Aly Antibody (YA2079)
(Synonyms: ALYREF; ALY; BEF; THOC4; THO complex subunit 4; Tho4; Ally of AML-1 and LEF-1; Aly/REF export factor; Transcriptional coactivator Aly/REF; bZIP-enhancing factor BEF)
Based on 1 Customer Validation
Aly Antibody (YA2079) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Aly.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-F, IHC-P, ICC/IF, FC, IP
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
FC
FC: Flow Cytometry
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IP
IP: Immunoprecipitation
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|---|---|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:200-1:500 | 1:100-1:200 | 1:50-1:100 | 1:20-1:50 |
Product Details
Aly Antibody (YA2079) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Aly.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 27-35 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 27 kDa
Entrez Gene: 10189 Human ; 21681 Mouse ; 690585 Rat
SwissProt: Q86V81 Human ; O08583 Mouse ;
OMIM: 604171 Human
A synthetic peptide of human Aly
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Aly functions as an mRNA export adapter; component of the transcription/export (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. 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 via the TAP/NXF1 pathway. Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Plays a key role in mRNP recognition and mRNA packaging by bridging the mRNP-bound EJC and the TREX core complex. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway). 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. Involved in mRNA export of C5-methylcytosine (m5C)-containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling. Acts as a chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation. Involved in transcription elongation and genome stability; (Microbial infection) 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[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17].
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Subcellular Localization
Nucleus; Nucleus speckle; Cytoplasm
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Expression
Tissue_specificity:Expressed in a wide variety of cancer types -
Subunit
Homomultimer; predominantly hexamer when bound to EJC-RNA complex (PubMed:16314458, PubMed:37020021). Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex (THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7); in the complex interacts (via UAP56-binding motif) with DDX39B with low affinity but this interaction is likely stabilized by multimerization (PubMed:11979277, PubMed:12944400, PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:17984224, PubMed:18974867, PubMed:23826332, PubMed:37020021). TREX seems to have a dynamic structure involving ATP-dependent remodeling; in the complex interacts with THOC1, THOC2 and THOC5 (PubMed:19165146, PubMed:23222130, PubMed:37020021). Component of the ALYREF/THOC4-EJC-RNA complex; in the complex interacts (via the WXHD motif) with EIF4A3 and interacts (via the RRM domain) with MAGOH; these interactions are likely specific to RNA-bound EJC (PubMed:14730019, PubMed:16314458, PubMed:37020021). Bridges the THO-DDX39B and EJC-RNA complexes to form the TREX-EJC-RNA complex; this interaction is essential for mRNP recognition and mRNA packaging (PubMed:37020021). Identified in the spliceosome C complex (PubMed:11991638, PubMed:12176931). Found in a mRNP complex with UPF3A and UPF3B (PubMed:11546873). Interacts with RBM8A, RBM15B, NCBP1, LEF1, RUNX1, RNPS1, SRRM1, IWS1 and EXOSC1 (PubMed:11118221, PubMed:11707413, PubMed:12944400, PubMed:17190602, PubMed:17234882). Interacts with RBM15B (PubMed:19586903). Interacts with NXF1; the interaction is direct (PubMed:11675789, PubMed:11707413, PubMed:14730019, PubMed:18974867, PubMed:19165146, PubMed:19586903, PubMed:23826332). Interacts with IVNS1ABP (via BACK domain); the interaction is indirect and likely plays a role in mRNA nuclear export (PubMed:30538201)
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SwissProt ID
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Synonyms
ALYREF; ALY; BEF; THOC4; THO complex subunit 4; Tho4; Ally of AML-1 and LEF-1; Aly/REF export factor; Transcriptional coactivator Aly/REF; bZIP-enhancing factor BEF
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Research Field
Epigenetics and Nuclear Signaling
Documentation
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Data Sheet (264 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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User Guide for Antibodies (1077 KB)
[1]. Guo S, et al. Linking transcriptional elongation and messenger RNA export to metastatic breast cancers. Cancer Res. 2005 Apr 15;65(8):3011-6. [Content Brief]
[2]. Masuda S, et al. Recruitment of the human TREX complex to mRNA during splicing. Genes Dev. 2005 Jul 1;19(13):1512-7. [Content Brief]
[3]. Cheng H, et al. Human mRNA export machinery recruited to the 5' end of mRNA. Cell. 2006 Dec 29;127(7):1389-400. [Content Brief]
[4]. Taniguchi I, et al. ATP-dependent recruitment of export factor Aly/REF onto intronless mRNAs by RNA helicase UAP56. Mol Cell Biol. 2008 Jan;28(2):601-8. [Content Brief]
[6]. Luo ML, et al. Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly. Nature. 2001 Oct 11;413(6856):644-7. [Content Brief]
[7]. Kataoka N, et al. Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex. EMBO J. 2001 Nov 15;20(22):6424-33. [Content Brief]
[8]. Strässer K, et al. TREX is a conserved complex coupling transcription with messenger RNA export. Nature. 2002 May 16;417(6886):304-8. [Content Brief]
[9]. Hautbergue GM, et al. Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP. Proc Natl Acad Sci U S A. 2008 Apr 1;105(13):5154-9. [Content Brief]
[10]. Domínguez-Sánchez MS, et al. Genome instability and transcription elongation impairment in human cells depleted of THO/TREX. PLoS Genet. 2011 Dec;7(12):e1002386. [Content Brief]
[11]. Viphakone N, et al. TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export. Nat Commun. 2012;3:1006. [Content Brief]
[12]. Chi B, et al. Aly and THO are required for assembly of the human TREX complex and association of TREX components with the spliced mRNA. Nucleic Acids Res. 2013 Jan;41(2):1294-306. [Content Brief]
[13]. Viphakone N, et al. Luzp4 defines a new mRNA export pathway in cancer cells. Nucleic Acids Res. 2015 Feb 27;43(4):2353-66. [Content Brief]
[14]. Katahira J, et al. Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA. EMBO J. 2009 Mar 4;28(5):556-67. [Content Brief]
[15]. Yang X, et al. 5-methylcytosine promotes mRNA export - NSUN2 as the methyltransferase and ALYREF as an m(5)C reader. Cell Res. 2017 May;27(5):606-625. [Content Brief]
[16]. Virbasius CM, et al. A human nuclear-localized chaperone that regulates dimerization, DNA binding, and transcriptional activity of bZIP proteins. Mol Cell. 1999 Aug;4(2):219-28. [Content Brief]
[17]. Chen IH, et al. ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway. J Virol. 2002 Dec;76(24):12877-89. [Content Brief]
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