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DDX42 Blocking Peptide (N-Term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q86XP3 |
|---|---|
| Other Accession | Q810A7, Q5R7D1 |
| Gene ID | 11325 |
|---|---|
| Other Names | ATP-dependent RNA helicase DDX42, DEAD box protein 42, RNA helicase-like protein, RHELP, RNA helicase-related protein, RNAHP, SF3b DEAD box protein, Splicing factor 3B-associated 125 kDa protein, SF3b125, DDX42 |
| Target/Specificity | The synthetic peptide sequence is selected from aa 124-138 of HUMAN DDX42 |
| 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 | DDX42 {ECO:0000303|PubMed:16397294, ECO:0000312|HGNC:HGNC:18676} |
|---|---|
| Function | ATP-dependent RNA helicase that binds to partially double- stranded RNAs (dsRNAs) in order to unwind RNA secondary structures (PubMed:16397294). Unwinding is promoted in the presence of single- strand binding proteins (PubMed:16397294). Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein (PubMed:16397294). ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP- bound form of the protein triggers annealing of complementary RNA strands (PubMed:16397294). Required for assembly of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs: DDX42 associates transiently with the SF3B subcomplex of the 17S U2 SnRNP complex and is released after fulfilling its role in the assembly of 17S U2 SnRNP (PubMed:12234937, PubMed:36797247). Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis- stimulating activity of TP53BP2 (PubMed:19377511). Relocalizes TP53BP2 to the cytoplasm (PubMed:19377511). |
| Cellular Location | Cytoplasm. Nucleus |
| Tissue Location | Expressed in several cell lines (at protein level). Expressed in liver, lung, tonsil, thymus, muscle and pancreatic islets |
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
ATP-dependent RNA helicase. Binds to partially double- stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm.
References
Suk K.,et al.Biochim. Biophys. Acta 1501:63-69(2000).
Ikeda A.,et al.Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Zody M.C.,et al.Nature 440:1045-1049(2006).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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