癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
MAGOH Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | P61326 |
| Other Accession | Q27W02, P61327, Q566Y8, P50594, Q3ZBV3, Q9CQL1, Q96A72, Q0VC92, NP_002361.1 |
| Reactivity | Human |
| Predicted | Bovine, Mouse, Chicken, Zebrafish, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 17164 Da |
| Antigen Region | 46-74 aa |
| Gene ID | 4116 |
|---|---|
| Other Names | Protein mago nashi homolog, MAGOH, MAGOHA |
| Target/Specificity | This MAGOH antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 46-74 amino acids from the Central region of human MAGOH. |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | MAGOH Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MAGOH |
|---|---|
| Synonyms | MAGOHA |
| 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 pre-initiation 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. |
| Cellular Location | Nucleus. Nucleus speckle. Cytoplasm. Note=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). {ECO:0000250, ECO:0000250|UniProtKB:Q27W02, ECO:0000269|PubMed:19324961} |
| Tissue Location | Ubiquitous. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Drosophila that have mutations in their mago nashi (grandchildless) 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.
REFERENCES
Gehring, N.H., et al. Cell 137(3):536-548(2009)
Muromoto, R., et al. Biochem. Biophys. Res. Commun. 382(1):63-68(2009)
Diem, M.D., et al. Nat. Struct. Mol. Biol. 14(12):1173-1179(2007)
Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :
Andersen, C.B., et al. Science 313(5795):1968-1972(2006)
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