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THOC4 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q86V81 |
|---|---|
| Clone Names | 100525311 |
| Gene ID | 10189 |
|---|---|
| Other Names | THO complex subunit 4, Tho4, Ally of AML-1 and LEF-1, Aly/REF export factor, Transcriptional coactivator Aly/REF, bZIP-enhancing factor BEF, ALYREF, ALY, BEF, THOC4 |
| 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 | ALYREF |
|---|---|
| Synonyms | ALY, BEF, THOC4 |
| Function | Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway) (PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:11707413, PubMed:11675789, PubMed:11979277, PubMed:18364396, PubMed:22144908, PubMed:22893130, PubMed:23222130, PubMed:25662211). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm (PubMed:15833825, PubMed:15998806, PubMed:17190602). TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1 (PubMed:15833825, PubMed:15998806, PubMed:17190602). The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production; ALYREF/THOC4 mediates the recruitment of the TREX complex to the intronless viral mRNA (PubMed:18974867). Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC) (PubMed:15998806, PubMed:17984224). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim (PubMed:19165146). Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability (PubMed:12438613, PubMed:17984224). Involved in mRNA export of C5-methylcytosine (m5C)-containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo- cytoplasmic shuttling (PubMed:28418038). |
| Cellular Location | Nucleus. Nucleus speckle Cytoplasm Note=Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (PubMed:19324961) Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur (PubMed:23826332) |
| Tissue Location | Expressed in a wide variety of cancer types. |
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Provided below are standard protocols that you may find useful for product applications.
Background
THOC4 is a heat stable, nuclearprotein and functions as a molecular chaperone. It is thought toregulate dimerization, DNA binding, and transcriptional activity ofbasic region-leucine zipper (bZIP) proteins.
References
Corbin-Lickfett, K.A., et al. J. Virol. 84(5):2212-2222(2010)Souki, S.K., et al. J. Virol. 83(17):8970-8975(2009)Johnson, L.A., et al. J. Virol. 83(13):6335-6346(2009)Colgan, K.J., et al. J. Gen. Virol. 90 (PT 6), 1455-1460 (2009) :Katahira, J., et al. EMBO J. 28(5):556-567(2009)
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