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Mouse Monoclonal Anti-UHRF1 antibody (STJ99024)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-2000; ELISA 1:10000-20000
Recommended protocols: check protocols
Click or hover above images to see image description for Anti-UHRF1 antibody.
Check alternative names for the antibodyExpand
|Ac2-121 antibody|MGC138707 antibody|NP95 antibody|Nuclear phosphoprotein, 95-KD antibody|Nuclear protein 95 antibody|Nuclear zinc finger protein Np95 antibody|RING finger protein 106 antibody|RNF106 antibody|Transcription factor ICBP90 antibody|Ubiquitin like containing PHD and RING finger domains protein 1 antibody|Ubiquitin like PHD and RING finger domain containing protein 1 antibody|Ubiquitin-like PHD and RING finger domain-containing protein 1 antibody|Ubiquitin-like protein containing PHD and RING finger domains 1 antibody|Ubiquitin-like with PHD and ring finger domains 1 antibody|Ubiquitin-like, containing PHD and RING finger domains, 1 antibody|Ubiquitin-like-containing PHD and RING finger domains protein 1 antibody|UHRF1 antibody|UHRF1_HUMAN antibody|Anti-UHRF1 antibody [EPR18803-11] (ab213223)
SCBT cat No:
|Catalogue No.|| |
Anti-UHRF1 antibody detects endogenous levels of UHRF1 and does not cross-react with related proteins.
Purified recombinant human UHRF1 protein fragments expressed in E.coil.
|Recommended dilution|| |
WB 1:500-2000; ELISA 1:10000-20000
|Molecular weight|| |
Anti-UHRF1 antibody was tube-contained in liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Anti-UHRF1 antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Ac2-121 antibody, MGC138707 antibody, NP95 antibody, Nuclear phosphoprotein, 95-KD antibody, Nuclear protein 95 antibody, Nuclear zinc finger protein Np95 antibody, RING finger protein 106 antibody, RNF106 antibody, Transcription factor ICBP90 antibody, Ubiquitin like containing PHD and RING finger domains protein 1 antibody, Ubiquitin like PHD and RING finger domain containing protein 1 antibody, Ubiquitin-like PHD and RING finger domain-containing protein 1 antibody, Ubiquitin-like protein containing PHD and RING finger domains 1 antibody, Ubiquitin-like with PHD and ring finger domains 1 antibody, Ubiquitin-like, containing PHD and RING finger domains, 1 antibody, Ubiquitin-like-containing PHD and RING finger domains protein 1 antibody, UHRF1 antibody, UHRF1_HUMAN antibody
|Database links|| |
|Protein function|| |
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, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at ‘Lys-9’ (H3K9me3) and unmethylated at ‘Arg-2’ (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair. .
|Protein tissue specificity|| |
Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer. .
|Involvement in disease|| |
Note=Defects in UHRF1 may be a cause of cancers. Overexpressed in many different forms of human cancers, including bladder, breast, cervical, colorectal and prostate cancers, as well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Expression is associated with a poor prognosis in patients with various cancers, suggesting that it participates in cancer progression.
|Protein sequence and domain|| |
Contains 1 PHD-type zinc finger. ; Contains 1 RING-type zinc finger. ; Contains 1 ubiquitin-like domain. ; Contains 1 YDG domain. 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.
|Protein post-translational modifications|| |
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 intereaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage. .
|Protein cellular localization|| |
Nucleus . Note=Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions.
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St John’s Laboratory Ltd.
|Product type|| |
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