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Anti-Propionyllysine Antibody Conjugated Agarose Beads

PTM-202
PTM BIO
ReactivityAll Species
Product group Antibodies
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Overview

  • Supplier
    PTM BIO
  • Product Name
    Anti-Propionyllysine Antibody Conjugated Agarose Beads
  • Delivery Days Customer
    5
  • Antibody Specificity
    With the immobilization of highly specific anti-propionyllysine antibody, the Anti-Propionyllysine Antibody Conjugated Agarose Beads selectively capture peptides/proteins bearing propionyllysine residues, but does not cross-react with the peptides/proteins bearing other structurally similar modified residues. This product has been well utilized to affinity purify peptides for global proteomic screening of lysine propionylation.
  • Applications Supplier
    IAP
  • Category Supplier
    Antibody
  • Certification
    Research Use Only
  • Clonality
    Mix
  • Clone ID
    PA-024-15
  • Conjugate
    Agarose
  • 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.
  • Reactivity
    All Species
  • Reactivity Supplier
    All
  • Storage Instruction
    Store at -20°C. Avoid freeze/thaw cycles.
  • UNSPSC
    12352203

References

  • Yanyan Xu, et al. 'Branched-Chain Amino Acid Catabolism Promotes Thrombosis Risk by Enhancing Tropomodulin-3 Propionylation in Platelets' CIRCULATION (2020)
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  • Xiaohuang Lin, et al. 'Characterization of Lysine Monomethylome and Methyltransferase in Model Cyanobacterium Synechocystis sp. PCC 6803' GENOMICS PROTEOMICS & BIOINFORMATICS (2020)
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  • Liu Xin, et al. 'Structural and Functional Insights into a Lysine Deacylase in the Cyanobacterium Synechococcus sp. PCC 7002' PLANT PHYSIOLOGY (2020)
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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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  • Cluntun Ahmad A., et al. 'The rate of glycolysis quantitatively mediates specific histone acetylation sites' Cancer & Metabolism (2015)
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  • Qianwen Ding, et al. 'Propionate induces intestinal oxidative stress via Sod2 propionylation in zebrafish' iScience (2021)
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  • Ding Qian-wen, et al. 'Propionate Induces Intestinal Oxidative Stress Via SOD2 Propionylation' iScience (2021)
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  • Tian-Yun Wang, et al. 'Crosstalk among the proteome, lysine phosphorylation, and acetylation in romidepsin-treated colon cancer cells' Oncotarget (2016)
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  • Xu Xingye, et al. 'Proteome-Wide Identification of Lysine Propionylation in the Conidial and Mycelial Stages of Trichophyton rubrum' Frontiers in Microbiology (2019)
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  • Mingya Zhang, et al. 'Global landscape of lysine acylomes in Bacillus subtilis' Journal of Proteomics (2022)
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