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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human RNASE13, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 13.67 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 | Val20-His116 |
Aliases /Synonyms | RNASE13, Probable inactive ribonuclease-like protein 13 |
Reference | ARO-P13310 |
Note | For research use only. |
Recombinant Human RNASE13, also known as Ribonuclease 13, is a recombinant protein that has been produced through genetic engineering techniques. It is a member of the ribonuclease A superfamily and plays a crucial role in various physiological processes. In this article, we will discuss the structure, activity, and applications of Recombinant Human RNASE13 in detail.
Recombinant Human RNASE13 is a small protein consisting of 124 amino acids with a molecular weight of 13.7 kDa. It is composed of a single polypeptide chain with four disulfide bonds that stabilize its three-dimensional structure. The protein has a unique tertiary structure with a characteristic alpha-helical fold and a beta-sheet. The active site of RNASE13 is located in a cleft formed by two loops, known as the S-peptide and S-protein, which are essential for its catalytic activity.
Recombinant Human RNASE13 is a potent endoribonuclease, which means it can cleave RNA molecules at specific sites. It has a preference for single-stranded RNA and hydrolyzes the phosphodiester bonds between the 5′-phosphate group and the 3′-hydroxyl group of RNA. This activity is essential for various physiological processes, such as RNA turnover, RNA processing, and mRNA degradation. Additionally, RNASE13 has also been shown to have antiviral and antibacterial properties, making it a crucial component of the innate immune system.
The unique structure and activity of Recombinant Human RNASE13 make it a valuable tool in various scientific fields. Here are some of its applications:
Recombinant Human RNASE13 can be produced in large quantities through genetic engineering techniques, making it a readily available protein for research purposes. Its small size and stability make it an ideal candidate for protein expression and purification studies.
RNASE13 has been identified as a potential antigen for diagnostic tests for various diseases. Antibodies against RNASE13 have been found in patients with autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus. These antibodies can be used as biomarkers for disease diagnosis and monitoring.
Studies have shown that Recombinant Human RNASE13 has potent antimicrobial activity against both bacteria and viruses. It has been shown to inhibit the growth of various pathogenic bacteria, including Staphylococcus aureus and Pseudomonas aeruginosa. It has also been found to have antiviral activity against HIV, influenza, and herpes simplex virus.
Due to its ability to cleave RNA, Recombinant Human RNASE13 has shown potential as a therapeutic agent for various diseases. It has been studied as a potential treatment for viral infections, cancer, and autoimmune diseases. Its small size and stability make it an attractive candidate for drug development.
Recombinant Human RNASE13 has been used as a research tool to study various biological processes, such as RNA metabolism and innate immunity. Its ability to cleave RNA at specific sites makes it a valuable tool for studying RNA structure and function.
In conclusion, Recombinant Human RNASE13 is a small but powerful protein with a unique structure and activity. Its role in various physiological processes and its potential applications in research and medicine make it a valuable tool in the scientific community. Further studies on this protein
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