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RNF10 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q8N5U6 |
|---|---|
| Clone Names | 110617142 |
| Gene ID | 9921 |
|---|---|
| Other Names | RING finger protein 10, RNF10, KIAA0262, RIE2 |
| 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 | RNF10 {ECO:0000303|PubMed:10697961, ECO:0000312|HGNC:HGNC:10055} |
|---|---|
| Function | E3 ubiquitin-protein ligase that catalyzes monoubiquitination of 40S ribosomal proteins RPS2/us5 and RPS3/us3 in response to ribosome stalling (PubMed:34348161, PubMed:34469731). Part of a ribosome quality control that takes place when ribosomes have stalled during translation initiation (iRQC): RNF10 acts by mediating monoubiquitination of RPS2/us5 and RPS3/us3, promoting their degradation by the proteasome (PubMed:34348161, PubMed:34469731). Also promotes ubiquitination of 40S ribosomal proteins in response to ribosome stalling during translation elongation (PubMed:34348161). The action of RNF10 in iRQC is counteracted by USP10 (PubMed:34469731). May also act as a transcriptional factor involved in the regulation of MAG (Myelin- associated glycoprotein) expression (By similarity). Acts as a regulator of Schwann cell differentiation and myelination (By similarity). |
| Cellular Location | Cytoplasm. Nucleus {ECO:0000250|UniProtKB:Q5XI59} |
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene contains a ring fingermotif, which is known to be involved in protein-proteininteractions. The specific function of this protein has not yetbeen determined. EST data suggests the existence of multiplealternatively spliced transcript variants, however, their fulllength nature is not known.
References
Hoshikawa, S., et al. PLoS ONE 3 (10), E3464 (2008) :Stelzl, U., et al. Cell 122(6):957-968(2005)Lin, J., et al. Mol. Cell. Biochem. 275 (1-2), 75-84 (2005) :Seki, N., et al. J. Hum. Genet. 45(1):38-42(2000)
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