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Anti-Human UBR5 Polyclonal Antibody (HC972014)

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Overview
Catalog No.HC972014
Description
Anti-Human UBR5 Polyclonal Antibody (HC972014) is a rabbit polyclonal antibody detecting UBR5. Suitable for Human, Mouse, and Rat.
Highlights
  • Multi-Species — Cross-reactive for translational research.
Species reactivityHuman, Mouse, Rat
ApplicationsELISA, IHC, WB
Host speciesRabbit
IsotypeIgG
Clonality Polyclonal
Immunogen E. coli - derived recombinant Human UBR5 (Pro640-Ala870).
Target E3 ubiquitin-protein ligase UBR5, E3 ubiquitin-protein ligase, HECT domain-containing 1, EC:2.3.2.26, EDD, EDD1, HYD, Hyperplastic discs protein homolog, KIAA0896, Progestin-induced protein, UBR5, hHYD
Endotoxin level Please contact with the lab for this information.
Purification Purified by antigen affinity column.
Accession O95071
Form Liquid
Storage buffer 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Product Usage Information
Application Dilution
ELISA 1:5000-1:20000
IHC 1:50-1:500
WB 1:500-1:2000
Background

E3 ubiquitin-protein ligase UBR5 is a ~309 kDa protein. E3 ubiquitin-protein ligase involved in different protein quality control pathways in the cytoplasm and nucleus. Mainly acts as a ubiquitin chain elongator that extends pre-ubiquitinated substrates. Component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation. Recognizes type-1 N-degrons, containing positively charged amino acids (Arg, Lys and His). Together with UBR4, part of a cytoplasm protein quality control pathway that prevents protein aggregation by catalyzing assembly of heterotypic 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on aggregated proteins, leading to substrate recognition by the segregase p97/VCP and degradation by the proteasome: UBR5 is probably branching multiple 'Lys-48'-linked chains of substrates initially modified with mixed conjugates by UBR4.

1. Yau, RG. et al. (2017) Cell 171, 918-933.e20. PMID: 29033132
2. Schukur, L. et al. (2020) Scientific reports 10, 20044. PMID: 33208877
3. Tsai, JM. et al. (2023) Molecular cell 83, 2753-2767.e10. PMID: 37478846
4. Mark, KG. et al. (2023) Cell 186, 3460-3475.e23. PMID: 37478862
5. Hodáková, Z. et al. (2023) The EMBO journal 42, e113348. PMID: 37409633
6. Ohtake, F. et al. (2018) Proceedings of the National Academy of Sciences of the United States of America 115, E1401-E1408. PMID: 29378950
10. Jiang, W. et al. (2011) Molecular cell 43, 33-44. PMID: 21726808
Note For research use only
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