Recombinant Human USP51 protein (Tagged) is a Human Fragment protein, in the 227 to 711 aa range, expressed in Baculovirus infected Sf9, with >80% purity and suitable for SDS-PAGE.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Specifically deubiquitinates 'Lys-14' (H2AK13Ub) and 'Lys-16'(H2AK15Ub) of histone H2A regulating the DNA damage response at double-strand breaks (DSBs) (PubMed:27083998, PubMed:33022275). USP51 is recruited to chromatin after DNA damage and regulates the dynamic assembly/disassembly of TP53BP1 and BRCA1. Functions in DNA double-strand break repair also by mediating the deubiquitination and subsequent stabilization of DGCR8, leading to the recruitment of DGCR8 binding partners to double strand breaks such as RNF168 or MDC1 (PubMed:34188037). In addition, promotes the deubiquitination and stabilization of the transcriptional repressor ZEB1 (PubMed:29119051).
Ubiquitin carboxyl-terminal hydrolase 51, Deubiquitinating enzyme 51, Ubiquitin thioesterase 51, Ubiquitin-specific-processing protease 51, USP51
Recombinant Human USP51 protein (Tagged) is a Human Fragment protein, in the 227 to 711 aa range, expressed in Baculovirus infected Sf9, with >80% purity and suitable for SDS-PAGE.
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF
Affinity purified.
Specifically deubiquitinates 'Lys-14' (H2AK13Ub) and 'Lys-16'(H2AK15Ub) of histone H2A regulating the DNA damage response at double-strand breaks (DSBs) (PubMed:27083998, PubMed:33022275). USP51 is recruited to chromatin after DNA damage and regulates the dynamic assembly/disassembly of TP53BP1 and BRCA1. Functions in DNA double-strand break repair also by mediating the deubiquitination and subsequent stabilization of DGCR8, leading to the recruitment of DGCR8 binding partners to double strand breaks such as RNF168 or MDC1 (PubMed:34188037). In addition, promotes the deubiquitination and stabilization of the transcriptional repressor ZEB1 (PubMed:29119051).
Belongs to the peptidase C19 family.
USP51 also known as Ubiquitin Specific Peptidase 51 functions as a deubiquitinating enzyme. It has a mass of approximately 96 kDa. This protein regulates the ubiquitin-proteasome pathway by removing ubiquitin molecules from ubiquitinated substrates. USP51 gets predominantly expressed in tissues such as the testis and the brain. Through its enzymatic activity USP51 maintains protein homeostasis which is essential for various cellular processes.
Ubiquitin Specific Peptidase 51 plays a role in DNA damage repair and cell cycle regulation. It forms part of multiprotein complexes where it collaborates with components like BRCA1 and RAD51 to maintain genomic stability. This activity ensures the cell's integrity and function. Moreover USP51 interacts with other deubiquitinating enzymes indicating a coordinated action in cellular maintenance.
The activity of USP51 integrates into the DNA damage response and cell cycle checkpoints. It contributes to the homologous recombination repair pathway alongside proteins like RAD51 ensuring proper repair of DNA double-strand breaks. Additionally USP51 influences the Wnt signaling pathway where it affects the stability of proteins like β-catenin which are integral to cell proliferation and differentiation.
The regulation by USP51 impacts cancer development and neurodegenerative disorders. Abnormal expression or mutation of USP51 has links to breast cancer due to its influence on the BRCA1-associated DNA repair pathway. In neurodegenerative diseases like Alzheimer's USP51 may alter protein aggregation through its effect on ubiquitin pathways potentially intersecting with proteins such as tau. These connections present USP51 as a significant target for therapeutic research and development.
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SDS-PAGE analysis of ab269125.
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