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Anti-L-Lactyllysine Antibody Conjugated Agarose Beads

PTM-1404
PTM BIO
ReactivityAll Species
Product group Antibodies
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Overview

  • Supplier
    PTM BIO
  • Product Name
    Anti-L-Lactyllysine Antibody Conjugated Agarose Beads
  • Delivery Days Customer
    5
  • Antibody Specificity
    With the immobilization of highly specific Anti-L-Lactyllysine Antibodies, the Anti-L-Lactyllysine Antibody Conjugated Agarose Beads selectively capture peptides/proteins bearing L-lactyllysine residues, but do 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 lactylation.
  • Applications Supplier
    IAP
  • Category Supplier
    Antibody
  • Certification
    Research Use Only
  • Clonality
    Mix
  • Conjugate
    Agarose
  • Host
    Rabbit
  • Isotype
    IgG
  • Scientific Description
    Lactate, previously recognized solely as an energy source and metabolic byproduct, has now emerged as a crucial player in cancer biology, especially within the scope of the Warburg effect and its intricate interplay with various cellular processes, including angiogenesis, hypoxia, polarization of macrophages, and T cell activation. Recent investigations have unveiled an unprecedented function of lactate in the realm of histone modification, specifically through lysine L-lactylation, which exerts regulatory control over gene expression. The extent and dynamics of this modification are highly reliant on lactate levels within the cellular microenvironment and can be modulated through the introduction of extracellular lactate in cultured cells or the stimulation of intracellular glycolysis. The acetyltransferase p300 is responsible for introducing lysine L-lactylation, while Class I histone deacetylases (HDAC 1-3) have been identified as an eraser of the lactylation marks on histones.
  • 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

  • Dong Hanyang, et al. 'YiaC and CobB regulate lysine lactylation in Escherichia coli' Nature Communications (2022)
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  • Yinggai Song, et al. 'Post-translational changes in Phialophora verrucosa via lysine lactylation during prolonged presence in a patient with a CARD9-related immune disorder' Frontiers in Immunology (2022)
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  • Deqi Yin, et al. 'Protein Lactylation and Metabolic Regulation of the Zoonotic Parasite Toxoplasma gondii' GENOMICS PROTEOMICS & BIOINFORMATICS (2022)
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  • Zhao Wei, et al. 'Systematic identification of the lysine lactylation in the protozoan parasite Toxoplasma gondii' Parasites & Vectors (2022)
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  • Zhang Naijin, et al. 'alfa-myosin heavy chain lactylation maintains sarcomeric structure and function and alleviates the development of heart failure' CELL RESEARCH (2023)
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  • Gao Ruxin, et al. 'Mitochondrial pyruvate carrier 1 regulates fatty acid synthase lactylation and mediates treatment of nonalcoholic fatty liver disease' HEPATOLOGY (2023)
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  • Gaoxiang Cao, et al. 'cKMT1 is a new lysine methyltransferase that methylates the ferredoxin-NADP(+) oxidoreductase (FNR) and regulates energy transfer in cyanobacteria' MOLECULAR & CELLULAR PROTEOMICS (2023)
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  • Jiao Wang, et al. 'Novel Insight of Nitrogen Deprivation Affected Lipid Accumulation by Genome-Wide Lactylation in Nannochloropsis oceanica' JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY (2023)
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  • Qibin Wu, et al. 'Deciphering the Atlas of Post-Translational Modification in Sugarcane' JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY (2023)
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  • Song Fan, et al. 'Lactylome Analyses Suggest Systematic Lysine-Lactylated Substrates in Oral Squamous Cell Carcinoma Under Normoxia and Hypoxia' iScience (2023)
    Read more