Bio-Connect

Anti-Diglycyl-Lysine Antibody Conjugated Agarose Beads

PTM-1104
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-Diglycyl-Lysine Antibody Conjugated Agarose Beads
  • Delivery Days Customer
    5
  • Antibody Specificity
    With the immobilization of highly specific Anti-Diglycyl-Lysine Antibody, the Anti-Diglycyl-Lysine Antibody Conjugated Agarose Beads selectively capture peptides/proteins bearing K-ɛ-G-G residues, which are remnants of ubiquitin left in protein substrates after trypsin digestion or remnants of SUMO after alfa-lytic protease WaLP digestion. This product has been well utilized to affinity purify peptides for global proteomic screening of ubiquitination and SUMOylation.
  • Applications Supplier
    IAP
  • Category Supplier
    Antibody
  • Certification
    Research Use Only
  • Clonality
    Mix
  • Conjugate
    Agarose
  • Isotype
    IgG
  • Scientific Description
    Ubiquitin (Ub) is a highly conserved 76-amino acid protein that plays a critical role in regulating cellular processes. By covalently attaching to target proteins through a three-step process involving Ub-activating (E1), Ub-conjugating (E2), and Ub-ligating (E3) enzymes, ubiquitination marks the target proteins for proteasomal degradation and controls the activity of many signal transduction pathways. Ubiquitination occurs through the formation of an isopeptide bond between its C-terminus and a lysine residue in the target protein. This process can occur either as a monomer (monoubiquitin) or as a polymer (polyubiquitin chains), where the C-terminus of a chain extending ubiquitin becomes linked to the N-terminus (M1) or one of seven Lys residues (Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, and Lys63) within a substrate-bound ubiquitin molecule.Members of the ubiquitin-like protein family, such as small ubiquitin-related modifier 1, 2 and 3 (SUMO1, 2 and 3), have functions similar to ubiquitin, whereby they bind to target proteins as part of a post-translational modification system. SUMO can be covalently attached to proteins as a monomer or a lysine-linked polymer via an isopeptide bond. SUMO-1 regulates nuclear trafficking, formation of subnuclear structures, transcriptional activity, and protein stability by being conjugated to proteins such as RanGAP, PML, p53 and IkappaB-alfa. SUMO-2/-3 forms poly-(SUMO) chains and is conjugated to topoisomerase II and APP, regulating chromosomal segregation and cellular responses to environmental stress.
  • 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

  • Yan Lingjie, et al. 'SENP1 prevents steatohepatitis by suppressing RIPK1-driven apoptosis and inflammation' Nature Communications (2022)
    Read more
  • Yang Lu, et al. 'Ubiquitylome study identifies increased histone 2A ubiquitylation as an evolutionarily conserved aging biomarker' Nature Communications (2019)
    Read more
  • Yuan Sen, et al. 'Global analysis of HBV-mediated host proteome and ubiquitylome change in HepG2.2.15 human hepatoblastoma cell line' Cell and Bioscience (2021)
    Read more
  • Liya Zhu, et al. 'Ubiquitinome Profiling Reveals the Landscape of Ubiquitination Regulation in Rice Young Panicles' GENOMICS PROTEOMICS & BIOINFORMATICS (2020)
    Read more
  • Xu Dacai, et al. 'Serpinc1 Acts as a Tumor Suppressor in Hepatocellular Carcinoma Through Inducing Apoptosis and Blocking Macrophage Polarization in an Ubiquitin-Proteasome Manner' Frontiers in Oncology (2021)
    Read more
  • Wei Lan, et al. 'Establishment of a Landscape of UPL5-Ubiquitinated on Multiple Subcellular Components of Leaf Senescence Cell in Arabidopsis' INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2022)
    Read more
  • Nathalie Berger, et al. 'Root Membrane Ubiquitinome under Short-Term Osmotic Stress' INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2022)
    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
  • Yu Liu, et al. 'Comprehensive Analysis of Ubiquitome Changes in Nicotiana benthamiana after Rice Stripe Virus Infection' Viruses-Basel (2022)
    Read more
  • Haichao Hu, et al. 'Central Role of Ubiquitination in Wheat Response to CWMV Infection' Viruses-Basel (2022)
    Read more