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UHRF1 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
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- BACKGROUND
| Primary Accession | Q96T88 |
|---|---|
| Clone Names | 90625257 |
| Gene ID | 29128 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase UHRF1, 632-, Inverted CCAAT box-binding protein of 90 kDa, Nuclear protein 95, Nuclear zinc finger protein Np95, HuNp95, hNp95, RING finger protein 106, Transcription factor ICBP90, Ubiquitin-like PHD and RING finger domain-containing protein 1, hUHRF1, Ubiquitin-like-containing PHD and RING finger domains protein 1, UHRF1, ICBP90, NP95, RNF106 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8846c was selected from the Center region of human UHRF1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | UHRF1 |
|---|---|
| Synonyms | ICBP90, NP95, RNF106 |
| 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. Plays a role in DNA repair by cooperating with UHRF2 to ensure recruitment of FANCD2 to interstrand cross-links (ICLs) leading to FANCD2 activation. Acts as a critical player of proper spindle architecture by catalyzing the 'Lys-63'-linked ubiquitination of KIF11, thereby controlling KIF11 localization on the spindle (PubMed:37728657). |
| Cellular Location | Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:10646863, ECO:0000269|PubMed:17673620, ECO:0000269|PubMed:17967883, ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:21777816, ECO:0000269|PubMed:30335751} Note=Associated, through the YDG domain (also called SRA domain), with replicating DNA from early to late S phase, including at replicating pericentric heterochromatin (By similarity). Also localizes to euchromatic regions. In non-S-phase cells, homogenously distributed through the nucleus (By similarity). {ECO:0000250|UniProtKB:Q8VDF2} |
| Tissue Location | Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer. |
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Provided below are standard protocols that you may find useful for product applications.
Background
UHRF1 is a member of a subfamily of RING-finger type E3 ubiquitin ligases. The protein binds to specific DNA sequences, and recruits a histone acetylase to regulate gene expression. 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.
References
Achour,M.,et.al., Biochem. Biophys. Res. Commun. 390 (3), 523-528 (2009)
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