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OTUD1 Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q5VV17 |
|---|---|
| Clone Names | 100126027 |
| Gene ID | 220213 |
|---|---|
| Other Names | OTU domain-containing protein 1, DUBA-7, OTUD1, DUBA7, OTDC1 |
| 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 | OTUD1 {ECO:0000303|PubMed:23827681, ECO:0000312|HGNC:HGNC:27346} |
|---|---|
| Function | Deubiquitinating enzyme that specifically hydrolyzes 'Lys- 63'-linked polyubiquitin to monoubiquitin (PubMed:23827681). Required for the stability and translation of a subset mRNAs with a high abundance of rare codons by mediating deubiquitination of 40S ribosomal protein RPS10/eS10, thereby antagonizing ZNF598-mediated 40S ubiquitination (PubMed:36445135). The abundance of rare codons in mRNAs can limit the translation rate and can lead to ribosome collisions that trigger activation of ribosome quality control (RQC) pathway by ZNF598 (PubMed:36445135). OTUD1-mediated deubiquitination prevents activation of the RQC and subsequent dissociation of ribosomes and stimulates formation of polysomes and translation (PubMed:36445135). |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Deubiquitinating enzymes (DUBs; see MIM 603478) areproteases that specifically cleave ubiquitin (MIM 191339) linkages,negating the action of ubiquitin ligases. DUBA7 belongs to a DUBsubfamily characterized by an ovarian tumor (OTU) domain.[suppliedby OMIM].
References
Franke, A., et al. Gastroenterology 135(4):1207-1215(2008)Kayagaki, N., et al. Science 318(5856):1628-1632(2007)Deloukas, P., et al. Nature 429(6990):375-381(2004)Makarova, K.S., et al. Trends Biochem. Sci. 25(2):50-52(2000)
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