4°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)
Brand
ProteoGenix
Host species
Escherichia coli (E.coli)
Fragment Type
Glu557~Lys646
Protein Accession
EAW78268.1
NCBI Reference
WP_001583586
Aliases /Synonyms
EIF-4G1, EIF4F, EIF4G, EIF4GI, P220, PARK18
Reference
PX-P2069
Note
For research use only
Description of Human eIF4G Recombinant Protein
The Structure of Human eIF4G Recombinant Protein
Human eIF4G (eukaryotic initiation factor 4G) is a large multidomain protein that plays a crucial role in the initiation of protein synthesis in eukaryotic cells. It is a key component of the eIF4F complex, which is responsible for recruiting the 40S ribosomal subunit to the 5′ end of mRNA, allowing for the initiation of translation. The eIF4G protein is composed of three major domains: the N-terminal domain, the central domain, and the C-terminal domain.
The N-terminal domain of eIF4G is responsible for binding to eIF4E, the cap-binding protein, and forming the eIF4F complex. This domain also contains binding sites for other eIF4 proteins, such as eIF4A and eIF4B, which are involved in unwinding the mRNA secondary structure. The central domain of eIF4G contains multiple HEAT repeats, which are structural motifs that facilitate protein-protein interactions. This domain is responsible for binding to eIF3, another key component of the translation initiation complex. The C-terminal domain of eIF4G contains a binding site for the poly(A)-binding protein (PABP), which is responsible for recruiting the 60S ribosomal subunit to the mRNA.
The Activity of this protein
As mentioned earlier, eIF4G plays a crucial role in the initiation of protein synthesis. It is involved in multiple steps of this process, including binding to the mRNA cap, recruiting the ribosome, and promoting mRNA unwinding. The eIF4G protein also interacts with other translation initiation factors, such as eIF3 and PABP, to facilitate the formation of the translation initiation complex.
One of the key activities of eIF4G is its ability to bind to eIF4E and form the eIF4F complex. This interaction is essential for the recruitment of the 40S ribosomal subunit to the mRNA, as eIF4E is responsible for recognizing and binding to the mRNA cap structure. Additionally, the central domain of eIF4G plays a crucial role in promoting the unwinding of mRNA secondary structures, allowing for efficient translation initiation.
Another important activity of eIF4G is its interaction with eIF3. This interaction is crucial for the assembly of the 43S pre-initiation complex, which consists of the 40S ribosomal subunit, eIF3, and other initiation factors. The eIF4G-eIF3 interaction also helps to position the mRNA in the correct orientation for translation initiation.
The Application of Human eIF4G Recombinant Protein
Given its crucial role in protein synthesis, eIF4G has been identified as a potential drug target for various diseases. Dysregulation of translation initiation has been linked to several diseases, including cancer, viral infections, and neurological disorders. In cancer, for example, overexpression of eIF4G has been observed in many types of tumors, and targeting eIF4G has been shown to inhibit tumor growth. This makes eIF4G an attractive target for the development of anticancer therapies.
In addition to its potential as a drug target, eIF4G recombinant protein has also been used in various research applications. It can be used to study the mechanisms of translation initiation and its role in various diseases. Recombinant eIF4G can also be used in in vitro translation assays to investigate the effects of different factors on translation efficiency.
In conclusion, Human eIF4G recombinant protein is a crucial component of the translation initiation complex, with a well-defined structure and multiple activities that are essential for efficient protein synthesis. Its potential as a drug target and its applications in research make it a valuable protein for further study.
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