Recombinant Human RNASE13, N-His

The Structure and Activity of Recombinant Human RNASE13

Recombinant human RNASE13 is a type of protein that is produced through genetic engineering techniques. It is a member of the ribonuclease (RNase) family, which are enzymes that play a crucial role in the breakdown of RNA molecules. RNASE13 is found in humans and is encoded by the RNASE13 gene located on chromosome 14. This protein has been extensively studied due to its potential therapeutic applications in various diseases.

Structure of Recombinant Human RNASE13

The recombinant human RNASE13 protein is composed of 124 amino acids and has a molecular weight of approximately 14 kDa. It has a compact structure with a three-dimensional conformation that is stabilized by four disulfide bonds. The protein has a characteristic β-sheet structure, with six β-strands connected by five loops. This structure is essential for the enzyme’s catalytic activity and stability.

The active site of recombinant human RNASE13 is located in a cleft between two loops, known as the “catalytic cleft.” This cleft contains amino acid residues that are responsible for the enzyme’s catalytic activity. The active site also has a histidine residue that plays a crucial role in the cleavage of RNA molecules.

Activity of Recombinant Human RNASE13

The main function of recombinant human RNASE13 is to cleave single-stranded RNA molecules, resulting in the formation of smaller fragments. This activity is essential for various biological processes, such as the degradation of RNA from viruses and the regulation of gene expression. The enzyme’s activity is highly specific, as it only cleaves RNA molecules and does not affect DNA or proteins.

The catalytic activity of recombinant human RNASE13 is dependent on various factors, including pH, temperature, and the presence of divalent cations such as magnesium and calcium. The optimal pH for the enzyme’s activity is between 7.0-8.0, and it is most active at temperatures ranging from 37-55°C. The presence of divalent cations is crucial for maintaining the enzyme’s stability and enhancing its catalytic activity.

Application of Recombinant Human RNASE13

Recombinant human RNASE13 has shown potential therapeutic applications in various diseases, including cancer, viral infections, and autoimmune disorders. The enzyme’s ability to cleave RNA molecules makes it a promising candidate for cancer treatment, as it can target and destroy cancer cells by disrupting their protein synthesis. It has also been shown to have antiviral activity, making it a potential treatment for viral infections such as influenza and HIV.

In addition to its therapeutic applications, recombinant human RNASE13 has also been used in research as a tool for studying RNA molecules. Its specific activity and stability make it a valuable tool for RNA analysis, such as RNA sequencing and RNA structure determination.

Conclusion

Recombinant human RNASE13 is a compact protein with a specific structure and catalytic activity. Its ability to cleave RNA molecules has potential therapeutic applications in various diseases and has also been used as a research tool. The recombinant protein has shown promising results in preclinical studies, and further research is being conducted to explore its full potential as a therapeutic agent.

Keywords: recombinant protein, antigen, RNASE13, ribonuclease, structure, activity, application, therapeutic, research, RNA molecules.

ProteoGenix catalogue number ARO-P13310. For research use only.

Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 13.67 kDa; Fragment: Val20-His116; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..

Available configurations: 50ug, 100ug, 1mg.

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