Bio-Connect

Anti-2-Hydroxyisobutyryllysine Antibody Conjugated Agarose Beads

PTM-804
PTM BIO
ReactivityAll Species
Product group Antibodies
Sign in to order and to see your custom pricing.
Large volume orders?
Order with a bulk request

Overview

  • Supplier
    PTM BIO
  • Product Name
    Anti-2-Hydroxyisobutyryllysine Antibody Conjugated Agarose Beads
  • Delivery Days Customer
    5
  • Antibody Specificity
    With a mixture of high-quality rabbit- and mouse-derived anti-crotonyllysine antibodies cross-linked, this Anti-Phosphorylatedtyrosine Antibody Conjugated Agarose Beads present extraordinary capability to specifically capture peptides/proteins bearing crotonyllysine residues but do not cross-react with the peptides/proteins bearing structurally similar acetyllysine residues. This product has been well utilized to affinity purify peptides for global proteomic screening of lysine crotonylation.
  • Applications Supplier
    IAP
  • Category Supplier
    Antibody
  • Certification
    Research Use Only
  • Clonality
    Mix
  • Conjugate
    Agarose
  • Isotype
    IgG
  • Scientific Description
    Histones are subjected to a variety of enzyme catalyzed modifications, including acetylation, methylation, ubiquitylation, etc. 2-Hydroxyisobutyrylation of lysine is a newly identified reversible modification controlling chromosome structure and gene transcription. The reversible lysine 2-hydroxyisobutyrylation has been well demonstrated in eukaryotic histones from worm to human. The unique structure and genomic localization of histone lysine 2-hydroxyisobutyrylation suggest that it is mechanistically and functionally different from histone lysine acetylation.
  • 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

  • Zheng Lanlan, et al. 'Functional interplay of histone lysine 2-hydroxyisobutyrylation and acetylation in Arabidopsis under dark-induced starvation' NUCLEIC ACIDS RESEARCH (2021)
    Read more
  • Huang He, et al. 'Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway' CELL RESEARCH (2017)
    Read more
  • Dong Hanyang, et al. 'TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate transcription' Nature Chemical Biology (2021)
    Read more
  • Huang Jing, et al. '2-Hydroxyisobutyrylation on histone H4K8 is regulated by glucose homeostasis in Saccharomyces cerevisiae' PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2017)
    Read more
  • Xiaoyang Chen, et al. 'Comprehensive identification of lysine 2-hydroxyisobutyrylated proteins in Ustilaginoidea virens reveals the involvement of lysine 2-hydroxyisobutyrylation in fungal virulence' Journal of Integrative Plant Biology (2021)
    Read more
  • Zhang X, et al. 'Lysine Acylation Modification Landscape of Brucella abortus Proteome and its Virulent Proteins.' Frontiers in Cell and Developmental Biology (2022)
    Read more
  • Ning Wang, et al. 'Quantitative Proteomics Reveals the Role of Lysine 2-Hydroxyisobutyrylation Pathway Mediated by Tip60' Oxidative Medicine and Cellular Longevity (2022)
    Read more
  • Hailin Zheng, et al. 'Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in Candida albicans ; mSystems' mSystems (2021)
    Read more
  • Jianhua Wang, et al. 'Protein Modification Characteristics of the Malaria Parasite Plasmodium falciparum and the Infected Erythrocytes' MOLECULAR & CELLULAR PROTEOMICS (2020)
    Read more
  • Wenhe Zhu, et al. 'Global Lysine Acetylation and 2-Hydroxyisobutyrylation Profiling Reveals the Metabolism Conversion Mechanism in Giardia lamblia' MOLECULAR & CELLULAR PROTEOMICS (2021)
    Read more