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Mouse Anti-MAGOH Recombinant Antibody (CBFYM-1344) (CBMAB-M1503-FY)


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Summary

Host Animal
Mouse
Specificity
Mouse, Rat, Human
Clone
CBFYM-1344
Application
WB, IP, IF, ELISA

Basic Information

Specificity
Mouse, Rat, Human
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
mago-nashi homolog, proliferation-associated (Drosophila)
Introduction
Drosophila that have mutations in their mago nashi gene produce progeny with defects in germplasm assembly and germline development. This gene encodes the mammalian mago nashi homolog. In mammals, mRNA expression is not limited to the germ plasm, but is expressed ubiquitously in adult tissues and can be induced by serum stimulation of quiescent fibroblasts.
Entrez Gene ID
Human4116
Mouse17149
Rat298385
UniProt ID
HumanP61326
MouseP61327
RatQ27W02
Alternative Names
Mago Homolog, Exon Junction Complex Core Component; MAGOHA; Mago-Nashi (Drosophila) Homolog, Proliferation-Associated; Mago-Nashi Homolog, Proliferation-Associated (Drosophila); Mago-Nashi Homolog, Proliferation-Associated; Protein Mago Nashi Homolog; MAGOH1
Function
Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638).
Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense-mediated decay (NMD) pathway (PubMed:23917022).
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). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. 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.
Biological Process
mRNA export from nucleus1 PublicationIC:ComplexPortal
mRNA splicing, via spliceosome1 PublicationIC:UniProtKB
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decayManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of alternative mRNA splicing, via spliceosomeManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of mRNA processingManual Assertion Based On ExperimentIDA:ComplexPortal
Regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decayManual Assertion Based On ExperimentIDA:ComplexPortal
Regulation of translationIEA:UniProtKB-KW
RNA splicingManual Assertion Based On ExperimentIBA:GO_Central
Cellular Location
Nucleus
Nucleus speckle
Cytoplasm
Detected in granule-like structures in the dendroplasm (By similarity).
Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (PubMed:19324961).
More Infomation

Xiao, F., Long, Z., Guo, Y., Zhu, H., Zhang, Z., Xiao, Y., ... & Guo, H. (2023). MAGOH is correlated with poor prognosis and is essential for cell proliferation in lower-grade glioma. Aging (Albany NY), 15(12), 5713.

Mitra, R., Rehman, A., Singh, K. K., & Jaganathan, B. G. (2023). Multifaceted roles of MAGOH Proteins. Molecular Biology Reports, 50(2), 1931-1941.

Barreiro, R. A., Guardia, G. D., Meliso, F. M., Lei, X., Li, W. Q., Savio, A., ... & Galante, P. A. (2023). The paralogues MAGOH and MAGOHB are oncogenic factors in high-grade gliomas and safeguard the splicing of cell division and cell cycle genes. RNA biology, 20(1), 311-322.

Soederberg, A., Meißgeier, T., Bosserhoff, A. K., & Linck-Paulus, L. (2022). MAGOH and MAGOHB Knockdown in Melanoma Cells Decreases Nonsense-Mediated Decay Activity and Promotes Apoptosis via Upregulation of GADD45A. Cells, 11(23), 3859.

Fernandez-Abascal, J., Wang, L., Graziano, B., Johnson, C. K., & Bianchi, L. (2022). Exon-dependent transcriptional adaptation by exon-junction complex proteins Y14/RNP-4 and MAGOH/MAG-1 in Caenorhabditis elegans. PLoS genetics, 18(10), e1010488.

Zhou, Y., Li, Z., Wu, X., Tou, L., Zheng, J., & Zhou, D. (2020). MAGOH/MAGOHB inhibits the tumorigenesis of gastric cancer via inactivation of b-RAF/MEK/ERK signaling. OncoTargets and therapy, 12723-12735.

Gangras, P., Gallagher, T. L., Parthun, M. A., Yi, Z., Patton, R. D., Tietz, K. T., ... & Singh, G. (2020). Zebrafish rbm8a and magoh mutants reveal EJC developmental functions and new 3′ UTR intron-containing NMD targets. PLoS genetics, 16(6), e1008830.

Sheehan, C. J., McMahon, J. J., Serdar, L. D., & Silver, D. L. (2020). Dosage-dependent requirements of Magoh for cortical interneuron generation and survival. Development, 147(1), dev182295.

Ma, Q., Tatsuno, T., Nakamura, Y., & Ishigaki, Y. (2019). The stability of Magoh and Y14 depends on their heterodimer formation and nuclear localization. Biochemical and biophysical research communications, 511(3), 631-636.

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

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