RNF25 Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P |
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Primary Accession | Q96BH1 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 51kDa |
Dilution | IHC-P (10 µg/ml), WB (1:500-1:3000), |
Gene ID | 64320 |
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Other Names | E3 ubiquitin-protein ligase RNF25, 6.3.2.-, RING finger protein 25, RNF25 |
Target/Specificity | Human RNF25. |
Reconstitution & Storage | Aliquot and store at -20°C. Minimize freezing and thawing. |
Precautions | RNF25 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | RNF25 {ECO:0000303|PubMed:36638793, ECO:0000312|HGNC:HGNC:14662} |
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Function | E3 ubiquitin-protein ligase that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (PubMed:36638793). Catalyzes ubiquitination of RPS27A in response to ribosome collisions, promoting activation of RNF14 (PubMed:36638793). RNF25 catalyzes ubiquitination of other ribosomal proteins on stalled ribosomes, such as RPL0, RPL1, RPL12, RPS13 and RPS17 (PubMed:36638793). Also involved in ubiquitination and degradation of stalled ETF1/eRF1 (PubMed:36638793). Independently of its function in the response to stalled ribosomes, mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). May also stimulate transcription mediated by NF-kappa-B via its interaction with RELA/p65 (PubMed:12748188). |
Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:Q7SXJ6}. |
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Provided below are standard protocols that you may find useful for product applications.
Background
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). Stimulates transcription mediated by NF-kappa-B.
References
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Suzuki Y.,et al.Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
Hillier L.W.,et al.Nature 434:724-731(2005).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Asamitsu K.,et al.J. Biol. Chem. 278:26879-26887(2003).
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