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Rabbit Anti-EIF4A3 Recombinant Antibody (CBFYE-0701) (CBMAB-E1125-FY)

This product is rabbit antibody that recognizes EIF4A3. The antibody CBFYE-0701 can be used for immunoassay techniques such as: WB.
See all EIF4A3 antibodies

Summary

Host Animal
Rabbit
Specificity
Human
Clone
CBFYE-0701
Antibody Isotype
IgG
Application
WB

Basic Information

Immunogen
Synthetic peptide derived from Met316 residues of human eIF4A protein
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
EIF4A3
Introduction
This gene encodes a member of the DEAD box protein family. DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. The protein encoded by this gene is a nuclear matrix protein. Its amino acid sequence is highly similar to the amino acid sequences of the translation initiation factors eIF4AI and eIF4AII, two other members of the DEAD box protein family.
Entrez Gene ID
9775
UniProt ID
P38919
Alternative Names
Eukaryotic Translation Initiation Factor 4A3; Eukaryotic Initiation Factor 4A-Like NUK-34; DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 48; ATP-Dependent RNA Helicase EIF4A-3; ATP-Dependent RNA Helicase DDX48; Nuclear Matrix Protein 265; DEAD Box Protein 48; EIF-4A-III; EIF4A-III; HNMP 265; NMP 265; DDX48; Eukaryotic Translation Initiation Factor 4A, Isoform 3
Research Area
ATP-dependent RNA helicase (PubMed:16170325).

Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:22961380, PubMed:28502770, PubMed:28076346, PubMed:29301961).

Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs (PubMed:16209946, PubMed:16170325, PubMed:16314458, PubMed:16923391, PubMed:16931718, PubMed:19033377, PubMed:20479275).

The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly (PubMed:22203037).

Involved in craniofacial development (PubMed:24360810).
Biological Process
Associative learning Source: Ensembl
Cellular response to brain-derived neurotrophic factor stimulus Source: Ensembl
Cellular response to selenite ion Source: Ensembl
Embryonic cranial skeleton morphogenesis Source: UniProtKB
Exploration behavior Source: Ensembl
mRNA splicing, via spliceosome Source: UniProtKB
mRNA transport Source: UniProtKB-KW
Negative regulation of excitatory postsynaptic potential Source: Ensembl
Negative regulation of selenocysteine incorporation Source: Ensembl
Negative regulation of selenocysteine insertion sequence binding Source: Ensembl
Negative regulation of translation Source: HGNC-UCL
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
Positive regulation of translation Source: UniProtKB
Regulation of translation at postsynapse, modulating synaptic transmission Source: Ensembl
Response to organic cyclic compound Source: Ensembl
rRNA processing Source: UniProtKB-KW
Cellular Location
Nucleus; Nucleus speckle; Cytoplasm. Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments of neurons. Colocalizes with STAU1 and FMR1 in dendrites (By similarity).
Involvement in disease
Richieri-Costa-Pereira syndrome (RCPS):
The disease is caused by variants affecting the gene represented in this entry. EIF4A3 mutations resulting in Richieri-Costa-Pereira syndrome include a repeat expansion of 18 or 20 nucleotides in the 5' untranslated region. Affected individuals have 14 to 16 repeats, while healthy individuals have 3 to 12 repeats (PubMed:24360810). A syndrome characterized by a unique pattern of anomalies consisting of microstomia, micrognathia, abnormal fusion of mandible, cleft palate/Robin sequence, absence of central lower incisors, minor ears anomalies, hypoplastic first ray, abnormal tibiae, hypoplastic halluces, and clubfeet. Learning disability is also a common finding.

Wang, X., Song, H., Fang, L., & Wu, T. (2022). EIF4A3-mediated circPRKCI expression promotes triple-negative breast cancer progression by regulating WBP2 and PI3K/AKT signaling pathway. Cell death discovery, 8(1), 1-14.

Sakellariou, D., Tiberti, M., Kleiber, T. H., Blazquez, L., López, A. R., Abildgaard, M. H., ... & Frankel, L. B. (2021). eIF4A3 regulates the TFEB-mediated transcriptional response via GSK3B to control autophagy. Cell Death & Differentiation, 28(12), 3344-3356.

Yu, F., Zhang, Y., Wang, Z., Gong, W., & Zhang, C. (2021). Hsa_circ_0030042 regulates abnormal autophagy and protects atherosclerotic plaque stability by targeting eIF4A3. Theranostics, 11(11), 5404.

He, Q., Tao, L., Xu, H., Xie, X., & Cheng, S. (2021). Circ_0072995 Promotes Proliferation and Invasion via Regulating miR-1253/EIF4A3 Signaling in HCC. Cancer Management and Research, 13, 5981.

Kanellis, D. C., Espinoza, J. A., Zisi, A., Sakkas, E., Bartkova, J., Katsori, A. M., ... & Bartek, J. (2021). The exon-junction complex helicase eIF4A3 controls cell fate via coordinated regulation of ribosome biogenesis and translational output. Science advances, 7(32), eabf7561.

Wei, Y., Lu, C., Zhou, P., Zhao, L., Lyu, X., Yin, J., ... & You, Y. (2021). EIF4A3-induced circular RNA ASAP1 promotes tumorigenesis and temozolomide resistance of glioblastoma via NRAS/MEK1/ERK1–2 signaling. Neuro-oncology, 23(4), 611-624.

Mao, S., Zhang, W., Yang, F., Guo, Y., Wang, H., Wu, Y., ... & Yao, X. (2021). Hsa_circ_0004296 inhibits metastasis of prostate cancer by interacting with EIF4A3 to prevent nuclear export of ETS1 mRNA. Journal of Experimental & Clinical Cancer Research, 40(1), 1-17.

Wang, X., Chen, M., & Fang, L. (2021). hsa_circ_0068631 promotes breast cancer progression through c-Myc by binding to EIF4A3. Molecular Therapy-Nucleic Acids, 26, 122-134.

Zheng, X., Huang, M., Xing, L., Yang, R., Wang, X., Jiang, R., ... & Chen, J. (2020). The circRNA circSEPT9 mediated by E2F1 and EIF4A3 facilitates the carcinogenesis and development of triple-negative breast cancer. Molecular cancer, 19(1), 1-22.

Wang, R., Zhang, S., Chen, X., Li, N., Li, J., Jia, R., ... & Liang, H. (2018). EIF4A3-induced circular RNA MMP9 (circMMP9) acts as a sponge of miR-124 and promotes glioblastoma multiforme cell tumorigenesis. Molecular cancer, 17(1), 1-12.

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For research use only. Not intended for any clinical use.

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