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Anti-NIRF Antibody Picoband™ (monoclonal, 6B5)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IF, ICC, FC |
|---|---|
| Primary Accession | Q96PU4 |
| Host | Mouse |
| Isotype | Mouse IgG2b |
| Reactivity | Rat, Human |
| Clonality | Monoclonal |
| Format | Lyophilized |
| Description | Anti-NIRF Antibody Picoband™ (monoclonal, 6B5) . Tested in Flow Cytometry, IF, ICC, WB applications. This antibody reacts with Human, Rat. |
| Reconstitution | Adding 0.2 ml of distilled water will yield a concentration of 500 µg/ml. |
| Gene ID | 115426 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase UHRF2, 2.3.2.27, Np95/ICBP90-like RING finger protein, Np95-like RING finger protein, Nuclear protein 97, Nuclear zinc finger protein Np97, RING finger protein 107, RING-type E3 ubiquitin transferase UHRF2, Ubiquitin-like PHD and RING finger domain-containing protein 2, Ubiquitin-like-containing PHD and RING finger domains protein 2, UHRF2, NIRF, RNF107 |
| Calculated MW | 90 kDa |
| Application Details | Western blot, 0.25-0.5 µg/ml, Human Immunocytochemistry/Immunofluorescence, 5 µg/ml, Human Flow Cytometry, 1-3 µg/1x10^6 cells, Human, Rat |
| Contents | Each vial contains 4 mg Trehalose, 0.9 mg NaCl and 0.2 mg Na2HPO4. |
| Clone Names | Clone: 6B5 |
| Immunogen | A synthetic peptide corresponding to a sequence at the N-terminus of human NIRF, identical to the related mouse and rat sequences. |
| Purification | Immunogen affinity purified. |
| Storage | At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing. |
| Name | UHRF2 |
|---|---|
| Synonyms | NIRF, RNF107 |
| Function | E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair (PubMed:15178429, PubMed:23404503, PubMed:27743347, PubMed:29506131). Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them (PubMed:24813944, PubMed:27129234). This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (By similarity). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thereby inducing G1 arrest (PubMed:15178429, PubMed:15361834, PubMed:21952639). Also ubiquitinates PCNP leading to its degradation by the proteasome (PubMed:12176013, PubMed:14741369). Plays an active role in DNA damage repair by ubiquitinating p21/CDKN1A leading to its proteasomal degradation (PubMed:29923055). Also promotes DNA repair by acting as an interstrand cross-links (ICLs) sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent activation (PubMed:30335751). Contributes to UV-induced DNA damage response by physically interacting with ATR in response to irradiation, thereby promoting ATR activation (PubMed:33848395). |
| Cellular Location | Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:12176013, ECO:0000269|PubMed:23404503, ECO:0000269|PubMed:27129234, ECO:0000269|PubMed:27743347, ECO:0000269|PubMed:29923055, ECO:0000269|PubMed:30335751}. Chromosome. Note=Enriched at genomic loci that are enriched for 5-hydroxymethylcytosine (5hmC) |
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Provided below are standard protocols that you may find useful for product applications.
Background
E3 ubiquitin-protein ligase UHRF2 is an enzyme that in humans is encoded by the UHRF2 gene. This gene encodes a nuclear protein which is involved in cell-cycle regulation. The encoded protein is a ubiquitin-ligase capable of ubiquinating PCNP (PEST-containing nuclear protein), and together they may play a role in tumorigenesis. The encoded protein contains an NIRF_N domain, a PHD finger, a set- and ring-associated (SRA) domain, and a RING finger domain and several of these domains have been shown to be essential for the regulation of cell proliferation. This protein may also have a role in intranuclear degradation of polyglutamine aggregates. Alternative splicing results in multiple transcript variants some of which are non-protein coding.
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