Human Recombinant MAGOH protein, His Tag (V2LY-0526-LY5419)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant MAGOH protein, His Tag consist of Amino Acid: 1-146 and predicts a molecular mass of 18 kDa.
Molecule Mass
18 kDa
Sequence
Amino Acid: 1-146
Species
Human

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

Purity
>90% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Liquid
Buffer
Sodium phosphate, NaCl, Imidazole, PMSF, DTT, Glycerol
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
mago-nashi homolog, proliferation-associated (Drosophila)
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).

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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