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Anti-Propionyllysine Rabbit pAb

PTM-201
PTM BIO
ApplicationsWestern Blot
Product group Antibodies
ReactivityAll Species
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Overview

  • Supplier
    PTM BIO
  • Product Name
    Anti-Propionyllysine Rabbit pAb
  • Delivery Days Customer
    5
  • Antibody Specificity
    Anti- Propionyllysine Rabbit pAb detects proteins with propionylated lysine residues. This pan antibody recognizes propionylated 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
    Propionylation of lysine, structurally similar to lysine acetylation, is a newly identified reversible modification controlling protein activity. The reversible lysine propionylation has been well demonstrated in both prokaryotes and eukaryotes in wide ranges of proteins including histones and non-histone substrates, such as p53. It is speculated that lysine propionylation plays a vital role in the regulation of multiple cellular processes including chromatin dynamics, plasticity, and DNA transcriptional regulation by sharing same regulative enzymes with lysine acetylation or with its unique regulative enzymes.
  • 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

  • Sophie Trefely, et al. 'Quantitative subcellular acyl-CoA analysis reveals distinct nuclear metabolism and isoleucine-dependent histone propionylation' MOLECULAR CELL (2021)
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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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  • Kezhi Yan, et al. 'Deficient histone H3 propionylation by BRPF1-KAT6 complexes in neurodevelopmental disorders and cancer' Science Advances (2020)
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  • Fukuda Masatoshi, et al. 'SIRT7 has a critical role in bone formation by regulating lysine acylation of SP7/Osterix' Nature Communications (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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  • Liu Xiaoguang, et al. 'MOF as an evolutionarily conserved histone crotonyltransferase and transcriptional activation by histone acetyltransferase-deficient and crotonyltransferase-competent CBP/p300' Cell Discovery (2017)
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  • Sydney P Thomas, et al. 'Short-chain fatty acids activate acetyltransferase p300' eLife (2021)
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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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