Anti-K27-linkage Specific Ubiquitin / UBB / UBC, clone 31U80

Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol, 0.4-0.5mg/ml BSA. K27-linkage specific ubiquitin antibody detects ubiquitin chains linked through lysine 27, generated from ubiquitin encoded by the UBB and UBC genes. Ubiquitin is a small regulatory protein that is covalently attached to substrate proteins, marking them for degradation or altering their function. Ubiquitin chains can be linked through different lysines, with each linkage type conferring distinct signaling functions. K27-linkage specific ubiquitin antibody provides researchers with a highly selective reagent to study lysine 27 ubiquitination and its roles in signaling, DNA repair, and immunity.Unlike the well characterized K48 and K63 chains, lysine 27 linked ubiquitin chains are less abundant but play specialized roles. Research using K27-linkage specific ubiquitin antibody has shown that these chains regulate mitochondrial homeostasis, DNA damage repair, and innate immune signaling. By targeting proteins for specific fates, K27 chains contribute to non-proteolytic ubiquitin functions, highlighting the complexity of the ubiquitin code.In innate immunity, lysine 27 chains are involved in regulating antiviral signaling pathways such as RIG-I and MAVS. Studies with K27-linkage specific ubiquitin antibody have revealed that these chains promote activation of signaling complexes leading to interferon production. In DNA repair, K27 ubiquitin regulates assembly of repair factors at sites of damage. Dysregulation of K27 chains is linked to impaired genome stability and susceptibility to cancer.Because ubiquitin modifications are dynamic and context dependent, linkage-specific antibodies are essential for dissecting the ubiquitin code. K27-linkage specific ubiquitin antibody allows researchers to distinguish lysine 27 linkages from other ubiquitin chains, enabling studies of how different linkages integrate into signaling networks. This specificity is crucial for understanding how ubiquitination encodes information beyond protein degradation.K27-linkage specific ubiquitin antibody is applied in western blotting, immunoprecipitation, and immunofluorescence. Western blotting detects K27-linked chains in cellular extracts, immunoprecipitation isolates proteins modified with this linkage, and immunofluorescence reveals dynamic localization after stress or immune stimulation. These methods highlight its value in ubiquitin signaling research.By supplying validated K27-linkage specific ubiquitin antibody reagents, NSJ Bioreagents supports research into ubiquitin signaling, DNA repair, and immunity. Detection of lysine 27 ubiquitin chains provides a critical tool to decode how ubiquitin modifications regulate cellular processes.