Recombinant Human RBM8A Protein, N-His-SUMO

Reference: YHK66701
Product nameRecombinant Human RBM8A Protein, N-His-SUMO
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight21.70 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeGly72-Arg152
Aliases /SynonymsRibonucleoprotein RBM8A, RNA-binding protein Y14, RNA-binding motif protein 8A, BOV-1, RBM8A, Binder of OVCA1-1, RBM8, RNA-binding protein 8A
ReferenceYHK66701
NoteFor research use only.

Description of Recombinant Human RBM8A Protein, N-His-SUMO

Introduction to Recombinant Human RBM8A Protein

Recombinant Human RBM8A Protein, also known as RNA binding motif protein 8A, is a protein that plays a crucial role in RNA processing and transport. It is encoded by the RBM8A gene and is highly conserved among different species, including humans.

Structure of Recombinant Human RBM8A Protein

The Recombinant Human RBM8A Protein is a 23-kilodalton protein that consists of 205 amino acids. It contains an RNA recognition motif (RRM) domain, which is responsible for its binding to RNA molecules. This domain is highly conserved among different RBM8A proteins in various species, indicating its importance in the protein’s function.

In addition to the RRM domain, Recombinant Human RBM8A Protein also contains a nuclear localization signal, which allows it to be transported into the nucleus, where it carries out its functions in RNA processing.

Activity of Recombinant Human RBM8A Protein

Recombinant Human RBM8A Protein is primarily involved in the processing and transport of RNA molecules. It is a component of the exon junction complex (EJC), which is formed during pre-mRNA splicing. The EJC plays a crucial role in mRNA localization, stability, and translation.

RBM8A binds to RNA molecules through its RRM domain and helps in the recruitment of other EJC components, such as MAGOH and EIF4A3. This complex then associates with the mRNA and travels with it to the cytoplasm, where it plays a role in regulating its translation.

Furthermore, Recombinant Human RBM8A Protein also plays a role in nonsense-mediated mRNA decay (NMD), a cellular process that targets and degrades abnormal or erroneous mRNA molecules. It does so by interacting with UPF1, a key protein involved in NMD, and aiding in the recognition of premature stop codons in mRNA molecules.

Application of Recombinant Human RBM8A Protein

The crucial role of Recombinant Human RBM8A Protein in RNA processing and transport makes it a valuable tool in various research areas. One of its main applications is in studying the mechanisms of pre-mRNA splicing and mRNA localization. By using recombinant RBM8A protein, researchers can manipulate its levels and observe the effects on RNA processing and transport, providing insights into these essential cellular processes.

In addition, Recombinant Human RBM8A Protein has also been used in studies related to NMD. By overexpressing or silencing the protein, researchers can investigate its role in this process and its potential as a therapeutic target for diseases caused by NMD dysregulation, such as cystic fibrosis and Duchenne muscular dystrophy.

Furthermore, Recombinant Human RBM8A Protein has been used in the development of diagnostic tools for certain diseases. For example, it has been shown to be a potential biomarker for ovarian cancer, making it a promising candidate for early detection and monitoring of this disease.

Conclusion

In summary, Recombinant Human RBM8A Protein is a crucial component in RNA processing and transport. Its structure, activity, and applications make it a valuable tool in various research areas, including pre-mRNA splicing, mRNA localization, NMD, and disease diagnostics. Further studies on this protein may provide a better understanding of its role in these processes and its potential as a therapeutic target.

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