RNase inhibitor (RI) is an acidic ~50 kDa cytoplasmic protein that has pI 4.7 and a high content of Leucine and Cysteinyl. RI can bind to RNase A superfamily members in a 1:1 stoichiometry, completely inhibiting their catalytic activity by steric occlusion the enzyme active site . The complex formed by RI and its target ribonuclease is the tightest of known biomolecular interactions.
Figure 1. Three-dimensional structures of RI and its complexes with ribonucleases. (A) Porcine RI with colors corresponding to exon-encoded modules. (B) Porcine RI·RNase A complex (C) Human RI·ANG complex .
The repeating structural units of RI possess a highly repetitive amino acid sequence that is rich in leucine residues. These leucine-rich repeats (LRRs) are present in a large family of proteins that characteristically display a large surface area to facilitate protein interactions. The unique structure and function of RI make it a core protein for the study of LRRs, as well as its widespread use as a laboratory reagent to eliminate ribonucleolytic activity .
|Recombinant||Expressed in E. coli|
|Molecular Weight||~50 kDa|
|Grade||For molecular biology|
|Form||Buffered aqueous solution|
|Shipped in||Dry ice|
|Storage Condition||Store at -20 °C. Please avoid freeze-thaw cycles.|
|RNAse/E.coli DNA Contamination||Not detected|
|Note||This product is for research use only.|
- cDNA synthesis
- In vitro inhibition of ribonucleases
- In vitro transcription/translation
- Enzymatic RNA labeling reaction
- Other applications important to RNA integrity
Since the SARS-CoV-2 pandemic, research into the detection and treatment of Coronavirus has never stopped. Alfa Chemistry is committed to providing customers with the RNase inhibitor used in the nucleic acid detection process to meet their various needs. If the product you are looking for is not in our catalog, please contact us. We will be happy to provide you with customized synthesis services.
- Kobe, B.; et al. Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease A. Journal of molecular biology. 1996, 264(5): 1028-1043.
- Dickson, K. A.; et al. Ribonuclease inhibitor: structure and function. Progress in nucleic acid research and molecular biology. 2005, 80: 349-374.
Our products and services are for research use only and cannot be used for any clinical purposes.