REN Human, sf9
Description
REN is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Renin is an aspartic protease enzyme that plays a crucial role in the renin-angiotensin-aldosterone system (RAAS), which regulates blood pressure and fluid balance in the body. The recombinant form of human renin expressed in Sf-9 insect cells, known as Renin (Human Recombinant, sf9), has been extensively studied for its potential applications in medical research and drug development.
The expression of recombinant human renin in Sf-9 cells involves the use of a baculovirus expression system. Sf-9 cells, derived from the fall armyworm Spodoptera frugiperda, are commonly used for the production of recombinant proteins due to their high expression levels and ability to perform post-translational modifications similar to those in mammalian cells .
In this system, the gene encoding human renin is inserted into the baculovirus genome, which is then used to infect Sf-9 cells. The infected cells produce active recombinant human renin in the late stages of cultivation. This method allows for the production of large quantities of renin with high purity and activity .
The purification of recombinant human renin from Sf-9 cells typically involves multiple chromatography steps. After five days of culture, the renin is purified using column chromatography techniques. The process yields a significant amount of pure renin, which can then be characterized for its biochemical properties .
Characterization studies have shown that the recombinant renin produced in Sf-9 cells exhibits similar binding and catalytic properties to native human renin. This makes it a valuable tool for studying the enzyme’s structure and function, as well as for screening potential renin inhibitors .
Renin inhibitors have been a target for the development of novel treatments for hypertension and related cardiovascular diseases. The availability of recombinant human renin has facilitated the design and testing of these inhibitors. X-ray crystallographic studies, for example, have used recombinant renin to obtain high-resolution diffraction data, aiding in the development of more effective renin inhibitors .
Additionally, the recombinant enzyme is used in various biochemical assays to study the RAAS pathway and its role in disease. The ability to produce large quantities of active renin has also enabled researchers to explore its potential therapeutic applications more thoroughly.
