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Encompassing Amino Acids: 108-286
Applications: Useful for protein binding assays, screening inhibitors, and selectivity profiling.
Background: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, it also plays a key role in chromatin modification. The protein binds to specific DNA sequences, and recruits a histone deacetylase to regulate gene expression. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. May be involved in DNA repair. Its expression peaks at late G1 phase and continues during G2 and M phases of the cell cycle. It plays a major role in the G1/S transition by regulating topoisomerase IIalpha and retinoblastoma gene expression, and functions in the p53-dependent DNA damage checkpoint. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications.
Description: Tandem Tudor Domain region (a.a. 108-286) of human ubiquitin-like with PHD and ring finger domains 1 (UHRF1), GenBank Accession #NM_001048201, with N-terminal His-tag, MW = 21.6 kDa, expressed in an E. coli cell expression system.
Format: Aqueous buffer solution
Formulation: 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 10 mM β-mercaptoethanol, 250 mM imidazole, and 20% glycerol
Genbank: NM_001048201
Storage Stability: At least 6 months at -80°C.
Tags: N-terminal His-tag
Uniprot: Q96T88
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. Kofunato, Y., et al., Oncol Rep.
2012 Dec; 28(6):1997-2002.
2. Jazirehi, A.R., et al., Epigenomics.
2012 Jun;4(3):251-252.Application Reference(s):
De Vos, M., et al. Poly(ADP-ribose) polymerase 1 (PARP1) associates with E3 ubiquitin-protein ligase UHRF1 and modulates UHRF1 biological functions. J Biol Chem. 2014 Jun 6;289(23):16223-38. (2014)
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