| Form | Liquid |
|---|---|
| Host Species | Human |
| Clonality | Monoclonal |
| Isotype | VHH-Fc |
| Purity | >95% as determined by SDS-PAGE. |
| Purification | Protein A/G purified from cell culture supernatant. |
| Endotoxin Level | Please contact with the lab for this information. |
| Applications | ELISA |
| Species Reactivity | Human |
| Target | M-phase phosphoprotein 8, MPHOSPH8, MPP8, Twa3, Two hybrid-associated protein 3 with RanBPM |
| Storage Buffer | 0.01M PBS pH 7.4 |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Product Usage Information | ELISA: 1:2000-1:20000 |
| Accession Number | Q99549 |
| Background | M-phase phosphoprotein 8 (MPP8) is a ~97 kDa protein. Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression. As part of the HUSH complex, promotes epigenetic repression of mobile genetic elements, such as retroviruses and transposable elements: the HUSH complex mainly represses LINE-1 (L1) retrotransposons that are still capable of transposition. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression. MPHOSPH8 mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2, a chromatin remodeler that compacts chromatin. The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed. 1. Tchasovnikarova, IA. et al. (2015) Science (New York, N.Y.) 348, 1481-1485. PMID: 26022416 2. Tchasovnikarova, IA. et al. (2017) Nature genetics 49, 1035-1044. PMID: 28581500 3. Liu, N. et al. (2018) Nature 553, 228-232. PMID: 29211708 4. Zhu, Y. et al. (2018) Nature 564, 278-282. PMID: 30487602 5. Tunbak, H. et al. (2020) Nature communications 11, 5387. PMID: 33144593 6. Danac, JMC. et al. (2024) Molecular cell 84, 2870-2881.e5. PMID: 39013473 |
| Note | For research use only |
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