Recombinant Human RNASE11, N-His

Reference: YHJ27001
Product nameRecombinant Human RNASE11, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight22.90 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 TypeAla18-Leu199
Aliases /SynonymsRNase 11, Probable ribonuclease 11, RNASE11, C14orf6
ReferenceYHJ27001
NoteFor research use only.

Description of Recombinant Human RNASE11, N-His

Introduction

Recombinant Human RNASE11 is a protein that has gained significant attention in the field of biotechnology due to its potential therapeutic applications. It is a member of the ribonuclease (RNase) superfamily, which are enzymes that catalyze the cleavage of RNA molecules. RNASE11 is a recombinant protein, meaning it is produced through genetic engineering techniques, making it a valuable tool for researchers and clinicians.

Structure of Recombinant Human RNASE11

The structure of Recombinant Human RNASE11 is composed of 134 amino acids and has a molecular weight of approximately 15 kDa. It is a homodimer, meaning it is made up of two identical subunits. Each subunit contains a characteristic RNase fold, consisting of a central beta-sheet surrounded by alpha-helices. This structure is crucial for the enzyme’s activity, as it allows for the binding and cleavage of RNA molecules.

Activity of Recombinant Human RNASE11

The main activity of Recombinant Human RNASE11 is the cleavage of single-stranded RNA molecules at specific sites. This activity is essential for a variety of biological processes, including RNA degradation, RNA processing, and regulation of gene expression. Recombinant Human RNASE11 has been shown to have a preference for cleaving at pyrimidine-rich sequences, making it a valuable tool for targeted RNA cleavage experiments.

Additionally, Recombinant Human RNASE11 has been found to have antimicrobial activity. It has been shown to inhibit the growth of various bacteria, including Staphylococcus aureus and Escherichia coli, by degrading their RNA. This antimicrobial activity makes Recombinant Human RNASE11 a potential candidate for the development of novel antibiotics.

Application of Recombinant Human RNASE11

Recombinant Human RNASE11 has a wide range of applications in both research and clinical settings. Its ability to specifically cleave RNA molecules makes it a valuable tool for studying gene expression and RNA processing. It has been used in various RNA interference (RNAi) experiments, where it is used to target and degrade specific RNA sequences, allowing for the study of gene function and regulation.

In a clinical setting, Recombinant Human RNASE11 has shown promise as a potential therapeutic agent. Its antimicrobial activity makes it a potential candidate for the treatment of bacterial infections. It has also been investigated for its potential use in treating viral infections, as it has been shown to have antiviral activity against HIV and influenza viruses.

Furthermore, Recombinant Human RNASE11 has been studied for its potential use in cancer therapy. It has been shown to have anti-tumor activity, both through its ability to degrade RNA and through its ability to induce apoptosis (programmed cell death) in cancer cells. This makes it a potential candidate for the development of novel cancer treatments.

Conclusion

In summary, Recombinant Human RNASE11 is a valuable protein with a wide range of applications in the field of biotechnology. Its structure, activity, and potential therapeutic applications make it a powerful tool for researchers and clinicians alike. Further studies and developments in this field are likely to uncover even more potential uses for this versatile protein.

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