UHRF1 Antibody – Rabbit Polyclonal

Polyclonal

Rabbit IgG

Rabbit

Human, Mouse, Rat

Liquid. Rabbit IgG in phosphate buffered saline, pH7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin

1mg/ml (lot specific)

UHRF1 Antibody detects endogenous levels of total UHRF1.
Tissue Specificity: Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer.

Store at -20 degree C. Stable for 12 months from date of receipt.

Observed Molecular Weight The band size is ~90kDa

Chromosome: 19; NC_000019.9 (4909510..4962165). Location: 19p13.3

607990

ModBase 3D Structure for Q96T88

Manufactured in a lab with traceable raw materials manufactured on site. Coordinated product portfolio of antibodies, pairs, conjugates, recombinant proteins, and immunoassay materials available, please inquire.

A synthesized peptide derived from human UHRF1.

Unconjugated

Fab fragment

Phosphorylation at Ser-298 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome.Ubiquitinated; which leads to proteasomal degradation. Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation. Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents interaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage.

Interacts with DNMT3A and DNMT3B (By similarity). Interacts with DNMT1; the interaction is direct. Interacts with USP7; leading to its deubiquitination. Interacts with histone H3. Interacts with HDAC1, but not with HDAC2. Interacts with UHRF1BP1. Interacts with PML. Interacts with EHMT2. Binds hemimethylated CpG containing oligonucleotides.

The tudor-like regions specifically recognize and bind histone H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3). The tudor-like regions simultaneously recognizes H3K9me3 through a conserved aromatic cage in the first tudor-like subdomain and unmodified H3K4 (H3K4me0) within a groove between the tandem subdomains (PubMed:21489993, PubMed:21777816 and PubMed:22100450). The linker region plays a role in the formation of a histone H3-binding hole between the reader modules formed by the tudor-like regions and the PHD-type zinc finger by making extended contacts with the tandem tudor-like regions (PubMed:22837395).The YDG domain (also named SRA domain) specifically recognizes and binds hemimethylated DNA at replication forks (DNA that is only methylated on the mother strand of replicating DNA) (PubMed:17673620). It contains a binding pocket that accommodates the 5-methylcytosine that is flipped out of the duplex DNA. 2 specialized loops reach through the resulting gap in the DNA from both the major and the minor grooves to read the other 3 bases of the CpG duplex. The major groove loop confers both specificity for the CpG dinucleotide and discrimination against methylation of deoxycytidine of the complementary strand (PubMed:18772889). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC) (PubMed:21731699).The RING finger is required for ubiquitin ligase activity.

Nucleus.
Note: Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions.

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