crotonylation and Cystogenesis in Autosomal Dominant Polycystic Kidney Disease' JOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY (2022)
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  • Lu Yue, et al. 'Dynamics and functional interplay of histone lysine butyrylation, crotonylation, and acetylation in rice under starvation and submergence' GENOME BIOLOGY (2018)
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  • Simithy Johayra, et al. 'Characterization of histone acylations links chromatin modifications with metabolism' Nature Communications (2017)
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  • Aditya Bhattacharya, et al. 'Butyrylation Meets Adipogenesis-Probed by a p300-Catalyzed Acylation-Specific Small Molecule Inhibitor: Implication in Anti-obesity Therapy' JOURNAL OF MEDICINAL CHEMISTRY (2022)
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  • Yipeng Du, et al. 'Lysine Malonylation Is Elevated in Type 2 Diabetic Mouse Models and Enriched in Metabolic Associated Proteins *' MOLECULAR & CELLULAR PROTEOMICS (2014)
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  • Jun-Yu Xu, et al. 'Protein Acylation is a General Regulatory Mechanism in Biosynthetic Pathway of Acyl-CoA-Derived Natural Products' Cell Chemical Biology (2018)
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