More than 130 suppliers
ISO certified
In-house tech support
we Connect you
Bio-Connect
ProductsBack/Anti-Glutaryllysine Rabbit pAb

Anti-Glutaryllysine Rabbit pAb

PTM-1151
PTM BIO
ApplicationsWestern Blot
Product group Antibodies
ReactivityAll Species
Sign in to order and to see your custom pricing.
Large volume orders?
Order with a bulk request
More than 130 suppliers
ISO certified
In-house tech support

Overview

  • Supplier
    PTM BIO
  • Product Name
    Anti-Glutaryllysine Rabbit pAb
  • Delivery Days Customer
    5
  • Antibody Specificity
    Anti-Glutaryllysine Rabbit pAb detects proteins post-translationally modified by glutarylation on lysine residues. This pan antibody recognizes GL 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
    Lysine glutarylation is a histone post-translational modification (PTM) that has been recently identified through integrated proteomic approaches and elaborate biochemistry analyses. This modification has been shown to be evolutionarily conserved across multiple species of prokaryotes and eukaryotes, and is present in a wide range of proteins, including both histones and non-histone substrates. Lysine glutarylation is a PTM that is regulated by SIRT5 and nutrient availability, and it has been demonstrated to impact various metabolic processes and mitochondrial functions.
  • 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

  • Wang Yun-Qian, et al. 'Sirtuin5 contributes to colorectal carcinogenesis by enhancing glutaminolysis in a deglutarylation-dependent manner' Nature Communications (2018)
    Read more
  • Simithy Johayra, et al. 'Characterization of histone acylations links chromatin modifications with metabolism' Nature Communications (2017)
    Read more
  • Sushabhan Sadhukhan, et al. 'Metabolomics-assisted proteomics identifies succinylation and SIRT5 as important regulators of cardiac function' PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2016)
    Read more
  • Yang Xin, et al. 'SHMT2 Desuccinylation by SIRT5 Drives Cancer Cell ProliferationDesuccinylation of SHMT2 by SIRT5 Promotes Tumor Cell Growth' CANCER RESEARCH (2018)
    Read more
  • WenChao Gao, et al. 'Targeting oxidative pentose phosphate pathway prevents recurrence in mutant Kras colorectal carcinomas' PLOS BIOLOGY (2019)
    Read more
  • Jonathan B. Lin, et al. 'NAMPT-Mediated NAD+ Biosynthesis Is Essential for Vision In Mice' Cell Reports (2016)
    Read more
  • Lisha Zhou, et al. 'SIRT5 promotes IDH2 desuccinylation and G6PD deglutarylation to enhance cellular antioxidant defense' EMBO REPORTS (2016)
    Read more
  • Artem V. Artiukhov, et al. 'Phosphonate Inhibitors of Pyruvate Dehydrogenase Perturb Homeostasis of Amino Acids and Protein Succinylation in the Brain' INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2022)
    Read more
  • Yipeng Du, et al. 'SIRT5 deacylates metabolism-related proteins and attenuates hepatic steatosis in ob/ob mice' EBioMedicine (2018)
    Read more
  • Cheng Yi-min, et al. 'Lysine glutarylation in human sperm is associated with progressive motility' HUMAN REPRODUCTION (2019)
    Read more