RNF14 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- 产品详情
- 实验流程
- 背景知识
Application
| WB, E |
|---|---|
| Primary Accession | Q9UBS8 |
| Other Accession | NP_899646.1, NP_004281.1 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 53837 Da |
| Antigen Region | 336-364 aa |
| Gene ID | 9604 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase RNF14, 632-, Androgen receptor-associated protein 54, HFB30, RING finger protein 14, Triad2 protein, RNF14, ARA54 |
| Target/Specificity | This RNF14 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 336-364 amino acids from the C-terminal region of human RNF14. |
| Dilution | WB~~1:1000 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | RNF14 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | RNF14 {ECO:0000303|PubMed:36638793, ECO:0000312|HGNC:HGNC:10058} |
|---|---|
| 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, PubMed:37651229, PubMed:37951215, PubMed:37951216). Recruited to stalled ribosomes by the ribosome collision sensor GCN1 and mediates 'Lys-6'-linked ubiquitination of target proteins, leading to their degradation (PubMed:36638793, PubMed:37651229, PubMed:37951215, PubMed:37951216). Mediates ubiquitination of EEF1A1/eEF1A and ETF1/eRF1 translation factors on stalled ribosomes, leading to their degradation (PubMed:36638793, PubMed:37651229). Also catalyzes ubiquitination of ribosomal proteins RPL0, RPL1, RPL12, RPS13 and RPS17 (PubMed:36638793). Specifically required to resolve RNA-protein cross-links caused by reactive aldehydes, which trigger translation stress by stalling ribosomes: acts by catalying 'Lys-6'-linked ubiquitination of RNA-protein cross-links, leading to their removal by the ATP-dependent unfoldase VCP and subsequent degradation by the proteasome (PubMed:37951215, PubMed:37951216). Independently of its function in the response to stalled ribosomes, acts as a regulator of transcription in Wnt signaling via its interaction with TCF transcription factors (TCF7/TCF1, TCF7L1/TCF3 and TCF7L2/TCF4) (PubMed:23449499). May also play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription (PubMed:19345326). |
| Cellular Location | Cytoplasm. Nucleus |
| Tissue Location | Widely expressed.. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
The protein encoded by this gene contains a RING zinc finger, a motif known to be involved in protein-protein interactions. This protein interacts with androgen receptor (AR) and may function as a coactivator that induces AR target gene expression in prostate. A dominant negative mutant of this gene has been demonstrated to inhibit the AR-mediated growth of prostate cancer. This protein also interacts with class III ubiquitin-conjugating enzymes (E2s) and may act as a ubiquitin-ligase (E3) in the ubiquitination of certain nuclear proteins. Five alternatively spliced transcript variants encoding two distinct isoforms have been reported.
REFERENCES
Xu, K., et al. Cancer Cell 15(4):270-282(2009)
Lan, K.C., et al. Fertil. Steril. 89 (5 SUPPL), 1397-1405 (2008) :
Kikuchi, H., et al. Carcinogenesis 28(8):1752-1758(2007)
Yang, Z., et al. Endocrinology 148(3):1340-1349(2007)
Yang, Z., et al. Mol. Endocrinol. 21(2):343-358(2007)
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