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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human RPS8 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 21.80 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 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 | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Arg41-Lys208 |
Aliases /Synonyms | RPS8, Small ribosomal subunit protein eS8, 40S ribosomal protein S8 |
Reference | ARO-P10762 |
Note | For research use only. |
Recombinant Human RPS8 Protein, also known as ribosomal protein S8, is a protein that plays a crucial role in protein synthesis. It is a highly conserved protein found in both prokaryotes and eukaryotes, and has been extensively studied for its structure, activity, and potential applications.
The Recombinant Human RPS8 Protein is composed of 167 amino acids, with a molecular weight of approximately 19 kDa. It is a small subunit of the ribosome, and is responsible for binding to the messenger RNA (mRNA) during translation. The protein has a characteristic “S8” domain, which is highly conserved across different species.
Studies have shown that Recombinant Human RPS8 Protein has a unique structure, with two alpha helices and five beta strands arranged in a beta-barrel formation. This structure is essential for the protein’s function in binding to the ribosomal RNA (rRNA) and mRNA, and facilitating the assembly of the ribosome.
The primary function of Recombinant Human RPS8 Protein is to participate in the translation process, where it helps in the formation of the ribosome-mRNA complex. This complex is crucial for the accurate and efficient translation of genetic information into proteins.
In addition to its role in protein synthesis, Recombinant Human RPS8 Protein has also been found to have other activities. Studies have shown that it can interact with various proteins involved in cell growth and proliferation, suggesting its potential involvement in cell signaling pathways.
Moreover, Recombinant Human RPS8 Protein has been shown to have a role in the regulation of gene expression. It has been found to bind to specific regions of DNA, influencing the expression of certain genes. This activity highlights the diverse functions of this protein beyond its traditional role in translation.
The unique structure and activity of Recombinant Human RPS8 Protein make it a valuable tool in various scientific fields. One of its primary applications is in the study of protein synthesis and translation. Recombinant Human RPS8 Protein can be used in in vitro translation assays to investigate the mechanisms of protein synthesis and the role of different factors in this process.
Furthermore, Recombinant Human RPS8 Protein has potential applications in the development of new antibiotics. As it is highly conserved and essential for protein synthesis, targeting this protein could lead to the inhibition of bacterial growth and survival.
In the field of cancer research, Recombinant Human RPS8 Protein has been found to be overexpressed in certain types of cancer cells, making it a potential biomarker for cancer diagnosis and treatment. Additionally, its involvement in cell signaling pathways suggests its potential as a therapeutic target for cancer treatment.
In conclusion, Recombinant Human RPS8 Protein is a vital protein involved in protein synthesis and has diverse functions beyond its traditional role. Its unique structure and activity make it a valuable tool in various scientific fields, including protein synthesis studies, antibiotic development, and cancer research. Further research on this protein could lead to a better understanding of its functions and potential applications in the future.
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